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Volumn 54, Issue , 2003, Pages 167-206

Type II transmembrane serine proteases

(1)  Wu, Qingyu a  


Author keywords

[No Author keywords available]

Indexed keywords

CORIN PROTEIN, MOUSE; CRN PROTEIN, HUMAN; ENTEROPEPTIDASE; HEPSIN; MATRIPTASE; MEMBRANE PROTEIN; SERINE PROTEINASE; ST14 PROTEIN, HUMAN; TMPRSS2 PROTEIN, HUMAN; TRYPSIN;

EID: 0038463745     PISSN: 00702153     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0070-2153(03)54009-1     Document Type: Review
Times cited : (52)

References (164)
  • 1
    • 0035866379 scopus 로고    scopus 로고
    • Catalytic cleavage of the androgen-regulated TMPRSS2 protease results in its secretion by prostate and prostate cancer epithelia
    • D.E Afar I Vivanco R.S Hubert J Kuo E Chen D.C Saffran A.B Raitano A Jakobovits Catalytic cleavage of the androgen-regulated TMPRSS2 protease results in its secretion by prostate and prostate cancer epithelia Cancer Res. 61 2001 1686 1692
    • (2001) Cancer Res. , vol.61 , pp. 1686-1692
    • Afar, D.E1    Vivanco, I2    Hubert, R.S3    Kuo, J4    Chen, E5    Saffran, D.C6    Raitano, A.B7    Jakobovits, A8
  • 3
    • 0017727892 scopus 로고
    • Bovine enterokinase
    • L.E Anderson K.A Walsh H Neurath Bovine enterokinase Purification, specificity, and some molecular properties Biochemistry 16 1977 3354 3360
    • (1977) , pp. 3354-3360
    • Anderson, L.E1    Walsh, K.A2    Neurath, H3
  • 4
    • 0027312491 scopus 로고
    • The Drosophila Stubble-stubbloid gene encodes an apparent transmembrane serine protease required for epithelial morphogenesis
    • L.F Appel M Prout R Abu-Shumays A Hammonds J.C Garbe D Fristrom J Fristrom The Drosophila Stubble-stubbloid gene encodes an apparent transmembrane serine protease required for epithelial morphogenesis Proc. Natl. Acad. Sci. USA 90 1993 4937 4941
    • (1993) , pp. 4937-4941
    • Appel, L.F1    Prout, M2    Abu-Shumays, R3    Hammonds, A4    Garbe, J.C5    Fristrom, D6    Fristrom, J7
  • 6
    • 0029730738 scopus 로고    scopus 로고
    • A conserved signaling pathway: the Drosophila toll-dorsal pathway
    • M.P Belvin K.V Anderson A conserved signaling pathway: the Drosophila toll-dorsal pathway Annu. Rev. Cell. Dev. Biol. 12 1996 393 416
    • (1996) Annu. Rev. Cell. Dev. Biol. , vol.12 , pp. 393-416
    • Belvin, M.P1    Anderson, K.V2
  • 7
    • 0035081038 scopus 로고    scopus 로고
    • Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor
    • C Benaud R.B Dickson C.Y Lin Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor Eur. J. Biochem. 268 2001 1439 1447
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1439-1447
    • Benaud, C1    Dickson, R.B2    Lin, C.Y3
  • 8
    • 0037155905 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate, present in serum-derived lipoproteins, activates matriptase
    • C Benaud M Oberst J.P Hobson S Spiegel R.B Dickson C.Y Lin Sphingosine 1-phosphate, present in serum-derived lipoproteins, activates matriptase J. Biol. Chem. 277 2002 10539 10546
    • (2002) J. Biol. Chem. , vol.277 , pp. 10539-10546
    • Benaud, C1    Oberst, M2    Hobson, J.P3    Spiegel, S4    Dickson, R.B5    Lin, C.Y6
  • 14
    • 0030758231 scopus 로고    scopus 로고
    • LDL-receptor structure
    • M.S Brown J Herz J.L Goldstein LDL-receptor structure Calcium cages, acid baths and recycling receptors Nature 388 1997 629 630 [news; comment]
    • (1997) , pp. 629-630
    • Brown, M.S1    Herz, J2    Goldstein, J.L3
  • 16
    • 0031456158 scopus 로고    scopus 로고
    • Wnt signaling: a common theme in animal development
    • K.M Cadigan R Nusse Wnt signaling: a common theme in animal development Genes Dev. 11 1997 3286 3305
    • (1997) Genes Dev. , vol.11 , pp. 3286-3305
    • Cadigan, K.M1    Nusse, R2
  • 17
    • 0023105043 scopus 로고
    • Characterization of primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones
    • C.F Catterall A Lyons R.B Sim A.J Day T.J Harris Characterization of primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones Biochem. J. 242 1987 849 856
    • (1987) Biochem. J. , vol.242 , pp. 849-856
    • Catterall, C.F1    Lyons, A2    Sim, R.B3    Day, A.J4    Harris, T.J5
  • 18
    • 0035976996 scopus 로고    scopus 로고
    • N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease
    • E.G Cho M.G Kim C Kim S.R Kim I.S Seong C Chung R.H Schwartz D Park N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease J. Biol. Chem. 276 2001 44581 44589
    • (2001) J. Biol. Chem. , vol.276 , pp. 44581-44589
    • Cho, E.G1    Kim, M.G2    Kim, C3    Kim, S.R4    Seong, I.S5    Chung, C6    Schwartz, R.H7    Park, D8
  • 19
    • 0026331304 scopus 로고
    • Basic and clinical aspects of fibrinolysis and thrombolysis
    • D Collen H.R Lijnen Basic and clinical aspects of fibrinolysis and thrombolysis Blood 78 1991 3114 3124
    • (1991) Blood , vol.78 , pp. 3114-3124
    • Collen, D1    Lijnen, H.R2
  • 20
    • 0029115204 scopus 로고
    • Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner DsbA
    • L.A Collins-Racie J.M McColgan K.L Grant E.A Diblasio-Smith J.M McCoy E.R Lavallie Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner DsbA Biotechnology (NY) 13 1995 982 987
    • (1995) Biotechnology (NY) , vol.13 , pp. 982-987
    • Collins-Racie, L.A1    McColgan, J.M2    Grant, K.L3    Diblasio-Smith, E.A4    McCoy, J.M5    Lavallie, E.R6
  • 22
    • 0344656211 scopus 로고
    • Cloning of the mRNA for the protein that crosslinks to the egg peptide speract
    • L.J Dangott J.E Jordan R.A Bellet D.L Garbers Cloning of the mRNA for the protein that crosslinks to the egg peptide speract Proc. Natl. Acad. Sci. USA 86 1989 2128 2132
    • (1989) , pp. 2128-2132
    • Dangott, L.J1    Jordan, J.E2    Bellet, R.A3    Garbers, D.L4
  • 23
    • 0026337077 scopus 로고
    • The coagulation cascade: initiation, maintenance, and regulation
    • E.W Davie K Fujikawa W Kisiel The coagulation cascade: initiation, maintenance, and regulation Biochemistry 30 1991 10363 10370
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W1    Fujikawa, K2    Kisiel, W3
  • 24
    • 0022162343 scopus 로고
    • Atrial natriuretic factor: a hormone produced by the heart
    • A.J de Bold Atrial natriuretic factor: a hormone produced by the heart Science 230 1985 767 770
    • (1985) Science , vol.230 , pp. 767-770
