메뉴 건너뛰기




Volumn 428, Issue 3, 2010, Pages 325-346

The cutting edge: Membrane-anchored serine protease activities in the pericellular microenvironment

Author keywords

Membrane serine protease; Pericellular proteolysis; Serine protease inhibitor; Type II transmembrane serine protease (TTSP)

Indexed keywords

PERICELLULAR PROTEOLYSIS; SERINE PROTEASE; SERINE PROTEASE INHIBITOR; TRANSMEMBRANES; TYPE II;

EID: 77954915960     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100046     Document Type: Review
Times cited : (126)

References (240)
  • 1
    • 70350757743 scopus 로고    scopus 로고
    • Matriptase-2 mutations in iron-refractory iron deficiency anemia patients provide new insights into protease activation mechanisms
    • Ramsay, A. J., Quesada, V., Sanchez, M., Garabaya, C., Sarda, M. P., Baiget, M., Remacha, A., Velasco, G. and Lopez-Otin, C. (2009) Matriptase-2 mutations in iron-refractory iron deficiency anemia patients provide new insights into protease activation mechanisms. Hum. Mol. Genet. 18, 3673-3683
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3673-3683
    • Ramsay, A.J.1    Quesada, V.2    Sanchez, M.3    Garabaya, C.4    Sarda, M.P.5    Baiget, M.6    Remacha, A.7    Velasco, G.8    Lopez-Otin, C.9
  • 2
    • 0005292810 scopus 로고
    • Role of proteolytic enzymes in biological regulation (a review)
    • Neurath, H. and Walsh, K. A. (1976) Role of proteolytic enzymes in biological regulation (a review). Proc. Natl. Acad. Sci. U.S.A. 73, 3825-3832
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 3825-3832
    • Neurath, H.1    Walsh, K.A.2
  • 3
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom, L. (2002) Serine protease mechanism and specificity. Chem. Rev. 102, 4501-4524
    • (2002) Chem. Rev. , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 4
    • 34147124434 scopus 로고    scopus 로고
    • Introduction: Serine peptidases and their clans
    • 2nd edn, Barrett, A. J., Rawlings, N. D. and Woessner, J. F., eds, Elsevier, London
    • Rawlings, N. D. and Barrett, A. J. (2004) Introduction: serine peptidases and their clans. In Handbook of Proteolytic Enzymes, 2nd edn, vol. 2 (Barrett, A. J., Rawlings, N. D. and Woessner, J. F., eds), pp. 1417-1439, Elsevier, London
    • (2004) Handbook of Proteolytic Enzymes , vol.2 , pp. 1417-1439
    • Rawlings, N.D.1    Barrett, A.J.2
  • 6
    • 38749105868 scopus 로고    scopus 로고
    • The MEROPS batch BLAST: A tool to detect peptidases and their non-peptidase homologues in a genome
    • Rawlings, N. D. and Morton, F. R. (2008) The MEROPS batch BLAST: a tool to detect peptidases and their non-peptidase homologues in a genome. Biochimie 90, 243-259
    • (2008) Biochimie , vol.90 , pp. 243-259
    • Rawlings, N.D.1    Morton, F.R.2
  • 7
    • 0025611638 scopus 로고
    • Plasminogen receptors in the mediation of pericellular proteolysis
    • Plow, E. F. and Miles, L. A. (1990) Plasminogen receptors in the mediation of pericellular proteolysis. Cell Differ. Dev. 32, 293-298
    • (1990) Cell Differ. Dev. , vol.32 , pp. 293-298
    • Plow, E.F.1    Miles, L.A.2
  • 8
    • 0035846933 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes
    • Hooper, J. D., Clements, J. A., Quigley, J. P. and Antalis, T. M. (2001) Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes. J. Biol. Chem. 276, 857-860
    • (2001) J. Biol. Chem. , vol.276 , pp. 857-860
    • Hooper, J.D.1    Clements, J.A.2    Quigley, J.P.3    Antalis, T.M.4
  • 9
    • 0037688169 scopus 로고    scopus 로고
    • Membrane anchored serine proteases: A rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer
    • Netzel-Arnett, S., Hooper, J. D., Szabo, R., Madison, E. L., Quigley, J. P., Bugge, T. H. and Antalis, T. M. (2003) Membrane anchored serine proteases: a rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer. Cancer Metastasis Rev. 22, 237-258
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 237-258
    • Netzel-Arnett, S.1    Hooper, J.D.2    Szabo, R.3    Madison, E.L.4    Quigley, J.P.5    Bugge, T.H.6    Antalis, T.M.7
  • 10
    • 43049128477 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases in development and disease
    • Szabo, R. and Bugge, T. H. (2008) Type II transmembrane serine proteases in development and disease. Int. J. Biochem. Cell Biol. 40, 1297-1316
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1297-1316
    • Szabo, R.1    Bugge, T.H.2
  • 12
    • 69949118724 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases
    • Bugge, T. H., Antalis, T. M. and Wu, Q. (2009) Type II transmembrane serine proteases. J. Biol. Chem. 284, 23177-23181
    • (2009) J. Biol. Chem. , vol.284 , pp. 23177-23181
    • Bugge, T.H.1    Antalis, T.M.2    Wu, Q.3
  • 13
    • 0034659960 scopus 로고    scopus 로고
    • Characterization of human gamma-tryptases, novel members of the chromosome 16p mast cell tryptase and prostasin gene families
    • Caughey, G. H., Raymond, W. W., Blount, J. L., Hau, L. W., Pallaoro, M., Wolters, P. J. and Verghese, G. M. (2000) Characterization of human gamma-tryptases, novel members of the chromosome 16p mast cell tryptase and prostasin gene families. J. Immunol. 164, 6566-6575 (Pubitemid 30408843)
    • (2000) Journal of Immunology , vol.164 , Issue.12 , pp. 6566-6575
    • Caughey, G.H.1    Raymond, W.W.2    Blount, J.L.3    Hau, L.W.-T.4    Pallaoro, M.5    Wolters, P.J.6    Verghese, G.M.7
  • 14
    • 0032741435 scopus 로고    scopus 로고
    • Identification of a new member of the tryptase family of mouse and human mast cell proteases which possesses a novel COOH-terminal hydrophobic extension
    • Wong, G. W., Tang, Y., Feyfant, E., Sali, A., Li, L., Li, Y., Huang, C., Friend, D. S., Krilis, S. A. and Stevens, R. L. (1999) Identification of a new member of the tryptase family of mouse and human mast cell proteases which possesses a novel COOH-terminal hydrophobic extension. J. Biol. Chem. 274, 30784-30793
    • (1999) J. Biol. Chem. , vol.274 , pp. 30784-30793
    • Wong, G.W.1    Tang, Y.2    Feyfant, E.3    Sali, A.4    Li, L.5    Li, Y.6    Huang, C.7    Friend, D.S.8    Krilis, S.A.9    Stevens, R.L.10
  • 15
    • 0028282969 scopus 로고
    • Prostasin is a novel human serine proteinase from seminal fluid. Purification, tissue distribution, and localization in prostate gland
    • Yu, J. X., Chao, L. and Chao, J. (1994) Prostasin is a novel human serine proteinase from seminal fluid. Purification, tissue distribution, and localization in prostate gland. J. Biol. Chem. 269, 18843-18848
    • (1994) J. Biol. Chem. , vol.269 , pp. 18843-18848
    • Yu, J.X.1    Chao, L.2    Chao, J.3
  • 17
    • 33845308239 scopus 로고    scopus 로고
    • Prostasin regulates epithelial monolayer function: Cell-specific Gpld1-mediated secretion and functional role for GPI anchor
    • Verghese, G. M., Gutknecht, M. F. and Caughey, G. H. (2006) Prostasin regulates epithelial monolayer function: cell-specific Gpld1-mediated secretion and functional role for GPI anchor. Am. J. Physiol. Cell Physiol. 291, C1258-C1270
    • (2006) Am. J. Physiol. Cell Physiol. , vol.291
    • Verghese, G.M.1    Gutknecht, M.F.2    Caughey, G.H.3
  • 18
    • 0037053319 scopus 로고    scopus 로고
    • A mouse serine protease TESP5 is selectively included into lipid rafts of sperm membrane presumably as a glycosylphosphatidylinositol-anchored protein
    • Honda, A., Yamagata, K., Sugiura, S., Watanabe, K. and Baba, T. (2002) A mouse serine protease TESP5 is selectively included into lipid rafts of sperm membrane presumably as a glycosylphosphatidylinositol-anchored protein. J. Biol. Chem. 277, 16976-16984
    • (2002) J. Biol. Chem. , vol.277 , pp. 16976-16984
    • Honda, A.1    Yamagata, K.2    Sugiura, S.3    Watanabe, K.4    Baba, T.5
  • 20
    • 0028111631 scopus 로고
    • Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains
    • Kitamoto, Y., Yuan, X., Wu, Q., McCourt, D. W. and Sadler, J. E. (1994) Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains. Proc. Natl. Acad. Sci. U.S.A. 91, 7588-7592
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7588-7592
    • Kitamoto, Y.1    Yuan, X.2    Wu, Q.3    McCourt, D.W.4    Sadler, J.E.5
  • 22
    • 0041923832 scopus 로고    scopus 로고
    • Polyserase-I, a human polyprotease with the ability to generate independent serine protease domains from a single translation product
    • Cal, S., Quesada, V., Garabaya, C. and Lopez-Otin, C. (2003) Polyserase-I, a human polyprotease with the ability to generate independent serine protease domains from a single translation product. Proc. Natl. Acad. Sci. U.S.A. 100, 9185-9190
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9185-9190
    • Cal, S.1    Quesada, V.2    Garabaya, C.3    Lopez-Otin, C.4
  • 23
    • 33845807406 scopus 로고    scopus 로고
    • Serase-1B, a new splice variant of polyserase-1/TMPRSS9, activates urokinase-type plasminogen activator and the proteolytic activation is negatively regulated by glycosaminoglycans
    • Okumura, Y., Hayama, M., Takahashi, E., Fujiuchi, M., Shimabukuro, A., Yano, M. and Kido, H. (2006) Serase-1B, a new splice variant of polyserase-1/TMPRSS9, activates urokinase-type plasminogen activator and the proteolytic activation is negatively regulated by glycosaminoglycans. Biochem. J. 400, 551-561
    • (2006) Biochem. J. , vol.400 , pp. 551-561
    • Okumura, Y.1    Hayama, M.2    Takahashi, E.3    Fujiuchi, M.4    Shimabukuro, A.5    Yano, M.6    Kido, H.7
  • 24
    • 1642423649 scopus 로고    scopus 로고
    • The adrenal secretory serine protease AsP is a short secretory isoform of the transmembrane airway trypsin-like protease
    • Hansen, I. A., Fassnacht, M., Hahner, S., Hammer, F., Schammann, M., Meyer, S. R., Bicknell, A. B. and Allolio, B. (2004) The adrenal secretory serine protease AsP is a short secretory isoform of the transmembrane airway trypsin-like protease. Endocrinology 145, 1898-1905
    • (2004) Endocrinology , vol.145 , pp. 1898-1905
    • Hansen, I.A.1    Fassnacht, M.2    Hahner, S.3    Hammer, F.4    Schammann, M.5    Meyer, S.R.6    Bicknell, A.B.7    Allolio, B.8
  • 25
    • 0037474311 scopus 로고    scopus 로고
    • Structure and activity of human pancreasin, a novel tryptic serine peptidase expressed primarily by the pancreas
    • Bhagwandin, V. J., Hau, L. W., Mallen-St Clair, J., Wolters, P. J. and Caughey, G. H. (2003) Structure and activity of human pancreasin, a novel tryptic serine peptidase expressed primarily by the pancreas. J. Biol. Chem. 278, 3363-3371
    • (2003) J. Biol. Chem. , vol.278 , pp. 3363-3371
    • Bhagwandin, V.J.1    Hau, L.W.2    Mallen-St Clair, J.3    Wolters, P.J.4    Caughey, G.H.5
  • 26
    • 0036830570 scopus 로고    scopus 로고
    • Biochemical and functional characterization of human transmembrane tryptase (TMT)/tryptase gamma. TMT is an exocytosed mast cell protease that induces airway hyperresponsiveness in vivo via an interleukin-13/interleukin-4 receptor alpha/signal transducer and activator of transcription (STAT) 6-dependent pathway
