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Volumn 3, Issue , 2013, Pages 2772-2778

Kallikrein-Related Peptidase 5

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EID: 84884839489     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-382219-2.00611-6     Document Type: Chapter
Times cited : (2)

References (63)
  • 1
    • 0027303045 scopus 로고
    • Detection and characterization of endogenous protease associated with desquamation of stratum corneum
    • Suzuki Y., Nomura J., Hori J., Koyama J., Takahashi M., Horii I. Detection and characterization of endogenous protease associated with desquamation of stratum corneum. Arch. Dermatol. Res. 1993, 285(6):372-377.
    • (1993) Arch. Dermatol. Res. , vol.285 , Issue.6 , pp. 372-377
    • Suzuki, Y.1    Nomura, J.2    Hori, J.3    Koyama, J.4    Takahashi, M.5    Horii, I.6
  • 2
    • 0029925303 scopus 로고    scopus 로고
    • The role of two endogenous proteases of the stratum corneum in degradation of desmoglein-1 and their reduced activity in the skin of ichthyotic patients
    • Suzuki Y., Koyama J., Moro O., Horii I., Kikuchi K., Tanida M., Tagami H. The role of two endogenous proteases of the stratum corneum in degradation of desmoglein-1 and their reduced activity in the skin of ichthyotic patients. Br. J. Dermatol. 1996, 134(3):460-464.
    • (1996) Br. J. Dermatol. , vol.134 , Issue.3 , pp. 460-464
    • Suzuki, Y.1    Koyama, J.2    Moro, O.3    Horii, I.4    Kikuchi, K.5    Tanida, M.6    Tagami, H.7
  • 3
    • 0033569724 scopus 로고    scopus 로고
    • Purification, molecular cloning, and expression of a human stratum corneum trypsin-like serine protease with possible function in desquamation
    • Brattsand M., Egelrud T. Purification, molecular cloning, and expression of a human stratum corneum trypsin-like serine protease with possible function in desquamation. J. Biol. Chem. 1999, 274(42):30033-30040.
    • (1999) J. Biol. Chem. , vol.274 , Issue.42 , pp. 30033-30040
    • Brattsand, M.1    Egelrud, T.2
  • 4
    • 0033621445 scopus 로고    scopus 로고
    • The New Kallikrein-like Gene, KLK-L2. Molecular characterization, mapping, tissue expression, and hormonal regulation
    • Yousef G.M., Diamandis E.P. The New Kallikrein-like Gene, KLK-L2. Molecular characterization, mapping, tissue expression, and hormonal regulation. J. Biol. Chem. 1999, 274(53):37511-37516.
    • (1999) J. Biol. Chem. , vol.274 , Issue.53 , pp. 37511-37516
    • Yousef, G.M.1    Diamandis, E.P.2
  • 6
    • 54049150854 scopus 로고    scopus 로고
    • Utility of Kallikrein-related peptidases (KLKs) as cancer biomarkers
    • Emami N., Diamandis E.P. Utility of Kallikrein-related peptidases (KLKs) as cancer biomarkers. Clin. Chem. 2008, 54(10):1600-1607.
    • (2008) Clin. Chem. , vol.54 , Issue.10 , pp. 1600-1607
    • Emami, N.1    Diamandis, E.P.2
  • 8
    • 17644381001 scopus 로고    scopus 로고
    • Biochemical and enzymatic characterization of human kallikrein 5 (hK5), a novel serine protease potentially involved in cancer progression
    • [Epub 2005 Feb 15].
    • Michael I.P., Sotiropoulou G., Pampalakis G., Magklara A., Ghosh M., Wasney G., Diamandis E.P. Biochemical and enzymatic characterization of human kallikrein 5 (hK5), a novel serine protease potentially involved in cancer progression. J. Biol. Chem. 2005, 280(15):14628-14635. [Epub 2005 Feb 15].
    • (2005) J. Biol. Chem. , vol.280 , Issue.15 , pp. 14628-14635
    • Michael, I.P.1    Sotiropoulou, G.2    Pampalakis, G.3    Magklara, A.4    Ghosh, M.5    Wasney, G.6    Diamandis, E.P.7
  • 13
    • 38949120099 scopus 로고    scopus 로고
    • Activation of hepatocyte growth factor activator zymogen (pro-HGFA) by human kallikrein 1-related peptidases
    • Mukai S., Fukushima T., Naka D., Tanaka H., Osada Y., Kataoka H. Activation of hepatocyte growth factor activator zymogen (pro-HGFA) by human kallikrein 1-related peptidases. FEBS Journal 2008, 275(5):1003-1017.