    • de Bold, A.J1
  • 25
    • 0019352579 scopus 로고
    • A rapid and potent natriuretic response to intravenous injection of atrial myocardial extract in rats
    • A.J de Bold H.B Borenstein A.T Veress H Sonnenberg A rapid and potent natriuretic response to intravenous injection of atrial myocardial extract in rats Life Sci. 28 1981 89 94
    • (1981) Life Sci. , vol.28 , pp. 89-94
    • de Bold, A.J1    Borenstein, H.B2    Veress, A.T3    Sonnenberg, H4
  • 27
    • 0023024217 scopus 로고
    • A gene required for the specification of dorsal-ventral pattern in Drosophila appears to encode a serine protease
    • R Delotto P Spierer A gene required for the specification of dorsal-ventral pattern in Drosophila appears to encode a serine protease Nature 323 1986 688 692
    • (1986) Nature , vol.323 , pp. 688-692
    • Delotto, R1    Spierer, P2
  • 30
    • 0020063055 scopus 로고
    • Role of tumor cell membrane-bound serine proteases in tumor-induced target cytolysis
    • J.F Distefano G Beck B Lane S Zucker Role of tumor cell membrane-bound serine proteases in tumor-induced target cytolysis Cancer Res. 42 1982 207 218
    • (1982) Cancer Res. , vol.42 , pp. 207-218
    • Distefano, J.F1    Beck, G2    Lane, B3    Zucker, S4
  • 31
    • 0020523926 scopus 로고
    • Characterization of tumor cell membrane serine proteases by polyacrylamide gel electrophoresis
    • J.F Distefano G Beck S Zucker Characterization of tumor cell membrane serine proteases by polyacrylamide gel electrophoresis J. Histochem. Cytochem. 31 1983 1233 1240
    • (1983) J. Histochem. Cytochem. , vol.31 , pp. 1233-1240
    • Distefano, J.F1    Beck, G2    Zucker, S3
  • 33
    • 0035953310 scopus 로고    scopus 로고
    • Structure-based approach for the discovery of bis-benzamidines as novel inhibitors of matriptase
    • I.J Enyedy S.L Lee A.H Kuo R.B Dickson C.Y Lin S Wang Structure-based approach for the discovery of bis-benzamidines as novel inhibitors of matriptase J. Med. Chem. 44 2001 1349 1355
    • (2001) J. Med. Chem. , vol.44 , pp. 1349-1355
    • Enyedy, I.J1    Lee, S.L2    Kuo, A.H3    Dickson, R.B4    Lin, C.Y5    Wang, S6
  • 34
    • 0027190526 scopus 로고
    • Cloning and sequence analysis of rat hepsin, a cell surface serine proteinase
    • D Farley F Reymond H Nick Cloning and sequence analysis of rat hepsin, a cell surface serine proteinase Biochim. Biophys. Acta 1173 1993 350 352
    • (1993) Biochim. Biophys. Acta , vol.1173 , pp. 350-352
    • Farley, D1    Reymond, F2    Nick, H3
  • 36
    • 0024292694 scopus 로고
    • The molecular basis of blood coagulation
    • B Furie B.C Furie The molecular basis of blood coagulation Cell 53 1988 505 518
    • (1988) Cell , vol.53 , pp. 505-518
    • Furie, B1    Furie, B.C2
  • 37
    • 0020525406 scopus 로고
    • Isolated congenital enterokinase deficiency
    • F.K Ghishan P.C Lee E Lebenthal P Johnson C.A Bradley H.L Greene Isolated congenital enterokinase deficiency Recent findings and review of the literature Gastroenterology 85 1983 727 731
    • (1983) , pp. 727-731
    • Ghishan, F.K1    Lee, P.C2    Lebenthal, E3    Johnson, P4    Bradley, C.A5    Greene, H.L6
  • 38
    • 0024381672 scopus 로고
    • Prognostic importance of atrial natriuretic peptide in patients with chronic heart failure
    • S.S Gottlieb M.L Kukin D Ahern M Packer Prognostic importance of atrial natriuretic peptide in patients with chronic heart failure J. Am. Coll. Cardiol. 13 1989 1534 1539
    • (1989) J. Am. Coll. Cardiol. , vol.13 , pp. 1534-1539
    • Gottlieb, S.S1    Kukin, M.L2    Ahern, D3    Packer, M4
  • 40
    • 0018185007 scopus 로고
    • Optimisation of conditions for the affinity chromatography of human enterokinase on immobilised p-aminobenzamidine
    • D.A Grant A.I Magee J Hermon-Taylor Optimisation of conditions for the affinity chromatography of human enterokinase on immobilised p-aminobenzamidine Improvement of the preparative procedure by inclusion of negative affinity chromatography with glycylglycyl-aniline Eur. J. Biochem. 88 1978 183 189
    • (1978) , pp. 183-189
    • Grant, D.A1    Magee, A.I2    Hermon-Taylor, J3
  • 42
    • 85112948848 scopus 로고
    • Intestinal enterokinase deficiency
    • B Hadorn J.C Haworth B Gourley A Prasad V Troesch Intestinal enterokinase deficiency Occurrence in two sibs and age dependency of clinical expression Arch. Dis. Child 50 1975 277 282
    • (1975) , pp. 277-282
    • Hadorn, B1    Haworth, J.C2    Gourley, B3    Prasad, A4    Troesch, V5
  • 44
    • 12944332084 scopus 로고    scopus 로고
    • Gastrulation defective is a serine protease involved in activating the receptor toll to polarize the Drosophila embryo
    • J.H Han S.H Lee Y.Q Tan E.K Lemosy C Hashimoto Gastrulation defective is a serine protease involved in activating the receptor toll to polarize the Drosophila embryo Proc. Natl. Acad. Sci. USA 97 2000 9093 9097
    • (2000) , pp. 9093-9097
    • Han, J.H1    Lee, S.H2    Tan, Y.Q3    Lemosy, E.K4    Hashimoto, C5
  • 45
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • E Hartmann T.A Rapoport H.F Lodish Predicting the orientation of eukaryotic membrane-spanning proteins Proc. Natl. Acad. Sci. USA 86 1989 5786 5790
    • (1989) , pp. 5786-5790
    • Hartmann, E1    Rapoport, T.A2    Lodish, H.F3
  • 46
    • 0017649356 scopus 로고
    • Immunofluorescent localisation of enterokinase in human small intestine
    • J Hermon-Taylor J Perrin D.A Grant A Appleyard M Bubel A.I Magee Immunofluorescent localisation of enterokinase in human small intestine Gut 18 1977 259 265
    • (1977) Gut , vol.18 , pp. 259-265
    • Hermon-Taylor, J1    Perrin, J2    Grant, D.A3    Appleyard, A4    Bubel, M5    Magee, A.I6
  • 48
    • 0029120951 scopus 로고
    • An unusual mosaic protein with a protease domain, encoded by the nudel gene, is involved in defining embryonic dorsoventral polarity in Drosophila
    • C.C Hong C Hashimoto An unusual mosaic protein with a protease domain, encoded by the nudel gene, is involved in defining embryonic dorsoventral polarity in Drosophila Cell 82 1995 785 794
    • (1995) Cell , vol.82 , pp. 785-794
    • Hong, C.C1    Hashimoto, C2
  • 49
    • 0035846933 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases
    • J.D Hooper J.A Clements J.P Quigley T.M Antalis Type II transmembrane serine proteases Insights into an emerging class of cell surface proteolytic enzymes J. Biol. Chem. 276 2001 857 860