    • Wong, G. W., Foster, P. S., Yasuda, S., Qi, J. C., Mahalingam, S., Mellor, E. A., Katsoulotos, G., Li, L., Boyce, J. A., Krilis, S. A. and Stevens, R. L. (2002) Biochemical and functional characterization of human transmembrane tryptase (TMT)/tryptase gamma. TMT is an exocytosed mast cell protease that induces airway hyperresponsiveness in vivo via an interleukin-13/interleukin-4 receptor alpha/signal transducer and activator of transcription (STAT) 6-dependent pathway. J. Biol. Chem. 277, 41906-41915
    • (2002) J. Biol. Chem. , vol.277 , pp. 41906-41915
    • Wong, G.W.1    Foster, P.S.2    Yasuda, S.3    Qi, J.C.4    Mahalingam, S.5    Mellor, E.A.6    Katsoulotos, G.7    Li, L.8    Boyce, J.A.9    Krilis, S.A.10    Stevens, R.L.11
  • 27
    • 20544441281 scopus 로고    scopus 로고
    • Evidence for the occurrence of membrane-type serine protease 1/matriptase on the basolateral sides of enterocytes
    • Tsuzuki, S., Murai, N., Miyake, Y., Inouye, K., Hirayasu, H., Iwanaga, T. and Fushiki, T. (2005) Evidence for the occurrence of membrane-type serine protease 1/matriptase on the basolateral sides of enterocytes. Biochem. J. 388, 679-687
    • (2005) Biochem. J. , vol.388 , pp. 679-687
    • Tsuzuki, S.1    Murai, N.2    Miyake, Y.3    Inouye, K.4    Hirayasu, H.5    Iwanaga, T.6    Fushiki, T.7
  • 30
    • 1942486811 scopus 로고    scopus 로고
    • Assembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contacts
    • Hung, R. J., Hsu, I., Dreiling, J. L., Lee, M. J., Williams, C. A., Oberst, M. D., Dickson, R. B. and Lin, C. Y. (2004) Assembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contacts. Am. J. Physiol. Cell Physiol. 286, C1159-C1169
    • (2004) Am. J. Physiol. Cell Physiol. , vol.286
    • Hung, R.J.1    Hsu, I.2    Dreiling, J.L.3    Lee, M.J.4    Williams, C.A.5    Oberst, M.D.6    Dickson, R.B.7    Lin, C.Y.8
  • 31
    • 70449523435 scopus 로고    scopus 로고
    • Involvement of the cytoplasmic juxtamembrane region of matriptase in its exclusive localization to the basolateral membrane domain of Madin-Darby canine kidney epithelial cells
    • Murai, N., Miyake, Y., Tsuzuki, S., Inouye, K. and Fushiki, T. (2009) Involvement of the cytoplasmic juxtamembrane region of matriptase in its exclusive localization to the basolateral membrane domain of Madin-Darby canine kidney epithelial cells. Cytotechnology 59, 169-176
    • (2009) Cytotechnology , vol.59 , pp. 169-176
    • Murai, N.1    Miyake, Y.2    Tsuzuki, S.3    Inouye, K.4    Fushiki, T.5
  • 32
    • 27844596295 scopus 로고    scopus 로고
    • Filamin is essential for shedding of the transmembrane serine protease, epithin
    • Kim, C., Cho, Y., Kang, C. H., Kim, M. G., Lee, H., Cho, E. G. and Park, D. (2005) Filamin is essential for shedding of the transmembrane serine protease, epithin. EMBO Rep. 6, 1045-1051
    • (2005) EMBO Rep. , vol.6 , pp. 1045-1051
    • Kim, C.1    Cho, Y.2    Kang, C.H.3    Kim, M.G.4    Lee, H.5    Cho, E.G.6    Park, D.7
  • 33
    • 51649102862 scopus 로고    scopus 로고
    • Hepsin colocalizes with desmosomes and induces progression of ovarian cancer in a mouse model
    • Miao, J., Mu, D., Ergel, B., Singavarapu, R., Duan, Z., Powers, S., Oliva, E. and Orsulic, S. (2008) Hepsin colocalizes with desmosomes and induces progression of ovarian cancer in a mouse model. Int. J. Cancer 123, 2041-2047
    • (2008) Int. J. Cancer , vol.123 , pp. 2041-2047
    • Miao, J.1    Mu, D.2    Ergel, B.3    Singavarapu, R.4    Duan, Z.5    Powers, S.6    Oliva, E.7    Orsulic, S.8
  • 34
    • 0030879756 scopus 로고    scopus 로고
    • An epithelial serine protease activates the amiloride-sensitive sodium channel
    • Vallet, V., Chraibi, A., Gaeggeler, H. P., Horisberger, J. D. and Rossier, B. C. (1997) An epithelial serine protease activates the amiloride-sensitive sodium channel. Nature 389, 607-610
    • (1997) Nature , vol.389 , pp. 607-610
    • Vallet, V.1    Chraibi, A.2    Gaeggeler, H.P.3    Horisberger, J.D.4    Rossier, B.C.5
  • 36
    • 0033970075 scopus 로고    scopus 로고
    • Cloning, genomic organization, chromosomal assignment and expression of a novel mosaic serine proteinase: Epitheliasin
    • Jacquinet, E., Rao, N. V., Rao, G. V. and Hoidal, J. R. (2000) Cloning, genomic organization, chromosomal assignment and expression of a novel mosaic serine proteinase: epitheliasin. FEBS Lett. 468, 93-100
    • (2000) FEBS Lett. , vol.468 , pp. 93-100
    • Jacquinet, E.1    Rao, N.V.2    Rao, G.V.3    Hoidal, J.R.4
  • 37
    • 0035866379 scopus 로고    scopus 로고
    • Catalytic cleavage of the androgen-regulated TMPRSS2 protease results in its secretion by prostate and prostate cancer epithelia
    • Afar, D. E., Vivanco, I., Hubert, R. S., Kuo, J., Chen, E., Saffran, D. C., Raitano, A. B. and Jakobovits, A. (2001) Catalytic cleavage of the androgen-regulated TMPRSS2 protease results in its secretion by prostate and prostate cancer epithelia. Cancer Res. 61, 1686-1692
    • (2001) Cancer Res. , vol.61 , pp. 1686-1692
    • Afar, D.E.1    Vivanco, I.2    Hubert, R.S.3    Kuo, J.4    Chen, E.5    Saffran, D.C.6    Raitano, A.B.7    Jakobovits, A.8
  • 38
    • 0033555927 scopus 로고    scopus 로고
    • Apical sorting of bovine enteropeptidase does not involve detergent- resistant association with sphingolipid-cholesterol rafts
    • Zheng, X., Lu, D. and Sadler, J. E. (1999) Apical sorting of bovine enteropeptidase does not involve detergent- resistant association with sphingolipid-cholesterol rafts. J. Biol. Chem. 274, 1596-1605
    • (1999) J. Biol. Chem. , vol.274 , pp. 1596-1605
    • Zheng, X.1    Lu, D.2    Sadler, J.E.3
  • 39
    • 0036510358 scopus 로고    scopus 로고
    • Mucin-like domain of enteropeptidase directs apical targeting in Madin-Darby canine kidney cells
    • Zheng, X. and Sadler, J. E. (2002) Mucin-like domain of enteropeptidase directs apical targeting in Madin-Darby canine kidney cells. J. Biol. Chem. 277, 6858-6863
    • (2002) J. Biol. Chem. , vol.277 , pp. 6858-6863
    • Zheng, X.1    Sadler, J.E.2
  • 40
    • 38149089484 scopus 로고    scopus 로고
    • An integrated genetic and functional analysis of the role of type II transmembrane serine proteases (TMPRSSs) in hearing loss
    • Guipponi, M., Toh, M. Y., Tan, J., Park, D., Hanson, K., Ballana, E., Kwong, D., Cannon, P. Z., Wu, Q., Gout, A. et al. (2008) An integrated genetic and functional analysis of the role of type II transmembrane serine proteases (TMPRSSs) in hearing loss. Hum. Mutat. 29, 130-141
    • (2008) Hum. Mutat. , vol.29 , pp. 130-141
    • Guipponi, M.1    Toh, M.Y.2    Tan, J.3    Park, D.4    Hanson, K.5    Ballana, E.6    Kwong, D.7    Cannon, P.Z.8    Wu, Q.9    Gout, A.10
  • 41
    • 44649106949 scopus 로고    scopus 로고
    • The androgen-regulated type II serine protease TMPRSS2 is differentially expressed and mislocalized in prostate adenocarcinoma
    • Lucas, J. M., True, L., Hawley, S., Matsumura, M., Morrissey, C., Vessella, R. and Nelson, P. S. (2008) The androgen-regulated type II serine protease TMPRSS2 is differentially expressed and mislocalized in prostate adenocarcinoma. J. Pathol. 215, 118-125
    • (2008) J. Pathol. , vol.215 , pp. 118-125
    • Lucas, J.M.1    True, L.2    Hawley, S.3    Matsumura, M.4    Morrissey, C.5    Vessella, R.6    Nelson, P.S.7
  • 42
    • 73849123008 scopus 로고    scopus 로고
    • Urinary prostasin in humans: Relationships among prostasin, aldosterone and epithelial sodium channel activity
    • Koda, A., Wakida, N., Toriyama, K., Yamamoto, K., Iijima, H., Tomita, K. and Kitamura, K. (2009) Urinary prostasin in humans: relationships among prostasin, aldosterone and epithelial sodium channel activity. Hypertens. Res. 32, 276-281
    • (2009) Hypertens. Res. , vol.32 , pp. 276-281
    • Koda, A.1    Wakida, N.2    Toriyama, K.3    Yamamoto, K.4    Iijima, H.5    Tomita, K.6    Kitamura, K.7
  • 47
    • 0033603547 scopus 로고    scopus 로고
    • Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk
    • Lin, C. Y., Anders, J., Johnson, M. and Dickson, R. B. (1999) Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk. J. Biol. Chem. 274, 18237-18242
    • (1999) J. Biol. Chem. , vol.274 , pp. 18237-18242
    • Lin, C.Y.1    Anders, J.2    Johnson, M.3    Dickson, R.B.4
  • 48
    • 0027474797 scopus 로고
    • Identification and characterization of a novel matrix-degrading protease from hormone-dependent human breast cancer cells
    • Shi, Y. E., Torri, J., Yieh, L., Wellstein, A., Lippman, M. E. and Dickson, R. B. (1993) Identification and characterization of a novel matrix-degrading protease from hormone-dependent human breast cancer cells. Cancer Res. 53, 1409-1415 (Pubitemid 23097125)
    • (1993) Cancer Research , vol.53 , Issue.6 , pp. 1409-1415
    • Shi, Y.E.1    Torri, J.2    Yieh, L.3    Wellstein, A.4    Lippman, M.E.5    Dickson, R.B.6
  • 49
    • 0035976996 scopus 로고    scopus 로고
    • N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease
    • Cho, E. G., Kim, M. G., Kim, C., Kim, S. R., Seong, I. S., Chung, C., Schwartz, R. H. and Park, D. (2001) N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease. J. Biol. Chem. 276, 44581-44589
    • (2001) J. Biol. Chem. , vol.276 , pp. 44581-44589
    • Cho, E.G.1    Kim, M.G.2    Kim, C.3    Kim, S.R.4    Seong, I.S.5    Chung, C.6    Schwartz, R.H.7    Park, D.8
  • 50
    • 0035081038 scopus 로고    scopus 로고
    • Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor
    • Benaud, C., Dickson, R. B. and Lin, C. Y. (2001) Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor. Eur. J. Biochem. 268, 1439-1447
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1439-1447
    • Benaud, C.1    Dickson, R.B.2    Lin, C.Y.3
  • 51
    • 23944457415 scopus 로고    scopus 로고
    • Production of soluble matriptase by human cancer cell lines and cell surface activation of its zymogen by trypsin
    • Jin, X., Hirosaki, T., Lin, C. Y., Dickson, R. B., Higashi, S., Kitamura, H. and Miyazaki, K. (2005) Production of soluble matriptase by human cancer cell lines and cell surface activation of its zymogen by trypsin. J. Cell Biochem. 95, 632-647
    • (2005) J. Cell Biochem. , vol.95 , pp. 632-647
    • Jin, X.1    Hirosaki, T.2    Lin, C.Y.3    Dickson, R.B.4    Higashi, S.5    Kitamura, H.6    Miyazaki, K.7
  • 52
    • 0018565295 scopus 로고
    • The release of enterokinase following secretin and cholecystokinin- pancreozymin in man
    • Moss, S., Birch, G. R., Lobley, R. W. and Holmes, R. (1979) The release of enterokinase following secretin and cholecystokinin-pancreozymin in man. Scand. J. Gastroenterol. 14, 1001-1007
    • (1979) Scand. J. Gastroenterol. , vol.14 , pp. 1001-1007
    • Moss, S.1    Birch, G.R.2    Lobley, R.W.3    Holmes, R.4
  • 53
    • 0020028218 scopus 로고
    • Effect of pancreozymin and secretin on intraluminal enterokinase, trypsin, and chymotrypsin activities of cystic fibrosis and control children
    • Lebenthal, E. and Lee, P. C. (1982) Effect of pancreozymin and secretin on intraluminal enterokinase, trypsin, and chymotrypsin activities of cystic fibrosis and control children. Digestion 23, 39-47
    • (1982) Digestion , vol.23 , pp. 39-47
    • Lebenthal, E.1    Lee, P.C.2
  • 56
    • 11144248101 scopus 로고    scopus 로고
    • Shedding of membrane epithin is blocked without LDLRA4 and its protease activation site
    • Cho, E. G., Schwartz, R. H. and Kim, M. G. (2005) Shedding of membrane epithin is blocked without LDLRA4 and its protease activation site. Biochem. Biophys. Res. Commun. 327, 328-334