    • (2001) , pp. 857-860
    • Hooper, J.D1    Clements, J.A2    Quigley, J.P3    Antalis, T.M4
  • 50
    • 0033678992 scopus 로고    scopus 로고
    • Localization of the mosaic transmembrane serine protease corin to heart myocytes
    • J.D Hooper A.L Scarman B.E Clarke J.F Normyle T.M Antalis Localization of the mosaic transmembrane serine protease corin to heart myocytes Eur. J. Biochem. 267 2000 6931 6937
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6931-6937
    • Hooper, J.D1    Scarman, A.L2    Clarke, B.E3    Normyle, J.F4    Antalis, T.M5
  • 51
    • 85112937587 scopus 로고    scopus 로고
    • Pro-metastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1–6 GlcNAc-branching
    • S Ihara E Miyoshi J.H Ko K Murata S Nakahara K Honke R.B Dickson C.Y Lin N Taniguchi Pro-metastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1–6 GlcNAc-branching J. Biol. Chem. 25 2002 25
    • (2002) J. Biol. Chem. , vol.25 , pp. 25
    • Ihara, S1    Miyoshi, E2    Ko, J.H3    Murata, K4    Nakahara, S5    Honke, K6    Dickson, R.B7    Lin, C.Y8    Taniguchi, N9
  • 52
    • 0023096420 scopus 로고
    • Identification of a peptidase which processes atrial natriuretic factor precursor to its active form with 28 amino acid residues in particulate fractions of rat atrial homogenate
    • T Imada R Takayanagi T Inagami Identification of a peptidase which processes atrial natriuretic factor precursor to its active form with 28 amino acid residues in particulate fractions of rat atrial homogenate Biochem. Biophys. Res. Commun. 143 1987 587 592
    • (1987) Biochem. Biophys. Res. Commun. , vol.143 , pp. 587-592
    • Imada, T1    Takayanagi, R2    Inagami, T3
  • 53
    • 0023924764 scopus 로고
    • Atrioactivase, a specific peptidase in bovine atria for the processing of pro-atrial natriuretic factor
    • T Imada R Takayanagi T Inagami Atrioactivase, a specific peptidase in bovine atria for the processing of pro-atrial natriuretic factor Purification and characterization J. Biol. Chem. 263 1988 9515 9519
    • (1988) , pp. 9515-9519
    • Imada, T1    Takayanagi, R2    Inagami, T3
  • 54
    • 0024539509 scopus 로고
    • Atrial natriuretic factor
    • T Inagami Atrial natriuretic factor J. Biol. Chem. 264 1989 3043 3046
    • (1989) J. Biol. Chem. , vol.264 , pp. 3043-3046
    • Inagami, T1
  • 56
    • 0023700282 scopus 로고
    • Manipulation of stretch-induced atriopeptin prohormone release and processing in the perfused rat heart
    • T Ito Y Toki N Siegel J.K Gierse P Needleman Manipulation of stretch-induced atriopeptin prohormone release and processing in the perfused rat heart Proc. Natl. Acad. Sci. USA 85 1988 8365 8369
    • (1988) , pp. 8365-8369
    • Ito, T1    Toki, Y2    Siegel, N3    Gierse, J.K4    Needleman, P5
  • 57
    • 0033970075 scopus 로고    scopus 로고
    • Cloning, genomic organization, chromosomal assignment and expression of a novel mosaic serine proteinase: epitheliasin
    • E Jacquinet N.V Rao G.V Rao J.R Hoidal Cloning, genomic organization, chromosomal assignment and expression of a novel mosaic serine proteinase: epitheliasin FEBS Lett. 468 2000 93 100
    • (2000) FEBS Lett. , vol.468 , pp. 93-100
    • Jacquinet, E1    Rao, N.V2    Rao, G.V3    Hoidal, J.R4
  • 59
    • 0025238940 scopus 로고
    • Dominant and recessive alleles of the Drosophila easter gene are point mutations at conserved sites in the serine protease catalytic domain
    • Y.S Jin K.V Anderson Dominant and recessive alleles of the Drosophila easter gene are point mutations at conserved sites in the serine protease catalytic domain Cell 60 1990 873 881
    • (1990) Cell , vol.60 , pp. 873-881
    • Jin, Y.S1    Anderson, K.V2
  • 60
    • 0028943463 scopus 로고
    • Genetic decreases in atrial natriuretic peptide and salt-sensitive hypertension
    • S.W John J.H Krege P.M Oliver J.R Hagaman J.B Hodgin S.C Pang T.G Flynn O Smithies Genetic decreases in atrial natriuretic peptide and salt-sensitive hypertension Science 267 1995 679 681 [published erratum appears in Science (1995) 267, 1753]
    • (1995) Science , vol.267 , pp. 679-681
    • John, S.W1    Krege, J.H2    Oliver, P.M3    Hagaman, J.R4    Hodgin, J.B5    Pang, S.C6    Flynn, T.G7    Smithies, O8
  • 61
    • 0033564703 scopus 로고    scopus 로고
    • Complete nucleotide sequence, origin of isoform and functional characterization of the mouse hepsin gene
    • S Kawamura S Kurachi Y Deyashiki K Kurachi Complete nucleotide sequence, origin of isoform and functional characterization of the mouse hepsin gene Eur. J. Biochem. 262 1999 755 764
    • (1999) Eur. J. Biochem. , vol.262 , pp. 755-764
    • Kawamura, S1    Kurachi, S2    Deyashiki, Y3    Kurachi, K4
  • 62
    • 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
    • Y Kazama T Hamamoto D.C Foster W Kisiel 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 1995 66 72
    • (1995) J. Biol. Chem. , vol.270 , pp. 66-72
    • Kazama, Y1    Hamamoto, T2    Foster, D.C3    Kisiel, W4
  • 63
    • 0035911646 scopus 로고    scopus 로고
    • Cloning and expression of novel mosaic serine proteases with and without a transmembrane domain from human lung
    • D.R Kim S Sharmin M Inoue H Kido Cloning and expression of novel mosaic serine proteases with and without a transmembrane domain from human lung Biochim. Biophys. Acta 1518 2001 204 209
    • (2001) Biochim. Biophys. Acta , vol.1518 , pp. 204-209
    • Kim, D.R1    Sharmin, S2    Inoue, M3    Kido, H4
  • 64
    • 0032923230 scopus 로고    scopus 로고
    • Cloning and chromosomal mapping of a gene isolated from thymic stromal cells encoding a new mouse type II membrane serine protease, epithin, containing four LDL receptor modules and two CUB domains
    • M.G Kim C Chen M.S Lyu E.G Cho D Park C Kozak R.H Schwartz Cloning and chromosomal mapping of a gene isolated from thymic stromal cells encoding a new mouse type II membrane serine protease, epithin, containing four LDL receptor modules and two CUB domains Immunogenetics 49 1999 420 428
    • (1999) Immunogenetics , vol.49 , pp. 420-428
    • Kim, M.G1    Chen, C2    Lyu, M.S3    Cho, E.G4    Park, D5    Kozak, C6    Schwartz, R.H7
  • 66
    • 0028903750 scopus 로고
    • cDna sequence and chromosomal localization of human enterokinase, the proteolytic activator of trypsinogen
    • Y Kitamoto R.A Veile H Donis-Keller J.E Sadler cDna sequence and chromosomal localization of human enterokinase, the proteolytic activator of trypsinogen Biochemistry 34 1995 4562 4568
    • (1995) Biochemistry , vol.34 , pp. 4562-4568
    • Kitamoto, Y1    Veile, R.A2    Donis-Keller, H3    Sadler, J.E4
  • 67
    • 0028111631 scopus 로고
    • Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains
    • Y Kitamoto X Yuan Q Wu D.W McCourt J.E Sadler Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains Proc. Natl. Acad. Sci. USA 91 1994 7588 7592
    • (1994) , pp. 7588-7592
    • Kitamoto, Y1    Yuan, X2    Wu, Q3    McCourt, D.W4    Sadler, J.E5
  • 68
    • 0026722911 scopus 로고
    • Molecular biology of the natriuretic peptides and their receptors
    • K.J Koller D.V Goeddel Molecular biology of the natriuretic peptides and their receptors Circulation 86 1992 1081 1088
    • (1992) Circulation , vol.86 , pp. 1081-1088
    • Koller, K.J1    Goeddel, D.V2
  • 69
    • 0027212194 scopus 로고
    • Glycoprotein 330, a member of the low density lipoprotein receptor family, binds lipoprotein lipase in vitro
    • M.Z Kounnas D.A Chappell D.K Strickland W.S Argraves Glycoprotein 330, a member of the low density lipoprotein receptor family, binds lipoprotein lipase in vitro J. Biol. Chem. 268 1993 14176 14781
    • (1993) J. Biol. Chem. , vol.268 , pp. 14176-14781
    • Kounnas, M.Z1    Chappell, D.A2    Strickland, D.K3    Argraves, W.S4
  • 70
    • 0017324044 scopus 로고
    • Serine proteases: structure and mechanism of catalysis
    • J Kraut Serine proteases: structure and mechanism of catalysis Annu. Rev. Biochem. 46 1977 331 358
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 331-358
    • Kraut, J1
  • 71
    • 0028173897 scopus 로고
    • Structures and functions of multiligand lipoprotein receptors: macrophage scavenger receptors and LDL receptor-related protein (LRP)
    • M Krieger J Herz Structures and functions of multiligand lipoprotein receptors: macrophage scavenger receptors and LDL receptor-related protein (LRP) Annu. Rev. Biochem. 63 1994 601 637
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 601-637
    • Krieger, M1    Herz, J2
  • 72
    • 11744372696 scopus 로고
    • Formation of trypsin from crystalline trypsinogen by means of enterokinase
    • M Kunitz Formation of trypsin from crystalline trypsinogen by means of enterokinase J. Gen. Physiol. 22 1939 429 446
    • (1939) J. Gen. Physiol. , vol.22 , pp. 429-446
    • Kunitz, M1
  • 73
    • 14744306559 scopus 로고
    • Purification and concentration of enterokinase
    • M Kunitz Purification and concentration of enterokinase J. Gen. Physiol. 22 1939 447 450
    • (1939) J. Gen. Physiol. , vol.22 , pp. 447-450
    • Kunitz, M1
  • 75
    • 0020585438 scopus 로고
    • Isolation and characterization of a trypsin-like serine proteinase from the membranes of Walker 256 carcino-sarcoma cells
    • V.J Labombardi E Shaw J.F Distefano G Beck F Brown S Zucker Isolation and characterization of a trypsin-like serine proteinase from the membranes of Walker 256 carcino-sarcoma cells Biochem. J. 211 1983 695 700
    • (1983) Biochem. J. , vol.211 , pp. 695-700
    • Labombardi, V.J1    Shaw, E2    Distefano, J.F3    Beck, G4    Brown, F5    Zucker, S6
  • 76
    • 0021889298 scopus 로고
    • Atrial natriuretic factor-a circulating hormone stimulated by volume loading
    • R.E Lang H Tholken D Ganten F.C Luft H Ruskoaho T Unger Atrial natriuretic factor-a circulating hormone stimulated by volume loading Nature 314 1985 264 266
    • (1985) Nature , vol.314 , pp. 264-266
    • Lang, R.E1    Tholken, H2    Ganten, D3    Luft, F.C4    Ruskoaho, H5    Unger, T6
  • 78
    • 0034711244 scopus 로고    scopus 로고
    • Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease
    • S.L Lee R.B Dickson C.Y Lin Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease J. Biol. Chem. 275 2000 36720 36725
    • (2000) J. Biol. Chem. , vol.275 , pp. 36720-36725
    • Lee, S.L1    Dickson, R.B2    Lin, C.Y3
  • 80
    • 0023850048 scopus 로고
    • A novel trypsin-like serine protease (hepsin) with a putative transmembrane domain expressed by human liver and hepatoma cells
    • S.P Leytus K.R Loeb F.S Hagen K Kurachi E.W Davie A novel trypsin-like serine protease (hepsin) with a putative transmembrane domain expressed by human liver and hepatoma cells Biochemistry 27 1988 1067 1074
    • (1988) Biochemistry , vol.27 , pp. 1067-1074
    • Leytus, S.P1    Loeb, K.R2    Hagen, F.S3    Kurachi, K4    Davie, E.W5
  • 81
    • 0018786255 scopus 로고
    • The preparation and properties of bovine enterokinase
    • J.J Liepnieks A Light The preparation and properties of bovine enterokinase J. Biol. Chem. 254 1979 1677 1683
    • (1979) J. Biol. Chem. , vol.254 , pp. 1677-1683
    • Liepnieks, J.J1    Light, A2
  • 82
    • 0024498629 scopus 로고
    • Enterokinase (enteropeptidase): comparative aspects
    • A Light H Janska Enterokinase (enteropeptidase): comparative aspects Trends Biochem. Sci. 14 1989 110 112
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 110-112
    • Light, A1    Janska, H2
  • 83
    • 0026010575 scopus 로고
    • The amino-terminal sequence of the catalytic subunit of bovine enterokinase
    • A Light H Janska The amino-terminal sequence of the catalytic subunit of bovine enterokinase J. Protein Chem. 10 1991 475 480
    • (1991) J. Protein Chem. , vol.10 , pp. 475-480
    • Light, A1    Janska, H2
  • 84
    • 0033198498 scopus 로고    scopus 로고
    • Prostate-localized and androgen-regulated expression of the membrane-bound serine protease TMPRSS2
    • B Lin C Ferguson J.T White S Wang R Vessella L.D True L Hood P.S Nelson Prostate-localized and androgen-regulated expression of the membrane-bound serine protease TMPRSS2 Cancer Res. 59 1999 4180 4184
    • (1999) Cancer Res. , vol.59 , pp. 4180-4184
    • Lin, B1    Ferguson, C2    White, J.T3    Wang, S4    Vessella, R5    True, L.D6    Hood, L7    Nelson, P.S8
  • 85
    • 0033603547 scopus 로고    scopus 로고
    • Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk
    • C.Y Lin J Anders M Johnson R.B Dickson Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk J. Biol. Chem. 274 1999 18237 18242
    • (1999) J. Biol. Chem. , vol.274 , pp. 18237-18242
    • Lin, C.Y1    Anders, J2    Johnson, M3    Dickson, R.B4
  • 86