    • (2005) Biochem. Biophys. Res. Commun. , vol.327 , pp. 328-334
    • Cho, E.G.1    Schwartz, R.H.2    Kim, M.G.3
  • 57
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I. and Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 59
    • 12444316010 scopus 로고    scopus 로고
    • The structure of the extracellular region of human hepsin reveals a serine protease domain and a novel scavenger receptor cysteine-rich (SRCR) domain
    • Somoza, J. R., Ho, J. D., Luong, C., Ghate, M., Sprengeler, P. A., Mortara, K., Shrader, W. D., Sperandio, D., Chan, H., McGrath, M. E. and Katz, B. A. (2003) The structure of the extracellular region of human hepsin reveals a serine protease domain and a novel scavenger receptor cysteine-rich (SRCR) domain. Structure 11, 1123-1131
    • (2003) Structure , vol.11 , pp. 1123-1131
    • Somoza, J.R.1    Ho, J.D.2    Luong, C.3    Ghate, M.4    Sprengeler, P.A.5    Mortara, K.6    Shrader, W.D.7    Sperandio, D.8    Chan, H.9    McGrath, M.E.10    Katz, B.A.11
  • 60
    • 0344631102 scopus 로고    scopus 로고
    • Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide
    • Lu, D., Futterer, K., Korolev, S., Zheng, X., Tan, K., Waksman, G. and Sadler, J. E. (1999) Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide. J. Mol. Biol. 292, 361-373
    • (1999) J. Mol. Biol. , vol.292 , pp. 361-373
    • Lu, D.1    Futterer, K.2    Korolev, S.3    Zheng, X.4    Tan, K.5    Waksman, G.6    Sadler, J.E.7
  • 61
    • 34247143776 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase family
    • Kyrieleis, O. J., Huber, R., Ong, E., Oehler, R., Hunter, M., Madison, E. L. and Jacob, U. (2007) Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase family. FEBS J. 274, 2148-2160
    • (2007) FEBS J. , vol.274 , pp. 2148-2160
    • Kyrieleis, O.J.1    Huber, R.2    Ong, E.3    Oehler, R.4    Hunter, M.5    Madison, E.L.6    Jacob, U.7
  • 62
    • 68849090838 scopus 로고    scopus 로고
    • Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations
    • Spraggon, G., Hornsby, M., Shipway, A., Tully, D. C., Bursulaya, B., Danahay, H., Harris, J. L. and Lesley, S. A. (2009) Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations. Protein Sci. 18, 1081-1094
    • (2009) Protein Sci. , vol.18 , pp. 1081-1094
    • Spraggon, G.1    Hornsby, M.2    Shipway, A.3    Tully, D.C.4    Bursulaya, B.5    Danahay, H.6    Harris, J.L.7    Lesley, S.A.8
  • 65
    • 0036293418 scopus 로고    scopus 로고
    • The methyl group of Nα(Me)Arg-containing peptides disturbs the active-site geometry of thrombin, impairing efficient cleavage
    • Friedrich, R., Steinmetzer, T., Huber, R., Sturzebecher, J. and Bode, W. (2002) The methyl group of Nα(Me)Arg-containing peptides disturbs the active-site geometry of thrombin, impairing efficient cleavage. J. Mol. Biol. 316, 869-874
    • (2002) J. Mol. Biol. , vol.316 , pp. 869-874
    • Friedrich, R.1    Steinmetzer, T.2    Huber, R.3    Sturzebecher, J.4    Bode, W.5
  • 66
    • 0038035877 scopus 로고    scopus 로고
    • The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor
    • Oberst, M. D., Williams, C. A., Dickson, R. B., Johnson, M. D. and Lin, C. Y. (2003) The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor. J. Biol. Chem. 278, 26773-26779
    • (2003) J. Biol. Chem. , vol.278 , pp. 26773-26779
    • Oberst, M.D.1    Williams, C.A.2    Dickson, R.B.3    Johnson, M.D.4    Lin, C.Y.5
  • 68
    • 30044448792 scopus 로고    scopus 로고
    • Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin
    • Macao, B., Johansson, D. G., Hansson, G. C. and Hard, T. (2006) Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin. Nat. Struct. Mol. Biol. 13, 71-76
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 71-76
    • Macao, B.1    Johansson, D.G.2    Hansson, G.C.3    Hard, T.4
  • 70
    • 4544273338 scopus 로고    scopus 로고
    • Identification of domain structures in the propeptide of corin essential for the processing of proatrial natriuretic peptide
    • Knappe, S., Wu, F., Madlansacay, M. R. and Wu, Q. (2004) Identification of domain structures in the propeptide of corin essential for the processing of proatrial natriuretic peptide. J. Biol. Chem. 279, 34464-34471
    • (2004) J. Biol. Chem. , vol.279 , pp. 34464-34471
    • Knappe, S.1    Wu, F.2    Madlansacay, M.R.3    Wu, Q.4
  • 71
    • 0031466897 scopus 로고    scopus 로고
    • Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain
    • Lu, D., Yuan, X., Zheng, X. and Sadler, J. E. (1997) Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain. J. Biol. Chem. 272, 31293-31300
    • (1997) J. Biol. Chem. , vol.272 , pp. 31293-31300
    • Lu, D.1    Yuan, X.2    Zheng, X.3    Sadler, J.E.4
  • 72
    • 45849113987 scopus 로고    scopus 로고
    • N-glycosylation modulates the cell-surface expression and catalytic activity of corin
    • Gladysheva, I. P., King, S. M. and Houng, A. K. (2008) N-glycosylation modulates the cell-surface expression and catalytic activity of corin. Biochem. Biophys. Res. Commun. 373, 130-135
    • (2008) Biochem. Biophys. Res. Commun. , vol.373 , pp. 130-135
    • Gladysheva, I.P.1    King, S.M.2    Houng, A.K.3
  • 73
    • 34948839546 scopus 로고    scopus 로고
    • Role of glycosylation in corin zymogen activation
    • Liao, X., Wang, W., Chen, S. and Wu, Q. (2007) Role of glycosylation in corin zymogen activation. J. Biol. Chem. 282, 27728-27735
    • (2007) J. Biol. Chem. , vol.282 , pp. 27728-27735
    • Liao, X.1    Wang, W.2    Chen, S.3    Wu, Q.4
  • 74
    • 38449120396 scopus 로고    scopus 로고
    • The type II transmembrane serine protease matriptase-2-identification, structural features, enzymology, expression pattern and potential roles
    • Ramsay, A. J., Reid, J. C., Velasco, G., Quigley, J. P. and Hooper, J. D. (2008) The type II transmembrane serine protease matriptase-2-identification, structural features, enzymology, expression pattern and potential roles. Front. Biosci. 13, 569-579
    • (2008) Front. Biosci. , vol.13 , pp. 569-579
    • Ramsay, A.J.1    Reid, J.C.2    Velasco, G.3    Quigley, J.P.4    Hooper, J.D.5
  • 76
    • 70449467280 scopus 로고    scopus 로고
    • Haematologic data, iron parameters and molecular findings in two new cases of iron-refractory iron deficiency anaemia
    • Tchou, I., Diepold, M., Pilotto, P. A., Swinkels, D., Neerman-Arbez, M. and Beris, P. (2009) Haematologic data, iron parameters and molecular findings in two new cases of iron-refractory iron deficiency anaemia. Eur. J. Haematol. 83, 595-602
    • (2009) Eur. J. Haematol. , vol.83 , pp. 595-602
    • Tchou, I.1    Diepold, M.2    Pilotto, P.A.3    Swinkels, D.4    Neerman-Arbez, M.5    Beris, P.6
  • 77
    • 34047230586 scopus 로고    scopus 로고
    • Corin I555(P568) allele is associated with enhanced cardiac hypertrophic response to increased systemic afterload
    • Rame, J. E., Drazner, M. H., Post, W., Peshock, R., Lima, J., Cooper, R. S. and Dries, D. L. (2007) Corin I555(P568) allele is associated with enhanced cardiac hypertrophic response to increased systemic afterload. Hypertension 49, 857-864
    • (2007) Hypertension , vol.49 , pp. 857-864
    • Rame, J.E.1    Drazner, M.H.2    Post, W.3    Peshock, R.4    Lima, J.5    Cooper, R.S.6    Dries, D.L.7
  • 78
    • 27144449108 scopus 로고    scopus 로고
    • Corin gene minor allele defined by 2 missense mutations is common in blacks and associated with high blood pressure and hypertension
    • Dries, D. L., Victor, R. G., Rame, J. E., Cooper, R. S., Wu, X., Zhu, X., Leonard, D., Ho, S. I., Wu, Q., Post, W. and Drazner, M. H. (2005) Corin gene minor allele defined by 2 missense mutations is common in blacks and associated with high blood pressure and hypertension. Circulation 112, 2403-2410
    • (2005) Circulation , vol.112 , pp. 2403-2410
    • Dries, D.L.1    Victor, R.G.2    Rame, J.E.3    Cooper, R.S.4    Wu, X.5    Zhu, X.6    Leonard, D.7    Ho, S.I.8    Wu, Q.9    Post, W.10    Drazner, M.H.11
  • 79
    • 54049142560 scopus 로고    scopus 로고
    • Corin variant associated with hypertension and cardiac hypertrophy exhibits impaired zymogen activation and natriuretic peptide processing activity
    • Wang, W., Liao, X., Fukuda, K., Knappe, S., Wu, F., Dries, D. L., Qin, J. and Wu, Q. (2008) Corin variant associated with hypertension and cardiac hypertrophy exhibits impaired zymogen activation and natriuretic peptide processing activity. Circ. Res. 103, 502-508
    • (2008) Circ. Res. , vol.103 , pp. 502-508
    • Wang, W.1    Liao, X.2    Fukuda, K.3    Knappe, S.4    Wu, F.5    Dries, D.L.6    Qin, J.7    Wu, Q.8
  • 81
    • 0034714379 scopus 로고    scopus 로고
    • Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates
    • Takeuchi, T., Harris, J. L., Huang, W., Yan, K. W., Coughlin, S. R. and Craik, C. S. (2000) Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates. J. Biol. Chem. 275, 26333-26342
    • (2000) J. Biol. Chem. , vol.275 , pp. 26333-26342
    • Takeuchi, T.1    Harris, J.L.2    Huang, W.3    Yan, K.W.4    Coughlin, S.R.5    Craik, C.S.6
  • 82
    • 33646726556 scopus 로고    scopus 로고
    • Protease specificity determination by using cellular libraries of peptide substrates (CLiPS)
    • Boulware, K. T. and Daugherty, P. S. (2006) Protease specificity determination by using cellular libraries of peptide substrates (CLiPS). Proc. Natl. Acad. Sci. U.S.A. 103, 7583-7588
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 7583-7588
    • Boulware, K.T.1    Daugherty, P.S.2
  • 83
    • 21244448682 scopus 로고    scopus 로고
    • Hepatocyte growth factor is a preferred in vitro substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancers
    • Herter, S., Piper, D. E., Aaron, W., Gabriele, T., Cutler, G., Cao, P., Bhatt, A. S., Choe, Y., Craik, C. S., Walker, N. et al. (2005) Hepatocyte growth factor is a preferred in vitro substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancers. Biochem. J. 390, 125-136
    • (2005) Biochem. J. , vol.390 , pp. 125-136
    • Herter, S.1    Piper, D.E.2    Aaron, W.3    Gabriele, T.4    Cutler, G.5    Cao, P.6    Bhatt, A.S.7    Choe, Y.8    Craik, C.S.9    Walker, N.10
  • 86
    • 8744227027 scopus 로고    scopus 로고
    • Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes
    • Hobson, J. P., Netzel-Arnett, S., Szabo, R., Rehault, S. M., Church, F. C., Strickland, D. K., Lawrence, D. A., Antalis, T. M. and Bugge, T. H. (2004) Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes. J. Biol. Chem. 279, 46981-46994
    • (2004) J. Biol. Chem. , vol.279 , pp. 46981-46994
    • Hobson, J.P.1    Netzel-Arnett, S.2    Szabo, R.3    Rehault, S.M.4    Church, F.C.5    Strickland, D.K.6    Lawrence, D.A.7    Antalis, T.M.8    Bugge, T.H.9
  • 87
    • 63049086099 scopus 로고    scopus 로고
    • Probing the substrate specificities of matriptase, matriptase-2, hepsin and DESC1 with internally quenched fluorescent peptides
    • Beliveau, F., Desilets, A. and Leduc, R. (2009) Probing the substrate specificities of matriptase, matriptase-2, hepsin and DESC1 with internally quenched fluorescent peptides. FEBS J. 276, 2213-2226
    • (2009) FEBS J. , vol.276 , pp. 2213-2226
    • Beliveau, F.1    Desilets, A.2    Leduc, R.3
  • 89