    • 0033603574 scopus 로고    scopus 로고
    • Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity
    • C.Y Lin J Anders M Johnson Q.A Sang R.B Dickson Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity J. Biol. Chem. 274 1999 18231 18236
    • (1999) J. Biol. Chem. , vol.274 , pp. 18231-18236
    • Lin, C.Y1    Anders, J2    Johnson, M3    Sang, Q.A4    Dickson, R.B5
  • 87
    • 0030910387 scopus 로고    scopus 로고
    • Characterization of a novel, membrane-bound, 80-kDa matrix-degrading protease from human breast cancer cells
    • C.Y Lin J.K Wang J Torri L Dou Q.A Sang R.B Dickson Characterization of a novel, membrane-bound, 80-kDa matrix-degrading protease from human breast cancer cells Monoclonal antibody production, isolation, and localization J. Biol. Chem. 272 1997 9147 9152
    • (1997) , pp. 9147-9152
    • Lin, C.Y1    Wang, J.K2    Torri, J3    Dou, L4    Sang, Q.A5    Dickson, R.B6
  • 88
    • 0020965391 scopus 로고
    • Histochemical demonstration of enteropeptidase activity
    • Z Lojda R Gossrau Histochemical demonstration of enteropeptidase activity New method with a synthetic substrate and its comparison with the trypsinogen procedure Histochemistry 78 1983 251 270
    • (1983) , pp. 251-270
    • Lojda, Z1    Gossrau, R2
  • 89
    • 0028973389 scopus 로고
    • Salt-resistant hypertension in mice lacking the guanylyl cyclase-A receptor for atrial natriuretic peptide
    • M.J Lopez S.K Wong I Kishimoto S Dubois V Mach J Friesen D.L Garbers A Beuve Salt-resistant hypertension in mice lacking the guanylyl cyclase-A receptor for atrial natriuretic peptide Nature 378 1995 65 68
    • (1995) Nature , vol.378 , pp. 65-68
    • Lopez, M.J1    Wong, S.K2    Kishimoto, I3    Dubois, S4    Mach, V5    Friesen, J6    Garbers, D.L7    Beuve, A8
  • 90
    • 85112894294 scopus 로고    scopus 로고
    • D Lu J.E Sadler Handbook of Proteolytic Enzymes 1998 Academic Press Ltd London
    • (1998)
    • Lu, D1    Sadler, J.E2
  • 91
    • 0344631102 scopus 로고    scopus 로고
    • Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide
    • D Lu K Futterer S Korolev X Zheng K Tan G Waksman J.E Sadler Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide J. Mol. Biol. 292 1999 361 373
    • (1999) J. Mol. Biol. , vol.292 , pp. 361-373
    • Lu, D1    Futterer, K2    Korolev, S3    Zheng, X4    Tan, K5    Waksman, G6    Sadler, J.E7
  • 92
    • 0031466897 scopus 로고    scopus 로고
    • Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain
    • D Lu X Yuan X Zheng J.E Sadler Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain J. Biol. Chem. 272 1997 31293 31300
    • (1997) J. Biol. Chem. , vol.272 , pp. 31293-31300
    • Lu, D1    Yuan, X2    Zheng, X3    Sadler, J.E4
  • 93
    • 0035874995 scopus 로고    scopus 로고
    • Human prostate cancer and benign prostatic hyperplasia: molecular dissection by gene expression profiling
    • J Luo D.J Duggan Y Chen J Sauvageot C.M Ewing M.L Bittner J.M Trent W.B Isaacs Human prostate cancer and benign prostatic hyperplasia: molecular dissection by gene expression profiling Cancer Res. 61 2001 4683 4688
    • (2001) Cancer Res. , vol.61 , pp. 4683-4688
    • Luo, J1    Duggan, D.J2    Chen, Y3    Sauvageot, J4    Ewing, C.M5    Bittner, M.L6    Trent, J.M7    Isaacs, W.B8
  • 95
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • K.G Mann M.E Nesheim W.R Church P Haley S Krishnaswamy Surface-dependent reactions of the vitamin K-dependent enzyme complexes Blood 76 1990 1 16
    • (1990) Blood , vol.76 , pp. 1-16
    • Mann, K.G1    Nesheim, M.E2    Church, W.R3    Haley, P4    Krishnaswamy, S5
  • 96
    • 85112891083 scopus 로고
    • Enterokinase
    • N.S Mann S.K Mann Enterokinase Proc. Soc. Exp. Biol. Med. 206 1994 114 118
    • (1994) , pp. 114-118
    • Mann, N.S1    Mann, S.K2
  • 97
    • 0021878280 scopus 로고
    • Vasopressin-stimulated release of atriopeptin: endocrine antagonists in fluid homeostasis
    • P.T Manning D Schwartz N.C Katsube S.W Holmberg P Needleman Vasopressin-stimulated release of atriopeptin: endocrine antagonists in fluid homeostasis Science 229 1985 395 397
    • (1985) Science , vol.229 , pp. 395-397
    • Manning, P.T1    Schwartz, D2    Katsube, N.C3    Holmberg, S.W4    Needleman, P5
  • 98
    • 0015239936 scopus 로고
    • Purification and specificity of porcine enterokinase
    • S Maroux J Baratti P Desnuelle Purification and specificity of porcine enterokinase J. Biol. Chem. 246 1971 5031 5039
    • (1971) J. Biol. Chem. , vol.246 , pp. 5031-5039
    • Maroux, S1    Baratti, J2    Desnuelle, P3
  • 101
    • 0025865926 scopus 로고
    • The sequence and reactive site of ecotin
    • M.E McGrath W.M Hines J.A Sakanari R.J Fletterick C.S Craik The sequence and reactive site of ecotin A general inhibitor of pancreatic serine proteases from Escherichia coli J. Biol. Chem. 266 1991 6620 6625
    • (1991) , pp. 6620-6625
    • McGrath, M.E1    Hines, W.M2    Sakanari, J.A3    Fletterick, R.J4    Craik, C.S5
  • 102
    • 0027535914 scopus 로고
    • Biology and biochemistry of proteinases in tumor invasion
    • P Mignatti D.B Rifkin Biology and biochemistry of proteinases in tumor invasion Physiol. Rev. 73 1993 161 195
    • (1993) Physiol. Rev. , vol.73 , pp. 161-195
    • Mignatti, P1    Rifkin, D.B2
  • 103
    • 0027289115 scopus 로고
    • Molecular cloning and sequence analysis of the cDNA for a human serine protease reponsible for activation of hepatocyte growth factor
    • K Miyazawa T Shimomura A Kitamura J Kondo Y Morimoto N Kitamura Molecular cloning and sequence analysis of the cDNA for a human serine protease reponsible for activation of hepatocyte growth factor Structural similarity of the protease precursor to blood coagulation factor XII J. Biol. Chem. 268 1993 10024 10028
    • (1993) , pp. 10024-10028
    • Miyazawa, K1    Shimomura, T2    Kitamura, A3    Kondo, J4    Morimoto, Y5    Kitamura, N6
  • 105
    • 0021115222 scopus 로고
    • The role of proteinases in cellular invasiveness
    • D.E Mullins S.T Rohrlich The role of proteinases in cellular invasiveness Biochim. Biophys. Acta 695 1983 177 214
    • (1983) Biochim. Biophys. Acta , vol.695 , pp. 177-214
    • Mullins, D.E1    Rohrlich, S.T2
  • 106
    • 0026699904 scopus 로고
    • Activation of hepatocyte growth factor by proteolytic conversion of a single chain form to a heterodimer