    • 0022367735 scopus 로고
    • Proteolytic enzymes, past and present
    • Neurath, H. (1985) Proteolytic enzymes, past and present. Fed. Proc. 44, 2907-2913
    • (1985) Fed. Proc. , vol.44 , pp. 2907-2913
    • Neurath, H.1
  • 91
    • 0028804679 scopus 로고
    • Hepsin, a putative membrane-associated serine protease, activates human factor VII and initiates a pathway of blood coagulation on the cell surface leading to thrombin formation
    • Kazama, Y., Hamamoto, T., Foster, D. C. and Kisiel, W. (1995) Hepsin, a putative membrane-associated serine protease, activates human factor VII and initiates a pathway of blood coagulation on the cell surface leading to thrombin formation. J. Biol. Chem. 270, 66-72
    • (1995) J. Biol. Chem. , vol.270 , pp. 66-72
    • Kazama, Y.1    Hamamoto, T.2    Foster, D.C.3    Kisiel, W.4
  • 93
    • 33750156940 scopus 로고    scopus 로고
    • Pro-urokinase-type plasminogen activator is a substrate for hepsin
    • Moran, P., Li, W., Fan, B., Vij, R., Eigenbrot, C. and Kirchhofer, D. (2006) Pro-urokinase-type plasminogen activator is a substrate for hepsin. J. Biol. Chem. 281, 30439-30446
    • (2006) J. Biol. Chem. , vol.281 , pp. 30439-30446
    • Moran, P.1    Li, W.2    Fan, B.3    Vij, R.4    Eigenbrot, C.5    Kirchhofer, D.6
  • 94
    • 0034711244 scopus 로고    scopus 로고
    • Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease
    • Lee, S. L., Dickson, R. B. and Lin, C. Y. (2000) Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease. J. Biol. Chem. 275, 36720-36725
    • (2000) J. Biol. Chem. , vol.275 , pp. 36720-36725
    • Lee, S.L.1    Dickson, R.B.2    Lin, C.Y.3
  • 95
    • 33750614146 scopus 로고    scopus 로고
    • Initiation of plasminogen activation on the surface of monocytes expressing the type II transmembrane serine protease matriptase
    • Kilpatrick, L. M., Harris, R. L., Owen, K. A., Bass, R., Ghorayeb, C., Bar-Or, A. and Ellis, V. (2006) Initiation of plasminogen activation on the surface of monocytes expressing the type II transmembrane serine protease matriptase. Blood 108, 2616-2623
    • (2006) Blood , vol.108 , pp. 2616-2623
    • Kilpatrick, L.M.1    Harris, R.L.2    Owen, K.A.3    Bass, R.4    Ghorayeb, C.5    Bar-Or, A.6    Ellis, V.7
  • 97
    • 0033818463 scopus 로고    scopus 로고
    • Urokinase receptor: A molecular organizer in cellular communication
    • Preissner, K. T., Kanse, S. M. and May, A. E. (2000) Urokinase receptor: a molecular organizer in cellular communication. Curr. Opin. Cell Biol. 12, 621-628
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 621-628
    • Preissner, K.T.1    Kanse, S.M.2    May, A.E.3
  • 98
    • 33750315799 scopus 로고    scopus 로고
    • Matriptase activates stromelysin (MMP-3) and promotes tumor growth and angiogenesis
    • DOI 10.1111/j.1349-7006.2006.00328.x
    • Jin, X., Yagi, M., Akiyama, N., Hirosaki, T., Higashi, S., Lin, C. Y., Dickson, R. B., Kitamura, H. and Miyazaki, K. (2006) Matriptase activates stromelysin (MMP-3) and promotes tumor growth and angiogenesis. Cancer Sci. 97, 1327-1334 (Pubitemid 44614984)
    • (2006) Cancer Science , vol.97 , Issue.12 , pp. 1327-1334
    • Jin, X.1    Yagi, M.2    Akiyama, N.3    Hirosaki, T.4    Higashi, S.5    Lin, C.-Y.6    Dickson, R.B.7    Kitamura, H.8    Miyazaki, K.9
  • 101
    • 0031465168 scopus 로고    scopus 로고
    • Identification and cloning of the membrane-associated serine protease, hepsin, from mouse preimplantation embryos
    • Vu, T. K., Liu, R. W., Haaksma, C. J., Tomasek, J. J. and Howard, E. W. (1997) Identification and cloning of the membrane-associated serine protease, hepsin, from mouse preimplantation embryos. J. Biol. Chem. 272, 31315-31320
    • (1997) J. Biol. Chem. , vol.272 , pp. 31315-31320
    • Vu, T.K.1    Liu, R.W.2    Haaksma, C.J.3    Tomasek, J.J.4    Howard, E.W.5
  • 102
    • 43549108764 scopus 로고    scopus 로고
    • Neurobin/TMPRSS11c, a novel type II transmembrane serine protease that cleaves fibroblast growth factor-2 in vitro
    • Stallmach, R. and Gloor, S. M. (2008) Neurobin/TMPRSS11c, a novel type II transmembrane serine protease that cleaves fibroblast growth factor-2 in vitro. Biochem. J. 412, 81-91
    • (2008) Biochem. J. , vol.412 , pp. 81-91
    • Stallmach, R.1    Gloor, S.M.2
  • 103
    • 44849133938 scopus 로고    scopus 로고
    • Mutation G827R in matriptase causing autosomal recessive ichthyosis with hypotrichosis yields an inactive protease
    • Desilets, A., Beliveau, F., Vandal, G., McDuff, F. O., Lavigne, P. and Leduc, R. (2008) Mutation G827R in matriptase causing autosomal recessive ichthyosis with hypotrichosis yields an inactive protease. J. Biol. Chem. 283, 10535-10542
    • (2008) J. Biol. Chem. , vol.283 , pp. 10535-10542
    • Desilets, A.1    Beliveau, F.2    Vandal, G.3    McDuff, F.O.4    Lavigne, P.5    Leduc, R.6
  • 104
    • 0037020169 scopus 로고    scopus 로고
    • Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins
    • Velasco, G., Cal, S., Quesada, V., Sanchez, L. M. and Lopez-Otin, C. (2002) Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins. J. Biol. Chem. 277, 37637-37646
    • (2002) J. Biol. Chem. , vol.277 , pp. 37637-37646
    • Velasco, G.1    Cal, S.2    Quesada, V.3    Sanchez, L.M.4    Lopez-Otin, C.5
  • 105
    • 34250895029 scopus 로고    scopus 로고
    • Roles and regulation of membrane-associated serine proteases
    • Qiu, D., Owen, K., Gray, K., Bass, R. and Ellis, V. (2007) Roles and regulation of membrane-associated serine proteases. Biochem. Soc. Trans. 35, 583-587
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 583-587
    • Qiu, D.1    Owen, K.2    Gray, K.3    Bass, R.4    Ellis, V.5
  • 106
    • 33645465530 scopus 로고    scopus 로고
    • Activation of epithelial sodium channels by mouse channel activating proteases (mCAP) expressed in Xenopus oocytes requires catalytic activity of mCAP3 and mCAP2 but not mCAP1
    • Andreasen, D., Vuagniaux, G., Fowler-Jaeger, N., Hummler, E. and Rossier, B. C. (2006) Activation of epithelial sodium channels by mouse channel activating proteases (mCAP) expressed in Xenopus oocytes requires catalytic activity of mCAP3 and mCAP2 but not mCAP1. J. Am. Soc. Nephrol. 17, 968-976
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 968-976
    • Andreasen, D.1    Vuagniaux, G.2    Fowler-Jaeger, N.3    Hummler, E.4    Rossier, B.C.5
  • 107
    • 0033613183 scopus 로고    scopus 로고
    • How the protease thrombin talks to cells
    • Coughlin, S. R. (1999) How the protease thrombin talks to cells. Proc. Natl. Acad. Sci. U.S.A. 96, 11023-11027
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 11023-11027
    • Coughlin, S.R.1
  • 108
    • 34247388037 scopus 로고    scopus 로고
    • Protease-activated receptor signalling, endocytic sorting and dysregulation in cancer
    • Arora, P., Ricks, T. K. and Trejo, J. (2007) Protease-activated receptor signalling, endocytic sorting and dysregulation in cancer. J. Cell Sci. 120, 921-928
    • (2007) J. Cell Sci. , vol.120 , pp. 921-928
    • Arora, P.1    Ricks, T.K.2    Trejo, J.3
  • 109
    • 1642279517 scopus 로고    scopus 로고
    • Protease-activated receptors: Contribution to physiology and disease
    • Ossovskaya, V. S. and Bunnett, N. W. (2004) Protease-activated receptors: contribution to physiology and disease. Physiol Rev. 84, 579-621
    • (2004) Physiol Rev. , vol.84 , pp. 579-621
    • Ossovskaya, V.S.1    Bunnett, N.W.2
  • 110
    • 0346788901 scopus 로고    scopus 로고
    • Protease-activated receptor 2: Activation, signalling and function
    • Cottrell, G. S., Amadesi, S., Schmidlin, F. and Bunnett, N. (2003) Protease-activated receptor 2: activation, signalling and function. Biochem. Soc.Trans. 31, 1191-1197
    • (2003) Biochem. Soc.Trans. , vol.31 , pp. 1191-1197
    • Cottrell, G.S.1    Amadesi, S.2    Schmidlin, F.3    Bunnett, N.4
  • 111
    • 47549086134 scopus 로고    scopus 로고
    • Prostatic trypsin-like kallikrein-related peptidases (KLKs) and other prostate-expressed tryptic proteinases as regulators of signalling via proteinase-activated receptors (PARs)
    • Ramsay, A. J., Reid, J. C., Adams, M. N., Samaratunga, H., Dong, Y., Clements, J. A. and Hooper, J. D. (2008) Prostatic trypsin-like kallikrein-related peptidases (KLKs) and other prostate-expressed tryptic proteinases as regulators of signalling via proteinase-activated receptors (PARs). Biol. Chem. 389, 653-668
    • (2008) Biol. Chem. , vol.389 , pp. 653-668
    • Ramsay, A.J.1    Reid, J.C.2    Adams, M.N.3    Samaratunga, H.4    Dong, Y.5    Clements, J.A.6    Hooper, J.D.7
  • 112
    • 21744437441 scopus 로고    scopus 로고
    • The membrane-anchored serine protease, TMPRSS2, activates PAR-2 in prostate cancer cells
    • Wilson, S., Greer, B., Hooper, J., Zijlstra, A., Walker, B., Quigley, J. and Hawthorne, S. (2005) The membrane-anchored serine protease, TMPRSS2, activates PAR-2 in prostate cancer cells. Biochem. J. 388, 967-972
    • (2005) Biochem. J. , vol.388 , pp. 967-972
    • Wilson, S.1    Greer, B.2    Hooper, J.3    Zijlstra, A.4    Walker, B.5    Quigley, J.6    Hawthorne, S.7
  • 113
    • 34247229838 scopus 로고    scopus 로고
    • Membrane-type serine protease-1/matriptase induces interleukin-6 and -8 in endothelial cells by activation of protease-activated receptor-2: Potential implications in atherosclerosis
    • Seitz, I., Hess, S., Schulz, H., Eckl, R., Busch, G., Montens, H. P., Brandl, R., Seidl, S., Schomig, A. and Ott, I. (2007) Membrane-type serine protease-1/matriptase induces interleukin-6 and -8 in endothelial cells by activation of protease-activated receptor-2: potential implications in atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 27, 769-775
    • (2007) Arterioscler. Thromb. Vasc. Biol. , vol.27 , pp. 769-775
    • Seitz, I.1    Hess, S.2    Schulz, H.3    Eckl, R.4    Busch, G.5    Montens, H.P.6    Brandl, R.7    Seidl, S.8    Schomig, A.9    Ott, I.10
  • 114
    • 29144525916 scopus 로고    scopus 로고
    • Human airway trypsin-like protease induces amphiregulin release through a mechanism involving protease-activated receptor-2-mediated ERK activation and TNFα-converting enzyme activity in airway epithelial cells
    • Chokki, M., Eguchi, H., Hamamura, I., Mitsuhashi, H. and Kamimura, T. (2005) Human airway trypsin-like protease induces amphiregulin release through a mechanism involving protease-activated receptor-2-mediated ERK activation and TNFα-converting enzyme activity in airway epithelial cells. FEBS J. 272, 6387-6399
    • (2005) FEBS J. , vol.272 , pp. 6387-6399
    • Chokki, M.1    Eguchi, H.2    Hamamura, I.3    Mitsuhashi, H.4    Kamimura, T.5
  • 115
    • 70350439830 scopus 로고    scopus 로고
    • Prostasin regulates iNOS and cyclin D1 expression by modulating protease-activated receptor-2 signaling in prostate epithelial cells
    • Chen, L. M., Hatfield, M. L., Fu, Y. Y. and Chai, K. X. (2009) Prostasin regulates iNOS and cyclin D1 expression by modulating protease-activated receptor-2 signaling in prostate epithelial cells. Prostate 69, 1790-1801
    • (2009) Prostate , vol.69 , pp. 1790-1801
    • Chen, L.M.1    Hatfield, M.L.2    Fu, Y.Y.3    Chai, K.X.4
  • 116
    • 0028349254 scopus 로고