    • D Naka T Ishii Y Yoshiyama K Miyazawa H Hara T Hishida N Kidamura Activation of hepatocyte growth factor by proteolytic conversion of a single chain form to a heterodimer J. Biol. Chem. 267 1992 20114 20119
    • (1992) J. Biol. Chem. , vol.267 , pp. 20114-20119
    • Naka, D1    Ishii, T2    Yoshiyama, Y3    Miyazawa, K4    Hara, H5    Hishida, T6    Kidamura, N7
  • 107
    • 0022484841 scopus 로고
    • The versatility of proteolytic enzymes
    • H Neurath The versatility of proteolytic enzymes J. Cell. Biochem. 32 1986 35 49
    • (1986) J. Cell. Biochem. , vol.32 , pp. 35-49
    • Neurath, H1
  • 108
    • 0035069846 scopus 로고    scopus 로고
    • Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo
    • M Oberst J Anders B Xie B Singh M Ossandon M Johnson R.B Dickson C.Y Lin Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo Am. J. Pathol. 158 2001 1301 1311
    • (2001) Am. J. Pathol. , vol.158 , pp. 1301-1311
    • Oberst, M1    Anders, J2    Xie, B3    Singh, B4    Ossandon, M5    Johnson, M6    Dickson, R.B7    Lin, C.Y8
  • 109
    • 0015864390 scopus 로고
    • Fibrinolysis associated with oncogenic transformation
    • L Ossowski J.P Quigley G.M Kellerman E Reich Fibrinolysis associated with oncogenic transformation Requirement of plasminogen for correlated changes in cellular morphology, colony formation in agar, and cell migration J. Exp. Med. 138 1973 1056 1064
    • (1973) , pp. 1056-1064
    • Ossowski, L1    Quigley, J.P2    Kellerman, G.M3    Reich, E4
  • 110
    • 0015545381 scopus 로고
    • An enzymatic function associated with transformation of fibroblasts by oncogenic viruses. II. Mammalian fibroblast cultures transformed by DNA and RNA tumor viruses
    • L Ossowski J.C Unkeless A Tobia J.P Quigley D.B Rifkin E Reich An enzymatic function associated with transformation of fibroblasts by oncogenic viruses. II. Mammalian fibroblast cultures transformed by DNA and RNA tumor viruses J. Exp. Med. 137 1973 112 126
    • (1973) J. Exp. Med. , vol.137 , pp. 112-126
    • Ossowski, L1    Unkeless, J.C2    Tobia, A3    Quigley, J.P4    Rifkin, D.B5    Reich, E6
  • 111
    • 0031572305 scopus 로고    scopus 로고
    • Cloning of the TMPRSS2 gene, which encodes a novel serine protease with transmembrane, LDLRA, and SRCR domains and maps to 21q22.3
    • A Paoloni-Giacobino H Chen M.C Peitsch C Rossier S.E Antonarakis Cloning of the TMPRSS2 gene, which encodes a novel serine protease with transmembrane, LDLRA, and SRCR domains and maps to 21q22.3 Genomics 44 1997 309 320
    • (1997) Genomics , vol.44 , pp. 309-320
    • Paoloni-Giacobino, A1    Chen, H2    Peitsch, M.C3    Rossier, C4    Antonarakis, S.E5
  • 112
    • 85112920893 scopus 로고
    • Nobel Lecture, Physiology or Medicine 1901–1921
    • I.P Pavlov Nobel Lecture, Physiology or Medicine 1901–1921 1904 The Nobel Foundation
    • (1904)
    • Pavlov, I.P1
  • 113
    • 0016206865 scopus 로고
    • Plasminogen, the serum proenzyme activated by factors from cells transformed by oncogenic viruses
    • J.P Quigley L Ossowski E Reich Plasminogen, the serum proenzyme activated by factors from cells transformed by oncogenic viruses J. Biol. Chem. 249 1974 4306 4311
    • (1974) J. Biol. Chem. , vol.249 , pp. 4306-4311
    • Quigley, J.P1    Ossowski, L2    Reich, E3
  • 118
    • 0026596902 scopus 로고
    • The cosecretional maturation of atrial natriuretic factor by primary atrial myocytes
    • C.A Sei G.L Hand S.F Murray C.C Glembotski The cosecretional maturation of atrial natriuretic factor by primary atrial myocytes Mol. Endocrinol. 6 1992 309 319
    • (1992) Mol. Endocrinol. , vol.6 , pp. 309-319
    • Sei, C.A1    Hand, G.L2    Murray, S.F3    Glembotski, C.C4
  • 119
    • 0022901627 scopus 로고
    • Homologous IRCM-serine protease 1 from pituitary, heart atrium and ventricle: a common pro-hormone maturation enzyme
    • N.G Seidah J.A Cromlish J Hamelin G Thibault M Chretien Homologous IRCM-serine protease 1 from pituitary, heart atrium and ventricle: a common pro-hormone maturation enzyme Biosci. Rep. 6 1986 835 844
    • (1986) Biosci. Rep. , vol.6 , pp. 835-844
    • Seidah, N.G1    Cromlish, J.A2    Hamelin, J3    Thibault, G4    Chretien, M5
  • 120
    • 0027474797 scopus 로고
    • Identification and characterization of a novel matrix-degrading protease from hormone-dependent human breast cancer cells
    • Y.E Shi J Torri L Yieh A Wellstein M.E Lippman R.B Dickson Identification and characterization of a novel matrix-degrading protease from hormone-dependent human breast cancer cells Cancer Res. 53 1993 1409 1415
    • (1993) Cancer Res. , vol.53 , pp. 1409-1415
    • Shi, Y.E1    Torri, J2    Yieh, L3    Wellstein, A4    Lippman, M.E5    Dickson, R.B6
  • 121
    • 0023945178 scopus 로고
    • The post-translational processing of rat pro-atrial natriuretic factor by primary atrial myocyte cultures
    • P.P Shields C.C Glembotski The post-translational processing of rat pro-atrial natriuretic factor by primary atrial myocyte cultures J. Biol. Chem. 263 1988 8091 8098
    • (1988) J. Biol. Chem. , vol.263 , pp. 8091-8098
    • Shields, P.P1    Glembotski, C.C2
  • 123
    • 0031770250 scopus 로고    scopus 로고
    • Frizzled signaling and the developmental control of cell polarity
    • J.M Shulman N Perrimon J.D Axelrod Frizzled signaling and the developmental control of cell polarity Trends Genet. 14 1998 452 458
    • (1998) Trends Genet. , vol.14 , pp. 452-458
    • Shulman, J.M1    Perrimon, N2    Axelrod, J.D3
  • 126
    • 0030237229 scopus 로고    scopus 로고
    • Roles of mesenchymal-epithelial interactions and hepatocyte growth factor-scatter factor (HGF-SF) in placental development
    • F Stewart Roles of mesenchymal-epithelial interactions and hepatocyte growth factor-scatter factor (HGF-SF) in placental development Rev. Reprod. 1 1996 144 148
    • (1996) Rev. Reprod. , vol.1 , pp. 144-148
    • Stewart, F1
  • 127
    • 0023661693 scopus 로고
    • Scatter factor is a fibroblast-derived modulator of epithelial cell mobility
    • M Stoker E Gherardi M Perryman J Gray Scatter factor is a fibroblast-derived modulator of epithelial cell mobility Nature 327 1987 239 242
    • (1987) Nature , vol.327 , pp. 239-242
    • Stoker, M1    Gherardi, E2    Perryman, M3    Gray, J4
  • 128
    • 0016089567 scopus 로고
    • A family of protein-cutting proteins