    • Hepatocyte growth factor/scatter factor effects on epithelia. Regulation of intercellular junctions in transformed and nontransformed cell lines, basolateral polarization of c-met receptor in transformed and natural intestinal epithelia, and induction of rapid wound repair in a transformed model epithelium
    • Nusrat, A., Parkos, C. A., Bacarra, A. E., Godowski, P. J., Delp-Archer, C., Rosen, E. M. and Madara, J. L. (1994) Hepatocyte growth factor/scatter factor effects on epithelia. Regulation of intercellular junctions in transformed and nontransformed cell lines, basolateral polarization of c-met receptor in transformed and natural intestinal epithelia, and induction of rapid wound repair in a transformed model epithelium. J. Clin. Invest. 93, 2056-2065
    • (1994) J. Clin. Invest. , vol.93 , pp. 2056-2065
    • Nusrat, A.1    Parkos, C.A.2    Bacarra, A.E.3    Godowski, P.J.4    Delp-Archer, C.5    Rosen, E.M.6    Madara, J.L.7
  • 117
    • 34248535705 scopus 로고    scopus 로고
    • Coordinate expression and functional profiling identify an extracellular proteolytic signaling pathway
    • Bhatt, A. S., Welm, A., Farady, C. J., Vasquez, M., Wilson, K. and Craik, C. S. (2007) Coordinate expression and functional profiling identify an extracellular proteolytic signaling pathway. Proc. Natl. Acad. Sci. U.S.A. 104, 5771-5776
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 5771-5776
    • Bhatt, A.S.1    Welm, A.2    Farady, C.J.3    Vasquez, M.4    Wilson, K.5    Craik, C.S.6
  • 120
    • 73649147998 scopus 로고    scopus 로고
    • Matriptase/epithin participates in mammary epithelial cell growth and morphogenesis through HGF activation
    • Lee, S. L., Huang, P. Y., Roller, P., Cho, E. G., Park, D. and Dickson, R. B. (2010) Matriptase/epithin participates in mammary epithelial cell growth and morphogenesis through HGF activation. Mech. Dev. 127, 82-95
    • (2010) Mech. Dev. , vol.127 , pp. 82-95
    • Lee, S.L.1    Huang, P.Y.2    Roller, P.3    Cho, E.G.4    Park, D.5    Dickson, R.B.6
  • 121
    • 15544386767 scopus 로고    scopus 로고
    • Hepsin activates pro-hepatocyte growth factor and is inhibited by hepatocyte growth factor activator inhibitor-1B (HAI-1B) and HAI-2
    • Kirchhofer, D., Peek, M., Lipari, M. T., Billeci, K., Fan, B. and Moran, P. (2005) Hepsin activates pro-hepatocyte growth factor and is inhibited by hepatocyte growth factor activator inhibitor-1B (HAI-1B) and HAI-2. FEBS Lett. 579, 1945-1950
    • (2005) FEBS Lett. , vol.579 , pp. 1945-1950
    • Kirchhofer, D.1    Peek, M.2    Lipari, M.T.3    Billeci, K.4    Fan, B.5    Moran, P.6
  • 122
    • 34250220661 scopus 로고    scopus 로고
    • Prostasin induces protease-dependent and independent molecular changes in the human prostate carcinoma cell line PC-3
    • Chen, M., Fu, Y. Y., Lin, C. Y., Chen, L. M. and Chai, K. X. (2007) Prostasin induces protease-dependent and independent molecular changes in the human prostate carcinoma cell line PC-3. Biochim. Biophys. Acta 1773, 1133-1140
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1133-1140
    • Chen, M.1    Fu, Y.Y.2    Lin, C.Y.3    Chen, L.M.4    Chai, K.X.5
  • 123
    • 41949136687 scopus 로고    scopus 로고
    • The epidermal growth factor receptor (EGFR) is proteolytically modified by the matriptase-prostasin serine protease cascade in cultured epithelial cells
    • Chen, M., Chen, L. M., Lin, C. Y. and Chai, K. X. (2008) The epidermal growth factor receptor (EGFR) is proteolytically modified by the matriptase-prostasin serine protease cascade in cultured epithelial cells. Biochim. Biophys. Acta 1783, 896-903
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 896-903
    • Chen, M.1    Chen, L.M.2    Lin, C.Y.3    Chai, K.X.4
  • 124
    • 77949657431 scopus 로고    scopus 로고
    • Hepsin activates prostasin and cleaves the extracellular domain of the epidermal growth factor receptor
    • Chen, M., Chen, L. M., Lin, C. Y. and Chai, K. X. (2010) Hepsin activates prostasin and cleaves the extracellular domain of the epidermal growth factor receptor. Mol. Cell. Biochem. 337, 259-266
    • (2010) Mol. Cell. Biochem. , vol.337 , pp. 259-266
    • Chen, M.1    Chen, L.M.2    Lin, C.Y.3    Chai, K.X.4
  • 125
    • 38449087787 scopus 로고    scopus 로고
    • MT-SP1 proteolysis and regulation of cell-microenvironment interactions
    • Darragh, M. R., Bhatt, A. S. and Craik, C. S. (2008) MT-SP1 proteolysis and regulation of cell-microenvironment interactions. Front. Biosci. 13, 528-539
    • (2008) Front. Biosci. , vol.13 , pp. 528-539
    • Darragh, M.R.1    Bhatt, A.S.2    Craik, C.S.3
  • 126
    • 37549001403 scopus 로고    scopus 로고
    • Corin is co-expressed with pro-ANP and localized on the cardiomyocyte surface in both zymogen and catalytically active forms
    • Gladysheva, I. P., Robinson, B. R., Houng, A. K., Kovats, T. and King, S. M. (2008) Corin is co-expressed with pro-ANP and localized on the cardiomyocyte surface in both zymogen and catalytically active forms. J. Mol. Cell Cardiol. 44, 131-142
    • (2008) J. Mol. Cell Cardiol. , vol.44 , pp. 131-142
    • Gladysheva, I.P.1    Robinson, B.R.2    Houng, A.K.3    Kovats, T.4    King, S.M.5
  • 127
    • 0034682466 scopus 로고    scopus 로고
    • Corin, a transmembrane cardiac serine protease, acts as a pro-atrial natriuretic peptide-converting enzyme
    • Yan, W., Wu, F., Morser, J. and Wu, Q. (2000) Corin, a transmembrane cardiac serine protease, acts as a pro-atrial natriuretic peptide-converting enzyme. Proc. Natl. Acad. Sci. U.S.A. 97, 8525-8529
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8525-8529
    • Yan, W.1    Wu, F.2    Morser, J.3    Wu, Q.4
  • 128
    • 0037053365 scopus 로고    scopus 로고
    • Processing of pro-atrial natriuretic peptide by corin in cardiac myocytes
    • Wu, F., Yan, W., Pan, J., Morser, J. and Wu, Q. (2002) Processing of pro-atrial natriuretic peptide by corin in cardiac myocytes. J. Biol. Chem. 277, 16900-16905
    • (2002) J. Biol. Chem. , vol.277 , pp. 16900-16905
    • Wu, F.1    Yan, W.2    Pan, J.3    Morser, J.4    Wu, Q.5
  • 129
    • 64149088495 scopus 로고    scopus 로고
    • Role of natriuretic peptide family in cardiovascular medicine
    • Das, B. B. and Solinger, R. (2009) Role of natriuretic peptide family in cardiovascular medicine. Cardiovasc. Hematol. Agents Med. Chem. 7, 29-42
    • (2009) Cardiovasc. Hematol. Agents Med. Chem. , vol.7 , pp. 29-42
    • Das, B.B.1    Solinger, R.2
  • 130
    • 34250358937 scopus 로고    scopus 로고
    • Natriuretic peptides and therapeutic applications
    • Lee, C. Y. and Burnett, Jr, J. C. (2007) Natriuretic peptides and therapeutic applications. Heart Fail. Rev. 12, 131-142
    • (2007) Heart Fail. Rev. , vol.12 , pp. 131-142
    • Lee, C.Y.1    Burnett Jr., J.C.2
  • 131
    • 14144253541 scopus 로고    scopus 로고
    • Hypertension in mice lacking the proatrial natriuretic peptide convertase corin
    • Chan, J. C., Knudson, O., Wu, F., Morser, J., Dole, W. P. and Wu, Q. (2005) Hypertension in mice lacking the proatrial natriuretic peptide convertase corin. Proc. Natl. Acad. Sci. U.S.A. 102, 785-790
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 785-790
    • Chan, J.C.1    Knudson, O.2    Wu, F.3    Morser, J.4    Dole, W.P.5    Wu, Q.6
  • 133
    • 0037150210 scopus 로고    scopus 로고
    • B-type natriuretic peptide predicts sudden death in patients with chronic heart failure
    • Berger, R., Huelsman, M., Strecker, K., Bojic, A., Moser, P., Stanek, B. and Pacher, R. (2002) B-type natriuretic peptide predicts sudden death in patients with chronic heart failure. Circulation 105, 2392-2397
    • (2002) Circulation , vol.105 , pp. 2392-2397
    • Berger, R.1    Huelsman, M.2    Strecker, K.3    Bojic, A.4    Moser, P.5    Stanek, B.6    Pacher, R.7
  • 135
    • 77953668737 scopus 로고    scopus 로고
    • Dysfunctional corin I555(P568) allele is associated with impaired brain natriuretic peptide processing and adverse outcomes in blacks with systolic heart failure: Results from the genetic risk assessment in heart failure substudy
    • Rame, J. E., Tam, S. W., McNamara, D., Worcel, M., Sabolinski, M. L., Wu, A. H. and Dries, D. L. (2009) Dysfunctional corin I555(P568) allele is associated with impaired brain natriuretic peptide processing and adverse outcomes in blacks with systolic heart failure: results from the genetic risk assessment in heart failure substudy. Circ. Heart Fail. 2, 541-548
    • (2009) Circ. Heart Fail. , vol.2 , pp. 541-548
    • Rame, J.E.1    Tam, S.W.2    McNamara, D.3    Worcel, M.4    Sabolinski, M.L.5    Wu, A.H.6    Dries, D.L.7
  • 136
    • 0036023427 scopus 로고    scopus 로고
    • Synergistic activation of ENaC by three membrane-bound channel-activating serine proteases (mCAP1, mCAP2, and mCAP3) and serum- and glucocorticoid- regulated kinase (Sgk1) in Xenopus oocytes
    • Vuagniaux, G., Vallet, V., Jaeger, N. F., Hummler, E. and Rossier, B. C. (2002) Synergistic activation of ENaC by three membrane-bound channel-activating serine proteases (mCAP1, mCAP2, and mCAP3) and serum- and glucocorticoid- regulated kinase (Sgk1) in Xenopus oocytes. J. Gen. Physiol. 120, 191-201
    • (2002) J. Gen. Physiol. , vol.120 , pp. 191-201
    • Vuagniaux, G.1    Vallet, V.2    Jaeger, N.F.3    Hummler, E.4    Rossier, B.C.5
  • 137
    • 68949094195 scopus 로고    scopus 로고
    • ENaC at the cutting edge: Regulation of epithelial sodium channels by proteases
    • Kleyman, T. R., Carattino, M. D. and Hughey, R. P. (2009) ENaC at the cutting edge: regulation of epithelial sodium channels by proteases. J. Biol. Chem. 284, 20447-20451
    • (2009) J. Biol. Chem. , vol.284 , pp. 20447-20451
    • Kleyman, T.R.1    Carattino, M.D.2    Hughey, R.P.3
  • 140
    • 5444262302 scopus 로고    scopus 로고
    • Prostasin, a membrane-anchored serine peptidase, regulates sodium currents in JME/CF15 cells, a cystic fibrosis airway epithelial cell line
    • Tong, Z., Illek, B., Bhagwandin, V. J., Verghese, G. M. and Caughey, G. H. (2004) Prostasin, a membrane-anchored serine peptidase, regulates sodium currents in JME/CF15 cells, a cystic fibrosis airway epithelial cell line. Am. J. Physiol. Lung Cell. Mol. Physiol. 287, L928-L935
    • (2004) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.287
    • Tong, Z.1    Illek, B.2    Bhagwandin, V.J.3    Verghese, G.M.4    Caughey, G.H.5
  • 142
    • 54449088865 scopus 로고    scopus 로고
    • Proteolytic processing of the epithelial sodium channel gamma subunit has a dominant role in channel activation
    • Carattino, M. D., Hughey, R. P. and Kleyman, T. R. (2008) Proteolytic processing of the epithelial sodium channel gamma subunit has a dominant role in channel activation. J. Biol. Chem. 283, 25290-25295
    • (2008) J. Biol. Chem. , vol.283 , pp. 25290-25295
    • Carattino, M.D.1    Hughey, R.P.2    Kleyman, T.R.3
  • 144
    • 0036191884 scopus 로고    scopus 로고
    • Cell-surface expression of the channel activating protease xCAP-1 is required for activation of ENaC in the Xenopus oocyte
    • Vallet, V., Pfister, C., Loffing, J. and Rossier, B. C. (2002) Cell-surface expression of the channel activating protease xCAP-1 is required for activation of ENaC in the Xenopus oocyte. J. Am. Soc. Nephrol. 13, 588-594
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 588-594