    • R.M Stroud A family of protein-cutting proteins Sci. Am. 231 1974 74 88
    • (1974) Sci. Am. , vol.231 , pp. 74-88
    • Stroud, R.M1
  • 129
    • 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
    • T Takeuchi J.L Harris W Huang K.W Yan S.R Coughlin C.S Craik 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 2000 26333 26342
    • (2000) J. Biol. Chem. , vol.275 , pp. 26333-26342
    • Takeuchi, T1    Harris, J.L2    Huang, W3    Yan, K.W4    Coughlin, S.R5    Craik, C.S6
  • 130
    • 0033613123 scopus 로고    scopus 로고
    • Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue
    • T Takeuchi M.A Shuman C.S Craik Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue Proc. Natl. Acad. Sci. USA 96 1999 11054 11061
    • (1999) , pp. 11054-11061
    • Takeuchi, T1    Shuman, M.A2    Craik, C.S3
  • 131
    • 0030850099 scopus 로고    scopus 로고
    • Hepsin, a cell surface serine protease identified in hepatoma cells, is overexpressed in ovarian cancer
    • H Tanimoto Y Yan J Clarke S Korourian K Shigemasa T.H Parmley G.P Parham O.B TJ Hepsin, a cell surface serine protease identified in hepatoma cells, is overexpressed in ovarian cancer Cancer Res. 57 1997 2884 2887
    • (1997) Cancer Res. , vol.57 , pp. 2884-2887
    • Tanimoto, H1    Yan, Y2    Clarke, J3    Korourian, S4    Shigemasa, K5    Parmley, T.H6    Parham, G.P7    TJ, O.B8
  • 132
    • 0024580621 scopus 로고
    • The membrane form of guanylate cyclase
    • D.S Thorpe D.L Garbers The membrane form of guanylate cyclase Homology with a subunit of the cytoplasmic form of the enzyme J. Biol. Chem. 264 1989 6545 6549
    • (1989) , pp. 6545-6549
    • Thorpe, D.S1    Garbers, D.L2
  • 133
    • 14444283111 scopus 로고    scopus 로고
    • A novel low-density lipoprotein receptor-related protein with type II membrane protein-like structure is abundant in heart
    • Y Tomita D.H Kim K Magoori T Fujino T.T Yamamoto A novel low-density lipoprotein receptor-related protein with type II membrane protein-like structure is abundant in heart J. Biochem. (Tokyo) 124 1998 784 789
    • (1998) J. Biochem. (Tokyo) , vol.124 , pp. 784-789
    • Tomita, Y1    Kim, D.H2    Magoori, K3    Fujino, T4    Yamamoto, T.T5
  • 134
    • 0027257995 scopus 로고
    • Hepsin, a putative cell-surface serine protease, is required for mammalian cell growth
    • A Torres-Rosado O.S KS A Tsuji S.H Chou K Kurachi Hepsin, a putative cell-surface serine protease, is required for mammalian cell growth Proc. Natl. Acad. Sci. USA 90 1993 7181 7185
    • (1993) , pp. 7181-7185
    • Torres-Rosado, A1    KS, O.S2    Tsuji, A3    Chou, S.H4    Kurachi, K5
  • 135
    • 0025951220 scopus 로고
    • Hepsin, a cell membrane-associated protease
    • A Tsuji A Torres-Rosado T Arai M.M Le Beau R.S Lemons S.H Chou K Kurachi Hepsin, a cell membrane-associated protease Characterization, tissue distribution, and gene localization J. Biol. Chem. 266 1991 16948 16953
    • (1991) , pp. 16948-16953
    • Tsuji, A1    Torres-Rosado, A2    Arai, T3    Le Beau, M.M4    Lemons, R.S5    Chou, S.H6    Kurachi, K7
  • 136
    • 0028911690 scopus 로고
    • Placental defect and embryonic lethality in mice lacking hepatocyte growth factor/scatter factor
    • Y Uehara O Minowa C Mori K Shiota J Kuno T Noda N Kitamura Placental defect and embryonic lethality in mice lacking hepatocyte growth factor/scatter factor Nature 373 1995 702 705
    • (1995) Nature , vol.373 , pp. 702-705
    • Uehara, Y1    Minowa, O2    Mori, C3    Shiota, K4    Kuno, J5    Noda, T6    Kitamura, N7
  • 138
    • 0016255297 scopus 로고
    • Fibrinolysis associated with oncogenic transformation
    • J Unkeless K Dano G.M Kellerman E Reich Fibrinolysis associated with oncogenic transformation Partial purification and characterization of the cell factor, a plasminogen activator J. Biol. Chem. 249 1974 4295 4305
    • (1974) , pp. 4295-4305
    • Unkeless, J1    Dano, K2    Kellerman, G.M3    Reich, E4
  • 139
    • 0015548765 scopus 로고
    • An enzymatic function associated with transformation of fibroblasts by oncogenic viruses. I. Chick embryo fibroblast cultures transformed by avian RNA tumor viruses
    • J.C Unkeless A Tobia L Ossowski J.P Quigley D.B Rifkin E Reich An enzymatic function associated with transformation of fibroblasts by oncogenic viruses. I. Chick embryo fibroblast cultures transformed by avian RNA tumor viruses J. Exp. Med. 137 1973 85 111
    • (1973) J. Exp. Med. , vol.137 , pp. 85-111
    • Unkeless, J.C1    Tobia, A2    Ossowski, L3    Quigley, J.P4    Rifkin, D.B5    Reich, E6
  • 140
    • 0030070163 scopus 로고    scopus 로고
    • Autosomal recessive non-syndromic deafness locus (DFNB8) maps on chromosome 21q22 in a large consanguineous kindred from Pakistan
    • A Veske R Oehlmann F Younus A Mohyuddin B Muller-Myhsok S.Q Mehdi A Gal Autosomal recessive non-syndromic deafness locus (DFNB8) maps on chromosome 21q22 in a large consanguineous kindred from Pakistan Hum. Mol. Genet. 5 1996 165 168
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 165-168
    • Veske, A1    Oehlmann, R2    Younus, F3    Mohyuddin, A4    Muller-Myhsok, B5    Mehdi, S.Q6    Gal, A7
  • 141
    • 0031465168 scopus 로고    scopus 로고
    • Identification and cloning of the membrane-associated serine protease, hepsin, from mouse preimplantation embryos
    • T.K.H Vu R.W Liu C.J Haaksma J.J Tomasek E.W Howard Identification and cloning of the membrane-associated serine protease, hepsin, from mouse preimplantation embryos J. Biol. Chem. 272 1997 31315 31320
    • (1997) J. Biol. Chem. , vol.272 , pp. 31315-31320
    • Vu, T.K.H1    Liu, R.W2    Haaksma, C.J3    Tomasek, J.J4    Howard, E.W5
  • 145
    • 0030891703 scopus 로고    scopus 로고
    • The natriuretic-peptide family
    • M.R Wilkins J Redondo L.A Brown The natriuretic-peptide family Lancet 349 1997 1307 1310
    • (1997) Lancet , vol.349 , pp. 1307-1310
    • Wilkins, M.R1    Redondo, J2    Brown, L.A3
  • 146
    • 0037053365 scopus 로고    scopus 로고
    • Processing of pro-atrial natriuretic peptide by corin in cardiac myocytes
    • F Wu W Yan J Pan J Morser Q Wu Processing of pro-atrial natriuretic peptide by corin in cardiac myocytes J. Biol. Chem. 277 2002 16900 16905
    • (2002) J. Biol. Chem. , vol.277 , pp. 16900-16905
    • Wu, F1    Yan, W2    Pan, J3    Morser, J4    Wu, Q5
  • 147
    • 0035256368 scopus 로고    scopus 로고