    • Vallet, V.1    Pfister, C.2    Loffing, J.3    Rossier, B.C.4
  • 145
    • 59449104675 scopus 로고    scopus 로고
    • ENaC proteolytic regulation by channel-activating protease 2
    • Garcia-Caballero, A., Dang, Y., He, H. and Stutts, M. J. (2008) ENaC proteolytic regulation by channel-activating protease 2. J. Gen. Physiol. 132, 521-535
    • (2008) J. Gen. Physiol. , vol.132 , pp. 521-535
    • Garcia-Caballero, A.1    Dang, Y.2    He, H.3    Stutts, M.J.4
  • 148
    • 36348979793 scopus 로고    scopus 로고
    • Sodium channels and cystic fibrosis
    • Donaldson, S. H. and Boucher, R. C. (2007) Sodium channels and cystic fibrosis. Chest 132, 1631-1636
    • (2007) Chest , vol.132 , pp. 1631-1636
    • Donaldson, S.H.1    Boucher, R.C.2
  • 150
    • 0033051605 scopus 로고    scopus 로고
    • Implication of ENaC in salt-sensitive hypertension
    • Hummler, E. (1999) Implication of ENaC in salt-sensitive hypertension. J. Steroid Biochem. Mol. Biol. 69, 385-390
    • (1999) J. Steroid Biochem. Mol. Biol. , vol.69 , pp. 385-390
    • Hummler, E.1
  • 152
    • 58849147112 scopus 로고    scopus 로고
    • Camostat mesilate inhibits prostasin activity and reduces blood pressure and renal injury in salt-sensitive hypertension
    • Maekawa, A., Kakizoe, Y., Miyoshi, T., Wakida, N., Ko, T., Shiraishi, N., Adachi, M., Tomita, K. and Kitamura, K. (2009) Camostat mesilate inhibits prostasin activity and reduces blood pressure and renal injury in salt-sensitive hypertension. J. Hypertens. 27, 181-189
    • (2009) J. Hypertens. , vol.27 , pp. 181-189
    • Maekawa, A.1    Kakizoe, Y.2    Miyoshi, T.3    Wakida, N.4    Ko, T.5    Shiraishi, N.6    Adachi, M.7    Tomita, K.8    Kitamura, K.9
  • 153
    • 56449096622 scopus 로고    scopus 로고
    • The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin
    • Silvestri, L., Pagani, A., Nai, A., De, D., I, Kaplan, J. and Camaschella, C. (2008) The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin. Cell Metab. 8, 502-511
    • (2008) Cell Metab. , vol.8 , pp. 502-511
    • Silvestri, L.1    Pagani, A.2    Nai, A.3    De, D.I.4    Kaplan, J.5    Camaschella, C.6
  • 155
    • 52649096861 scopus 로고    scopus 로고
    • Two nonsense mutations in the TMPRSS6 gene in a patient with microcytic anemia and iron deficiency
    • Guillem, F., Lawson, S., Kannengiesser, C., Westerman, M., Beaumont, C. and Grandchamp, B. (2008) Two nonsense mutations in the TMPRSS6 gene in a patient with microcytic anemia and iron deficiency. Blood 112, 2089-2091
    • (2008) Blood , vol.112 , pp. 2089-2091
    • Guillem, F.1    Lawson, S.2    Kannengiesser, C.3    Westerman, M.4    Beaumont, C.5    Grandchamp, B.6
  • 156
    • 54349094273 scopus 로고    scopus 로고
    • A mutation in the TMPRSS6 gene, encoding a transmembrane serine protease that suppresses hepcidin production, in familial iron deficiency anemia refractory to oral iron
    • Melis, M. A., Cau, M., Congiu, R., Sole, G., Barella, S., Cao, A., Westerman, M., Cazzola, M. and Galanello, R. (2008) A mutation in the TMPRSS6 gene, encoding a transmembrane serine protease that suppresses hepcidin production, in familial iron deficiency anemia refractory to oral iron. Haematologica 93, 1473-1479
    • (2008) Haematologica , vol.93 , pp. 1473-1479
    • Melis, M.A.1    Cau, M.2    Congiu, R.3    Sole, G.4    Barella, S.5    Cao, A.6    Westerman, M.7    Cazzola, M.8    Galanello, R.9
  • 158
    • 70350482508 scopus 로고    scopus 로고
    • Suppression of the hepcidin-encoding gene Hamp permits iron overload in mice lacking both hemojuvelin and matriptase-2/TMPRSS6
    • Truksa, J., Gelbart, T., Peng, H., Beutler, E., Beutler, B. and Lee, P. (2009) Suppression of the hepcidin-encoding gene Hamp permits iron overload in mice lacking both hemojuvelin and matriptase-2/TMPRSS6. Br. J. Haematol. 147, 571-581
    • (2009) Br. J. Haematol. , vol.147 , pp. 571-581
    • Truksa, J.1    Gelbart, T.2    Peng, H.3    Beutler, E.4    Beutler, B.5    Lee, P.6
  • 159
    • 34447137331 scopus 로고    scopus 로고
    • Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance
    • Babitt, J. L., Huang, F. W., Xia, Y., Sidis, Y., Andrews, N. C. and Lin, H. Y. (2007) Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance. J. Clin. Invest. 117, 1933-1939
    • (2007) J. Clin. Invest. , vol.117 , pp. 1933-1939
    • Babitt, J.L.1    Huang, F.W.2    Xia, Y.3    Sidis, Y.4    Andrews, N.C.5    Lin, H.Y.6
  • 160
    • 67650079412 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases in cancer and viral infections
    • Choi, S. Y., Bertram, S., Glowacka, I., Park, Y. W. and Pohlmann, S. (2009) Type II transmembrane serine proteases in cancer and viral infections. Trends Mol. Med. 15, 303-312
    • (2009) Trends Mol. Med. , vol.15 , pp. 303-312
    • Choi, S.Y.1    Bertram, S.2    Glowacka, I.3    Park, Y.W.4    Pohlmann, S.5
  • 161
    • 70449578473 scopus 로고    scopus 로고
    • Host envelope glycoprotein processing proteases are indispensable for entry into human cells by seasonal and highly pathogenic avian influenza viruses
    • Kido, H., Okumura, Y., Takahashi, E., Pan, H. Y., Wang, S., Chida, J., Le, T. Q. and Yano, M. (2008) Host envelope glycoprotein processing proteases are indispensable for entry into human cells by seasonal and highly pathogenic avian influenza viruses. J. Mol. Genet. Med. 3, 167-175
    • (2008) J. Mol. Genet. Med. , vol.3 , pp. 167-175
    • Kido, H.1    Okumura, Y.2    Takahashi, E.3    Pan, H.Y.4    Wang, S.5    Chida, J.6    Le, T.Q.7    Yano, M.8
  • 162
    • 33748950305 scopus 로고    scopus 로고
    • Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium
    • Bottcher, E., Matrosovich, T., Beyerle, M., Klenk, H. D., Garten, W. and Matrosovich, M. (2006) Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium. J. Virol. 80, 9896-9898
    • (2006) J. Virol. , vol.80 , pp. 9896-9898
    • Bottcher, E.1    Matrosovich, T.2    Beyerle, M.3    Klenk, H.D.4    Garten, W.5    Matrosovich, M.6
  • 163
    • 68049130941 scopus 로고    scopus 로고
    • MDCK cells that express proteases TMPRSS2 and HAT provide a cell system to propagate influenza viruses in the absence of trypsin and to study cleavage of HA and its inhibition
    • Bottcher, E., Freuer, C., Steinmetzer, T., Klenk, H. D. and Garten, W. (2009) MDCK cells that express proteases TMPRSS2 and HAT provide a cell system to propagate influenza viruses in the absence of trypsin and to study cleavage of HA and its inhibition. Vaccine 27, 6324-6329
    • (2009) Vaccine , vol.27 , pp. 6324-6329
    • Bottcher, E.1    Freuer, C.2    Steinmetzer, T.3    Klenk, H.D.4    Garten, W.5
  • 165
    • 50149096147 scopus 로고    scopus 로고
    • Efficient multiplication of human metapneumovirus in Vero cells expressing the transmembrane serine protease TMPRSS2
    • Shirogane, Y., Takeda, M., Iwasaki, M., Ishiguro, N., Takeuchi, H., Nakatsu, Y., Tahara, M., Kikuta, H. and Yanagi, Y. (2008) Efficient multiplication of human metapneumovirus in Vero cells expressing the transmembrane serine protease TMPRSS2. J. Virol. 82, 8942-8946
    • (2008) J. Virol. , vol.82 , pp. 8942-8946
    • Shirogane, Y.1    Takeda, M.2    Iwasaki, M.3    Ishiguro, N.4    Takeuchi, H.5    Nakatsu, Y.6    Tahara, M.7    Kikuta, H.8    Yanagi, Y.9
  • 166
    • 17644383750 scopus 로고    scopus 로고
    • Human hepatitis B virus X protein promotes cell proliferation and inhibits cell apoptosis through interacting with a serine protease hepsin
    • Zhang, J. L., Zhao, W. G., Wu, K. L., Wang, K., Zhang, X., Gu, C. F., Li, Y., Zhu, Y. and Wu, J. G. (2005) Human hepatitis B virus X protein promotes cell proliferation and inhibits cell apoptosis through interacting with a serine protease hepsin. Arch. Virol. 150, 721-741
    • (2005) Arch. Virol. , vol.150 , pp. 721-741
    • Zhang, J.L.1    Zhao, W.G.2    Wu, K.L.3    Wang, K.4    Zhang, X.5    Gu, C.F.6    Li, Y.7    Zhu, Y.8    Wu, J.G.9
  • 167
    • 70949093997 scopus 로고    scopus 로고
    • Cleavage of the SARS coronavirus spike glycoprotein by airway proteases enhances virus entry into human bronchial epithelial cells in vitro
    • Kam, Y. W., Okumura, Y., Kido, H., Ng, L. F., Bruzzone, R. and Altmeyer, R. (2009) Cleavage of the SARS coronavirus spike glycoprotein by airway proteases enhances virus entry into human bronchial epithelial cells in vitro. PLoS ONE 4, e7870
    • (2009) PLoS ONE , vol.4
    • Kam, Y.W.1    Okumura, Y.2    Kido, H.3    Ng, L.F.4    Bruzzone, R.5    Altmeyer, R.6
  • 168
    • 0037161955 scopus 로고    scopus 로고
    • Matriptase/MT-SP1 is required for postnatal survival, epidermal barrier function, hair follicle development, and thymic homeostasis
    • List, K., Haudenschild, C. C., Szabo, R., Chen, W., Wahl, S. M., Swaim, W., Engelholm, L. H., Behrendt, N. and Bugge, T. H. (2002) Matriptase/MT-SP1 is required for postnatal survival, epidermal barrier function, hair follicle development, and thymic homeostasis. Oncogene 21, 3765-3779
    • (2002) Oncogene , vol.21 , pp. 3765-3779
    • List, K.1    Haudenschild, C.C.2    Szabo, R.3    Chen, W.4    Wahl, S.M.5    Swaim, W.6    Engelholm, L.H.7    Behrendt, N.8    Bugge, T.H.9
  • 169
    • 0345166962 scopus 로고    scopus 로고
    • Loss of proteolytically processed filaggrin caused by epidermal deletion of matriptase/MT-SP1
    • List, K., Szabo, R., Wertz, P. W., Segre, J., Haudenschild, C. C., Kim, S. Y. and Bugge, T. H. (2003) Loss of proteolytically processed filaggrin caused by epidermal deletion of matriptase/MT-SP1. J. Cell Biol. 163, 901-910
    • (2003) J. Cell Biol. , vol.163 , pp. 901-910
    • List, K.1    Szabo, R.2    Wertz, P.W.3    Segre, J.4    Haudenschild, C.C.5    Kim, S.Y.6    Bugge, T.H.7
  • 172
    • 37549057380 scopus 로고    scopus 로고
    • Autosomal ichthyosis with hypotrichosis syndrome displays low matriptase proteolytic activity and is phenocopied in ST14 hypomorphic mice
    • List, K., Currie, B., Scharschmidt, T. C., Szabo, R., Shireman, J., Molinolo, A., Cravatt, B. F., Segre, J. and Bugge, T. H. (2007) Autosomal ichthyosis with hypotrichosis syndrome displays low matriptase proteolytic activity and is phenocopied in ST14 hypomorphic mice. J. Biol. Chem. 282, 36714-36723
    • (2007) J. Biol. Chem. , vol.282 , pp. 36714-36723
    • List, K.1    Currie, B.2    Scharschmidt, T.C.3    Szabo, R.4    Shireman, J.5    Molinolo, A.6    Cravatt, B.F.7    Segre, J.8    Bugge, T.H.9
  • 173
    • 63149177512 scopus 로고    scopus 로고
    • Ichthyosis, follicular atrophoderma, and hypotrichosis caused by mutations in ST14 is associated with impaired profilaggrin processing
    • Alef, T., Torres, S., Hausser, I., Metze, D., Tursen, U., Lestringant, G. G. and Hennies, H. C. (2009) Ichthyosis, follicular atrophoderma, and hypotrichosis caused by mutations in ST14 is associated with impaired profilaggrin processing. J. Invest. Dermatol. 129, 862-869
    • (2009) J. Invest. Dermatol. , vol.129 , pp. 862-869
    • Alef, T.1    Torres, S.2    Hausser, I.3    Metze, D.4    Tursen, U.5    Lestringant, G.G.6    Hennies, H.C.7
  • 174
    • 73549091040 scopus 로고    scopus 로고
    • Epithelial integrity is maintained by a matriptase-dependent proteolytic pathway
    • List, K., Kosa, P., Szabo, R., Bey, A. L., Wang, C. B., Molinolo, A. and Bugge, T. H. (2009) Epithelial integrity is maintained by a matriptase-dependent proteolytic pathway. Am. J. Pathol. 175, 1453-1463
    • (2009) Am. J. Pathol. , vol.175 , pp. 1453-1463
    • List, K.1    Kosa, P.2    Szabo, R.3    Bey, A.L.4    Wang, C.B.5    Molinolo, A.6    Bugge, T.H.7
  • 175
    • 38449107595 scopus 로고    scopus 로고
    • TMPRSS3, a type II transmembrane serine protease mutated in non-syndromic autosomal recessive deafness
    • Guipponi, M., Antonarakis, S. E. and Scott, H. S. (2008) TMPRSS3, a type II transmembrane serine protease mutated in non-syndromic autosomal recessive deafness. Front. Biosci. 13, 1557-1567
    • (2008) Front. Biosci. , vol.13 , pp. 1557-1567
    • Guipponi, M.1    Antonarakis, S.E.2    Scott, H.S.3
  • 176
    • 0035167046 scopus 로고    scopus 로고
    • Insertion of beta-satellite repeats identifies a transmembrane protease causing both congenital and childhood onset autosomal recessive deafness
    • Scott, H. S., Kudoh, J., Wattenhofer, M., Shibuya, K., Berry, A., Chrast, R., Guipponi, M., Wang, J., Kawasaki, K., Asakawa, S. et al. (2001) Insertion of beta-satellite repeats identifies a transmembrane protease causing both congenital and childhood onset autosomal recessive deafness. Nat. Genet. 27, 59-63
    • (2001) Nat. Genet. , vol.27 , pp. 59-63
    • Scott, H.S.1    Kudoh, J.2    Wattenhofer, M.3    Shibuya, K.4    Berry, A.5    Chrast, R.6    Guipponi, M.7    Wang, J.8    Kawasaki, K.9    Asakawa, S.10
  • 177
    • 0042327815 scopus 로고    scopus 로고
    • Pathogenic mutations but not polymorphisms in congenital and childhood onset autosomal recessive deafness disrupt the proteolytic activity of TMPRSS3
    • Lee, Y. J., Park, D., Kim, S. Y. and Park, W. J. (2003) Pathogenic mutations but not polymorphisms in congenital and childhood onset autosomal recessive deafness disrupt the proteolytic activity of TMPRSS3. J. Med. Genet. 40, 629-631
    • (2003) J. Med. Genet. , vol.40 , pp. 629-631
    • Lee, Y.J.1    Park, D.2    Kim, S.Y.3    Park, W.J.4
  • 180
  • 181
    • 56049087354 scopus 로고    scopus 로고
    • Reduced fertility of mouse epididymal sperm lacking Prss21/Tesp5 is rescued by sperm exposure to uterine microenvironment
    • Yamashita, M., Honda, A., Ogura, A., Kashiwabara, S., Fukami, K. and Baba, T. (2008) Reduced fertility of mouse epididymal sperm lacking Prss21/Tesp5 is rescued by sperm exposure to uterine microenvironment. Genes Cells 13, 1001-1013
    • (2008) Genes Cells , vol.13 , pp. 1001-1013
    • Yamashita, M.1    Honda, A.2    Ogura, A.3    Kashiwabara, S.4    Fukami, K.5    Baba, T.6
  • 182
    • 38949212164 scopus 로고    scopus 로고
    • The serine protease corin is a novel modifier of the Agouti pathway
    • Enshell-Seijffers, D., Lindon, C. and Morgan, B. A. (2008) The serine protease corin is a novel modifier of the Agouti pathway. Development 135, 217-225
    • (2008) Development , vol.135 , pp. 217-225
    • Enshell-Seijffers, D.1    Lindon, C.2    Morgan, B.A.3
  • 183
    • 33947164004 scopus 로고    scopus 로고
    • Matriptase inhibition by hepatocyte growth factor activator inhibitor-1 is essential for placental development
    • Szabo, R., Molinolo, A., List, K. and Bugge, T. H. (2007) Matriptase inhibition by hepatocyte growth factor activator inhibitor-1 is essential for placental development. Oncogene 26, 1546-1556
    • (2007) Oncogene , vol.26 , pp. 1546-1556
    • Szabo, R.1    Molinolo, A.2    List, K.3    Bugge, T.H.4
  • 186
    • 0037053318 scopus 로고    scopus 로고
    • Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding β1-6 GlcNAc branching
    • Ihara, S., Miyoshi, E., Ko, J. H., Murata, K., Nakahara, S., Honke, K., Dickson, R. B., Lin, C. Y. and Taniguchi, N. (2002) Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding β1-6 GlcNAc branching. J. Biol. Chem. 277, 16960-16967
    • (2002) J. Biol. Chem. , vol.277 , pp. 16960-16967
    • Ihara, S.1    Miyoshi, E.2    Ko, J.H.3    Murata, K.4    Nakahara, S.5    Honke, K.6    Dickson, R.B.7    Lin, C.Y.8    Taniguchi, N.9
  • 187
    • 42249086794 scopus 로고    scopus 로고
    • TMPRSS4 promotes invasion, migration and metastasis of human tumor cells by facilitating an epithelial-mesenchymal transition
    • Jung, H., Lee, K. P., Park, S. J., Park, J. H., Jang, Y. S., Choi, S. Y., Jung, J. G., Jo, K., Park, D. Y., Yoon, J. H. et al. (2008) TMPRSS4 promotes invasion, migration and metastasis of human tumor cells by facilitating an epithelial-mesenchymal transition. Oncogene 27, 2635-2647
    • (2008) Oncogene , vol.27 , pp. 2635-2647
    • Jung, H.1    Lee, K.P.2    Park, S.J.3    Park, J.H.4    Jang, Y.S.5    Choi, S.Y.6    Jung, J.G.7    Jo, K.8    Park, D.Y.9    Yoon, J.H.10
  • 190
    • 48749092358 scopus 로고    scopus 로고
    • Genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitroand in vivoand affects FAK and paxillin localisation
    • Sanders, A. J., Parr, C., Martin, T. A., Lane, J., Mason, M. D. and Jiang, W. G. (2008) Genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitroand in vivoand affects FAK and paxillin localisation. J. Cell Physiol. 216, 780-789
    • (2008) J. Cell Physiol. , vol.216 , pp. 780-789
    • Sanders, A.J.1    Parr, C.2    Martin, T.A.3    Lane, J.4    Mason, M.D.5    Jiang, W.G.6
  • 191
    • 34250777391 scopus 로고    scopus 로고
    • Matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients
    • Parr, C., Sanders, A. J., Davies, G., Martin, T., Lane, J., Mason, M. D., Mansel, R. E. and Jiang, W. G. (2007) Matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients. Clin. Cancer Res. 13, 3568-3576
    • (2007) Clin. Cancer Res. , vol.13 , pp. 3568-3576
    • Parr, C.1    Sanders, A.J.2    Davies, G.3    Martin, T.4    Lane, J.5    Mason, M.D.6    Mansel, R.E.7    Jiang, W.G.8
  • 192
    • 0035147418 scopus 로고    scopus 로고
    • Differential expression of a novel serine protease homologue in squamous cell carcinoma of the head and neck
    • Lang, J. C. and Schuller, D. E. (2001) Differential expression of a novel serine protease homologue in squamous cell carcinoma of the head and neck. Br. J. Cancer 84, 237-243
    • (2001) Br. J. Cancer , vol.84 , pp. 237-243
    • Lang, J.C.1    Schuller, D.E.2
  • 194
    • 13444263249 scopus 로고    scopus 로고
    • Testisin, a glycosyl-phosphatidylinositol-linked serine protease, promotes malignant transformation in vitro and in vivo
    • Tang, T., Kmet, M., Corral, L., Vartanian, S., Tobler, A. and Papkoff, J. (2005) Testisin, a glycosyl-phosphatidylinositol-linked serine protease, promotes malignant transformation in vitroand in vivo. Cancer Res. 65, 868-878 (Pubitemid 40216446)
    • (2005) Cancer Research , vol.65 , Issue.3 , pp. 868-878
    • Tang, T.1    Kmet, M.2    Corral, L.3    Vartanian, S.4    Tobler, A.5    Papkoff, J.6
  • 195
    • 14944343729 scopus 로고    scopus 로고
    • Hypermethylation of the 5′ CpG island of the gene encoding the serine protease testisin promotes its loss in testicular tumorigenesis
    • Manton, K. J., Douglas, M. L., Netzel-Arnett, S., Fitzpatrick, D. R., Nicol, D. L., Boyd, A. W., Clements, J. A. and Antalis, T. M. (2005) Hypermethylation of the 5′ CpG island of the gene encoding the serine protease testisin promotes its loss in testicular tumorigenesis. Br. J. Cancer 92, 760-769
    • (2005) Br. J. Cancer , vol.92 , pp. 760-769
    • Manton, K.J.1    Douglas, M.L.2    Netzel-Arnett, S.3    Fitzpatrick, D.R.4    Nicol, D.L.5    Boyd, A.W.6    Clements, J.A.7    Antalis, T.M.8
  • 198
    • 57649155897 scopus 로고    scopus 로고
    • Laminin-332 is a substrate for hepsin, a protease associated with prostate cancer progression
    • Tripathi, M., Nandana, S., Yamashita, H., Ganesan, R., Kirchhofer, D. and Quaranta, V. (2008) Laminin-332 is a substrate for hepsin, a protease associated with prostate cancer progression. J. Biol. Chem. 283, 30576-30584
    • (2008) J. Biol. Chem. , vol.283 , pp. 30576-30584
    • Tripathi, M.1    Nandana, S.2    Yamashita, H.3    Ganesan, R.4    Kirchhofer, D.5    Quaranta, V.6
  • 199
    • 0035823595 scopus 로고    scopus 로고
    • The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
    • Silverman, G. A., Bird, P. I., Carrell, R. W., Church, F. C., Coughlin, P. B., Gettins, P. G., Irving, J. A., Lomas, D. A., Luke, C. J., Moyer, R. W. et al. (2001) The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J. Biol. Chem. 276, 33293-33296
    • (2001) J. Biol. Chem. , vol.276 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3    Church, F.C.4    Coughlin, P.B.5    Gettins, P.G.6    Irving, J.A.7    Lomas, D.A.8    Luke, C.J.9    Moyer, R.W.10
  • 200
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P. G. (2002) Serpin structure, mechanism, and function. Chem. Rev. 102, 4751-4804
    • (2002) Chem. Rev. , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 201
    • 0034836428 scopus 로고    scopus 로고
    • LRP: A multifunctional scavenger and signaling receptor
    • Herz, J. and Strickland, D. K. (2001) LRP: a multifunctional scavenger and signaling receptor. J. Clin. Invest 108, 779-784
    • (2001) J. Clin. Invest , vol.108 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 203
    • 23944450595 scopus 로고    scopus 로고
    • Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity
    • Szabo, R., Netzel-Arnett, S., Hobson, J. P., Antalis, T. M. and Bugge, T. H. (2005) Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity. Biochem. J. 390, 231-242
    • (2005) Biochem. J. , vol.390 , pp. 231-242
    • Szabo, R.1    Netzel-Arnett, S.2    Hobson, J.P.3    Antalis, T.M.4    Bugge, T.H.5
  • 205
    • 27144432513 scopus 로고    scopus 로고
    • Identification of hepatocyte growth factor activator inhibitor-1B as a potential physiological inhibitor of prostasin
    • Fan, B., Wu, T. D., Li, W. and Kirchhofer, D. (2005) Identification of hepatocyte growth factor activator inhibitor-1B as a potential physiological inhibitor of prostasin. J. Biol. Chem. 280, 34513-34520
    • (2005) J. Biol. Chem. , vol.280 , pp. 34513-34520
    • Fan, B.1    Wu, T.D.2    Li, W.3    Kirchhofer, D.4
  • 206
    • 0033603574 scopus 로고    scopus 로고
    • Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity
    • Lin, C. Y., Anders, J., Johnson, M., Sang, Q. A. and Dickson, R. B. (1999) Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity. J. Biol. Chem. 274, 18231-18236
    • (1999) J. Biol. Chem. , vol.274 , pp. 18231-18236
    • Lin, C.Y.1    Anders, J.2    Johnson, M.3    Sang, Q.A.4    Dickson, R.B.5
  • 208
    • 41449107352 scopus 로고    scopus 로고
    • Roles of functional and structural domains of hepatocyte growth factor activator inhibitor type 1 in the inhibition of matriptase
    • Kojima, K., Tsuzuki, S., Fushiki, T. and Inouye, K. (2008) Roles of functional and structural domains of hepatocyte growth factor activator inhibitor type 1 in the inhibition of matriptase. J. Biol. Chem. 283, 2478-2487
    • (2008) J. Biol. Chem. , vol.283 , pp. 2478-2487
    • Kojima, K.1    Tsuzuki, S.2    Fushiki, T.3    Inouye, K.4
  • 209
    • 67049144594 scopus 로고    scopus 로고
    • Loss of matriptase suppression underlies spint1 mutation-associated ichthyosis and postnatal lethality