    • Gene targeting in hemostasis
    • Q Wu Gene targeting in hemostasis Hepsin. Front. Biosci. 6 2001 D192 D200
    • (2001) Hepsin. Front. Biosci. , vol.6 , pp. D192-D200
    • Wu, Q1
  • 148
    • 0032518561 scopus 로고    scopus 로고
    • Generation and characterization of mice deficient in hepsin, a hepatic transmembrane serine protease
    • Q Wu D Yu J Post M Halks-Miller J.E Sadler J Morser Generation and characterization of mice deficient in hepsin, a hepatic transmembrane serine protease J. Clin. Invest. 101 1998 321 326
    • (1998) J. Clin. Invest. , vol.101 , pp. 321-326
    • Wu, Q1    Yu, D2    Post, J3    Halks-Miller, M4    Sadler, J.E5    Morser, J6
  • 150
    • 0036510530 scopus 로고    scopus 로고
    • Spinesin/TMPRSS5, a novel transmembrane serine protease, cloned from human spinal cord
    • N Yamaguchi A Okui T Yamada H Nakazato S Mitsui Spinesin/TMPRSS5, a novel transmembrane serine protease, cloned from human spinal cord J. Biol. Chem. 277 2002 6806 6812
    • (2002) J. Biol. Chem. , vol.277 , pp. 6806-6812
    • Yamaguchi, N1    Okui, A2    Yamada, T3    Nakazato, H4    Mitsui, S5
  • 151
    • 0032496275 scopus 로고    scopus 로고
    • Cloning and characterization of the cDNA for human airway trypsin-like protease
    • K Yamaoka K Masuda H Ogawa K Takagi N Umemoto S Yasuoka Cloning and characterization of the cDNA for human airway trypsin-like protease J. Biol. Chem. 273 1998 11895 11901
    • (1998) J. Biol. Chem. , vol.273 , pp. 11895-11901
    • Yamaoka, K1    Masuda, K2    Ogawa, H3    Takagi, K4    Umemoto, N5    Yasuoka, S6
  • 152
    • 0033591253 scopus 로고    scopus 로고
    • Corin, a mosaic transmembrane serine protease encoded by a novel cDNA from human heart
    • W Yan N Sheng M Seto J Morser Q Wu Corin, a mosaic transmembrane serine protease encoded by a novel cDNA from human heart J. Biol. Chem. 274 1999 14926 14935
    • (1999) J. Biol. Chem. , vol.274 , pp. 14926-14935
    • Yan, W1    Sheng, N2    Seto, M3    Morser, J4    Wu, Q5
  • 153
    • 0034682466 scopus 로고    scopus 로고
    • Corin, a transmembrane cardiac serine protease, acts as a pro-atrial natriuretic peptide-converting enzyme
    • W Yan F Wu J Morser Q Wu Corin, a transmembrane cardiac serine protease, acts as a pro-atrial natriuretic peptide-converting enzyme Proc. Natl. Acad. Sci. USA 97 2000 8525 8529
    • (2000) , pp. 8525-8529
    • Yan, W1    Wu, F2    Morser, J3    Wu, Q4
  • 155
    • 0033724609 scopus 로고    scopus 로고
    • Mice deficient in hepsin, a serine protease, exhibit normal embryogenesis and unchanged hepatocyte regeneration
    • I.S Yu H.J Chen Y.S Lee P.H Huang S.R Lin T.W Tsai S.W Lin Mice deficient in hepsin, a serine protease, exhibit normal embryogenesis and unchanged hepatocyte regeneration Thromb. Haemost. 84 2000 865 870
    • (2000) Thromb. Haemost. , vol.84 , pp. 865-870
    • Yu, I.S1    Chen, H.J2    Lee, Y.S3    Huang, P.H4    Lin, S.R5    Tsai, T.W6    Lin, S.W7
  • 156
    • 0031936659 scopus 로고    scopus 로고
    • Structure of murine enterokinase (enteropeptidase) and expression in small intestine during development
    • X Yuan X Zheng D Lu D.C Rubin C.Y Pung J.E Sadler Structure of murine enterokinase (enteropeptidase) and expression in small intestine during development Am. J. Physiol. 274 1998 G342 G349
    • (1998) Am. J. Physiol. , vol.274 , pp. G342-G349
    • Yuan, X1    Zheng, X2    Lu, D3    Rubin, D.C4    Pung, C.Y5    Sadler, J.E6
  • 157
    • 0032040383 scopus 로고    scopus 로고
    • Expression of the factor VII activating protease, hepsin, in situ in renal cell carcinoma [letter]
    • L.R Zacharski D.L Ornstein V.A Memoli S.M Rousseau W Kisiel Expression of the factor VII activating protease, hepsin, in situ in renal cell carcinoma [letter] Process Citation Thromb. Haemost. 79 1998 876 877
    • (1998) , pp. 876-877
    • Zacharski, L.R1    Ornstein, D.L2    Memoli, V.A3    Rousseau, S.M4    Kisiel, W5
  • 159
    • 0033969013 scopus 로고    scopus 로고
    • Activation of recombinant proenteropeptidase by duodenase
    • T.S Zamolodchikova E.A Sokolova D Lu J.E Sadler Activation of recombinant proenteropeptidase by duodenase FEBS Lett. 466 2000 295 299
    • (2000) FEBS Lett. , vol.466 , pp. 295-299
    • Zamolodchikova, T.S1    Sokolova, E.A2    Lu, D3    Sadler, J.E4
  • 160
    • 0028833203 scopus 로고
    • Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa
    • T.S Zamolodchikova T.I Vorotyntseva V.K Antonov Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa Purification and properties Eur. J. Biochem. 227 1995 866 872
    • (1995) , pp. 866-872
    • Zamolodchikova, T.S1    Vorotyntseva, T.I2    Antonov, V.K3
  • 161
    • 0028877683 scopus 로고
    • Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa
    • T.S Zamolodchikova T.I Vorotyntseva I.V Nazimov G.A Grishina Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa Primary structure of the enzyme Eur. J. Biochem. 227 1995 873 879
    • (1995) , pp. 873-879
    • Zamolodchikova, T.S1    Vorotyntseva, T.I2    Nazimov, I.V3    Grishina, G.A4
  • 162
    • 0033555927 scopus 로고    scopus 로고
    • Apical sorting of bovine enteropeptidase does not involve detergent-resistant association with sphingolipid-cholesterol rafts
    • X Zheng D Lu J.E Sadler Apical sorting of bovine enteropeptidase does not involve detergent-resistant association with sphingolipid-cholesterol rafts J. Biol. Chem. 274 1999 1596 1605
    • (1999) J. Biol. Chem. , vol.274 , pp. 1596-1605
    • Zheng, X1    Lu, D2    Sadler, J.E3
  • 163
    • 0036510358 scopus 로고    scopus 로고
    • Mucin-like domain of enteropeptidase directs apical targeting in Madin-Darby canine kidney cells
    • X Zheng J.E Sadler Mucin-like domain of enteropeptidase directs apical targeting in Madin-Darby canine kidney cells J. Biol. Chem. 277 2002 6858 6863
    • (2002) J. Biol. Chem. , vol.277 , pp. 6858-6863
    • Zheng, X1    Sadler, J.E2
  • 164
    • 0031552052 scopus 로고    scopus 로고
    • Purification and characterization of hepsin from rat liver microsomes
    • A Zhukov U Hellman M Ingelman-Sundberg Purification and characterization of hepsin from rat liver microsomes Biochim. Biophys. Acta 1337 1997 85 95
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 85-95
    • Zhukov, A1    Hellman, U2    Ingelman-Sundberg, M3


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