    • Szabo, R., Kosa, P., List, K. and Bugge, T. H. (2009) Loss of matriptase suppression underlies spint1 mutation-associated ichthyosis and postnatal lethality. Am. J. Pathol. 174, 2015-2022
    • (2009) Am. J. Pathol. , vol.174 , pp. 2015-2022
    • Szabo, R.1    Kosa, P.2    List, K.3    Bugge, T.H.4
  • 210
    • 55349099521 scopus 로고    scopus 로고
    • Defect of hepatocyte growth factor activator inhibitor type 1/serine protease inhibitor, Kunitz type 1 (Hai-1/Spint1) leads to ichthyosis-like condition and abnormal hair development in mice
    • Nagaike, K., Kawaguchi, M., Takeda, N., Fukushima, T., Sawaguchi, A., Kohama, K., Setoyama, M. and Kataoka, H. (2008) Defect of hepatocyte growth factor activator inhibitor type 1/serine protease inhibitor, Kunitz type 1 (Hai-1/Spint1) leads to ichthyosis-like condition and abnormal hair development in mice. Am. J. Pathol. 173, 1464-1475
    • (2008) Am. J. Pathol. , vol.173 , pp. 1464-1475
    • Nagaike, K.1    Kawaguchi, M.2    Takeda, N.3    Fukushima, T.4    Sawaguchi, A.5    Kohama, K.6    Setoyama, M.7    Kataoka, H.8
  • 211
    • 57649183234 scopus 로고    scopus 로고
    • Potent inhibition and global co-localization implicate the transmembrane Kunitz-type serine protease inhibitor hepatocyte growth factor activator inhibitor-2 in the regulation of epithelial matriptase activity
    • Szabo, R., Hobson, J. P., List, K., Molinolo, A., Lin, C. Y. and Bugge, T. H. (2008) Potent inhibition and global co-localization implicate the transmembrane Kunitz-type serine protease inhibitor hepatocyte growth factor activator inhibitor-2 in the regulation of epithelial matriptase activity. J. Biol. Chem. 283, 29495-29504
    • (2008) J. Biol. Chem. , vol.283 , pp. 29495-29504
    • Szabo, R.1    Hobson, J.P.2    List, K.3    Molinolo, A.4    Lin, C.Y.5    Bugge, T.H.6
  • 213
    • 69049092775 scopus 로고    scopus 로고
    • Regulation of cell surface protease matriptase by HAI2 is essential for placental development, neural tube closure and embryonic survival in mice
    • Szabo, R., Hobson, J. P., Christoph, K., Kosa, P., List, K. and Bugge, T. H. (2009) Regulation of cell surface protease matriptase by HAI2 is essential for placental development, neural tube closure and embryonic survival in mice. Development 136, 2653-2663
    • (2009) Development , vol.136 , pp. 2653-2663
    • Szabo, R.1    Hobson, J.P.2    Christoph, K.3    Kosa, P.4    List, K.5    Bugge, T.H.6
  • 214
    • 0031552052 scopus 로고    scopus 로고
    • Purification and characterization of hepsin from rat liver microsomes
    • Zhukov, A., Hellman, U. and Ingelman-Sundberg, M. (1997) Purification and characterization of hepsin from rat liver microsomes. Biochim. Biophys. Acta 1337, 85-95
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 85-95
    • Zhukov, A.1    Hellman, U.2    Ingelman-Sundberg, M.3
  • 215
    • 0042861481 scopus 로고    scopus 로고
    • Engineering of a macromolecular scaffold to develop specific protease inhibitors
    • Stoop, A. A. and Craik, C. S. (2003) Engineering of a macromolecular scaffold to develop specific protease inhibitors. Nat. Biotechnol. 21, 1063-1068
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1063-1068
    • Stoop, A.A.1    Craik, C.S.2
  • 218
    • 5344230112 scopus 로고    scopus 로고
    • CVS-3983, a selective matriptase inhibitor, suppresses the growth of androgen independent prostate tumor xenografts
    • Galkin, A. V., Mullen, L., Fox, W. D., Brown, J., Duncan, D., Moreno, O., Madison, E. L. and Agus, D. B. (2004) CVS-3983, a selective matriptase inhibitor, suppresses the growth of androgen independent prostate tumor xenografts. Prostate 61, 228-235
    • (2004) Prostate , vol.61 , pp. 228-235
    • Galkin, A.V.1    Mullen, L.2    Fox, W.D.3    Brown, J.4    Duncan, D.5    Moreno, O.6    Madison, E.L.7    Agus, D.B.8
  • 220
    • 0036510530 scopus 로고    scopus 로고
    • Spinesin/TMPRSS5, a novel transmembrane serine protease, cloned from human spinal cord
    • Yamaguchi, N., Okui, A., Yamada, T., Nakazato, H. and Mitsui, S. (2002) Spinesin/TMPRSS5, a novel transmembrane serine protease, cloned from human spinal cord. J. Biol. Chem. 277, 6806-6812
    • (2002) J. Biol. Chem. , vol.277 , pp. 6806-6812
    • Yamaguchi, N.1    Okui, A.2    Yamada, T.3    Nakazato, H.4    Mitsui, S.5
  • 222
    • 11744372696 scopus 로고
    • Formation of trypsin from crystalline trypsinogen by means of enterokinase
    • Kunitz, M. (1939) Formation of trypsin from crystalline trypsinogen by means of enterokinase. J. Gen. Physiol. 22, 429-446
    • (1939) J. Gen. Physiol. , vol.22 , pp. 429-446
    • Kunitz, M.1
  • 224
    • 0037374303 scopus 로고    scopus 로고
    • Tissue microarray analysis of hepatocyte growth factor/Met pathway components reveals a role for Met, matriptase, and hepatocyte growth factor activator inhibitor 1 in the progression of node-negative breast cancer
    • Kang, J. Y., Dolled-Filhart, M., Ocal, I. T., Singh, B., Lin, C. Y., Dickson, R. B., Rimm, D. L. and Camp, R. L. (2003) Tissue microarray analysis of hepatocyte growth factor/Met pathway components reveals a role for Met, matriptase, and hepatocyte growth factor activator inhibitor 1 in the progression of node-negative breast cancer. Cancer Res. 63, 1101-1105
    • (2003) Cancer Res. , vol.63 , pp. 1101-1105
    • Kang, J.Y.1    Dolled-Filhart, M.2    Ocal, I.T.3    Singh, B.4    Lin, C.Y.5    Dickson, R.B.6    Rimm, D.L.7    Camp, R.L.8
  • 225
    • 1642535487 scopus 로고    scopus 로고
    • The hepatocyte growth factor regulatory factors in human breast cancer
    • Parr, C., Watkins, G., Mansel, R. E. and Jiang, W. G. (2004) The hepatocyte growth factor regulatory factors in human breast cancer. Clin. Cancer Res. 10, 202-211
    • (2004) Clin. Cancer Res. , vol.10 , pp. 202-211
    • Parr, C.1    Watkins, G.2    Mansel, R.E.3    Jiang, W.G.4
  • 227
    • 33644943049 scopus 로고    scopus 로고
    • Identification of membrane-bound serine proteinase matriptase as processing enzyme of insulin-like growth factor binding protein-related protein-1 (IGFBP-rP1/angiomodulin/mac25)
    • Ahmed, S., Jin, X., Yagi, M., Yasuda, C., Sato, Y., Higashi, S., Lin, C. Y., Dickson, R. B. and Miyazaki, K. (2006) Identification of membrane-bound serine proteinase matriptase as processing enzyme of insulin-like growth factor binding protein-related protein-1 (IGFBP-rP1/angiomodulin/mac25). FEBS J. 273, 615-627
    • (2006) FEBS J. , vol.273 , pp. 615-627
    • Ahmed, S.1    Jin, X.2    Yagi, M.3    Yasuda, C.4    Sato, Y.5    Higashi, S.6    Lin, C.Y.7    Dickson, R.B.8    Miyazaki, K.9
  • 228
    • 0346732305 scopus 로고    scopus 로고
    • Functional analysis of the transmembrane domain and activation cleavage of human cor design and characterization of a soluble corin
    • Knappe, S., Wu, F., Masikat, M. R., Morser, J. and Wu, Q. (2003) Functional analysis of the transmembrane domain and activation cleavage of human corin: design and characterization of a soluble corin. J. Biol. Chem. 278, 52363-52370
    • (2003) J. Biol. Chem. , vol.278 , pp. 52363-52370
    • Knappe, S.1    Wu, F.2    Masikat, M.R.3    Morser, J.4    Wu, Q.5
  • 231
    • 31344447481 scopus 로고    scopus 로고
    • Phenotypic analysis of mice lacking the Tmprss2-encoded protease
    • Kim, T. S., Heinlein, C., Hackman, R. C. and Nelson, P. S. (2006) Phenotypic analysis of mice lacking the Tmprss2-encoded protease. Mol. Cell. Biol. 26, 965-975
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 965-975
    • Kim, T.S.1    Heinlein, C.2    Hackman, R.C.3    Nelson, P.S.4
  • 232
    • 33646514271 scopus 로고    scopus 로고
    • Delineation of matriptase protein expression by enzymatic gene trapping suggests diverging roles in barrier function, hair formation, and squamous cell carcinogenesis
    • List, K., Szabo, R., Molinolo, A., Nielsen, B. S. and Bugge, T. H. (2006) Delineation of matriptase protein expression by enzymatic gene trapping suggests diverging roles in barrier function, hair formation, and squamous cell carcinogenesis. Am. J. Pathol. 168, 1513-1525
    • (2006) Am. J. Pathol. , vol.168 , pp. 1513-1525
    • List, K.1    Szabo, R.2    Molinolo, A.3    Nielsen, B.S.4    Bugge, T.H.5
  • 234
    • 1642326652 scopus 로고    scopus 로고
    • Regulation of prostasin expression and function in the prostate
    • Chen, L. M., Zhang, X. and Chai, K. X. (2004) Regulation of prostasin expression and function in the prostate. Prostate 59, 1-12
    • (2004) Prostate , vol.59 , pp. 1-12
    • Chen, L.M.1    Zhang, X.2    Chai, K.X.3
  • 235
    • 34447328778 scopus 로고    scopus 로고
    • Human DESC1 serine protease confers tumorigenic properties to MDCK cells and it is upregulated in tumours of different origin
    • Viloria, C. G., Peinado, J. R., Astudillo, A., Garcia-Suarez, O., Gonzalez, M. V., Suarez, C. and Cal, S. (2007) Human DESC1 serine protease confers tumorigenic properties to MDCK cells and it is upregulated in tumours of different origin. Br. J. Cancer 97, 201-209
    • (2007) Br. J. Cancer , vol.97 , pp. 201-209
    • Viloria, C.G.1    Peinado, J.R.2    Astudillo, A.3    Garcia-Suarez, O.4    Gonzalez, M.V.5    Suarez, C.6    Cal, S.7
  • 236
    • 33645280043 scopus 로고    scopus 로고
    • Biochemical characterization of human enteropeptidase light chain
    • Moscow
    • Gasparian, M. E., Ostapchenko, V. G., Dolgikh, D. A. and Kirpichnikov, M. P. (2006) Biochemical characterization of human enteropeptidase light chain. Biochemistry (Moscow) 71, 113-119
    • (2006) Biochemistry , vol.71 , pp. 113-119
    • Gasparian, M.E.1    Ostapchenko, V.G.2    Dolgikh, D.A.3    Kirpichnikov, M.P.4
  • 237
    • 0018786255 scopus 로고
    • The preparation and properties of bovine enterokinase
    • Liepnieks, J. J. and Light, A. (1979) The preparation and properties of bovine enterokinase. J. Biol. Chem. 254, 1677-1683
    • (1979) J. Biol. Chem. , vol.254 , pp. 1677-1683
    • Liepnieks, J.J.1    Light, A.2
  • 239
    • 0141815667 scopus 로고    scopus 로고
    • Tissue expression, protease specificity, and Kunitz domain functions of hepatocyte growth factor activator inhibitor-1B (HAI-1B), a new splice variant of HAI-1
    • Kirchhofer, D., Peek, M., Li, W., Stamos, J., Eigenbrot, C., Kadkhodayan, S., Elliott, J. M., Corpuz, R. T., Lazarus, R. A. and Moran, P. (2003) Tissue expression, protease specificity, and Kunitz domain functions of hepatocyte growth factor activator inhibitor-1B (HAI-1B), a new splice variant of HAI-1. J. Biol. Chem. 278, 36341-36349
    • (2003) J. Biol. Chem. , vol.278 , pp. 36341-36349
    • Kirchhofer, D.1    Peek, M.2    Li, W.3    Stamos, J.4    Eigenbrot, C.5    Kadkhodayan, S.6    Elliott, J.M.7    Corpuz, R.T.8    Lazarus, R.A.9    Moran, P.10
  • 240
    • 0037908862 scopus 로고    scopus 로고
    • Inhibition of membrane-type serine protease 1/matriptase by natural and synthetic protease inhibitors
    • Tokyo
    • Yamasaki, Y., Satomi, S., Murai, N., Tsuzuki, S. and Fushiki, T. (2003) Inhibition of membrane-type serine protease 1/matriptase by natural and synthetic protease inhibitors. J. Nutr. Sci. Vitaminol. (Tokyo) 49, 27-32
    • (2003) J. Nutr. Sci. Vitaminol. , vol.49 , pp. 27-32
    • Yamasaki, Y.1    Satomi, S.2    Murai, N.3    Tsuzuki, S.4    Fushiki, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.