    • (2008) FEBS Journal , vol.275 , Issue.5 , pp. 1003-1017
    • Mukai, S.1    Fukushima, T.2    Naka, D.3    Tanaka, H.4    Osada, Y.5    Kataoka, H.6
  • 16
    • 33744962676 scopus 로고    scopus 로고
    • Human tissue kallikrein 5 is a member of a proteolytic cascade pathway involved in seminal clot liquefaction and potentially in prostate cancer progression
    • [Epub 2006 Mar 3]
    • Michael I.P., Pampalakis G., Mikolajczyk S.D., Malm J., Sotiropoulou G., Diamandis E.P. Human tissue kallikrein 5 is a member of a proteolytic cascade pathway involved in seminal clot liquefaction and potentially in prostate cancer progression. J. Biol. Chem. 2006, 281(18):12743-12750. [Epub 2006 Mar 3].
    • (2006) J. Biol. Chem. , vol.281 , Issue.18 , pp. 12743-12750
    • Michael, I.P.1    Pampalakis, G.2    Mikolajczyk, S.D.3    Malm, J.4    Sotiropoulou, G.5    Diamandis, E.P.6
  • 18
    • 33745665581 scopus 로고    scopus 로고
    • Inhibition profiles of human tissue kallikreins by serine protease inhibitors
    • Luo L.-Y., Jiang W. Inhibition profiles of human tissue kallikreins by serine protease inhibitors. Biol. Chem. 2006, 387(6):813-816.
    • (2006) Biol. Chem. , vol.387 , Issue.6 , pp. 813-816
    • Luo, L.-Y.1    Jiang, W.2
  • 20
    • 28244435723 scopus 로고    scopus 로고
    • Inhibition of human kallikreins 5 and 7 by the serine protease inhibitor lympho-epithelial Kazal-type inhibitor (LEKTI)
    • Schechter N.M., Choi E.J., Wang Z.M., Hanakawa Y., Stanley J.R., Kang Y., Clayman G.L., Jayakumar A. Inhibition of human kallikreins 5 and 7 by the serine protease inhibitor lympho-epithelial Kazal-type inhibitor (LEKTI). Biol. Chem. 2005, 386(11):1173-1184.
    • (2005) Biol. Chem. , vol.386 , Issue.11 , pp. 1173-1184
    • Schechter, N.M.1    Choi, E.J.2    Wang, Z.M.3    Hanakawa, Y.4    Stanley, J.R.5    Kang, Y.6    Clayman, G.L.7    Jayakumar, A.8
  • 24
    • 84864278360 scopus 로고    scopus 로고
    • Identification of lympho-epithelial kazal-type inhibitor 2 in human skin as a kallikrein-related peptidase 5-specific protease inhibitor
    • Meyer-Hoffert U., Wu Z., Schröder J.-M. Identification of lympho-epithelial kazal-type inhibitor 2 in human skin as a kallikrein-related peptidase 5-specific protease inhibitor. PLoS ONE 2009, 4(2):e4372.
    • (2009) PLoS ONE , vol.4 , Issue.2
    • Meyer-Hoffert, U.1    Wu, Z.2    Schröder, J.-M.3
  • 26
    • 0021111661 scopus 로고
    • Refined 2 A X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase. Crystallization, structure determination, crystallographic refinement, structure and its comparison with bovine trypsin
    • Bode W., Chen Z., Bartels K., Kutzbach C., Schmidt-Kastner G., Bartunik H. Refined 2 A X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase. Crystallization, structure determination, crystallographic refinement, structure and its comparison with bovine trypsin. J. Mol. Biol. 1983, 164(2):237-282.
    • (1983) J. Mol. Biol. , vol.164 , Issue.2 , pp. 237-282
    • Bode, W.1    Chen, Z.2    Bartels, K.3    Kutzbach, C.4    Schmidt-Kastner, G.5    Bartunik, H.6
  • 27
    • 0016741380 scopus 로고
    • The single calcium-binding site of crystallin bovin beta-trypsin
    • Bode W., Schwager P. The single calcium-binding site of crystallin bovin beta-trypsin. FEBS Lett. 1975, 56(1):139-143.
    • (1975) FEBS Lett. , vol.56 , Issue.1 , pp. 139-143
    • Bode, W.1    Schwager, P.2
  • 28
    • 0023192209 scopus 로고
    • Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution
    • Fujinaga M., James M.N. Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution. J. Mol. Biol. 1987, 195(2):373-396.
    • (1987) J. Mol. Biol. , vol.195 , Issue.2 , pp. 373-396
    • Fujinaga, M.1    James, M.N.2
  • 29
    • 0027050807 scopus 로고
    • The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • Bode W., Turk D., Karshikov A. The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci. 1992, 1(4):426-471.
    • (1992) Protein Sci. , vol.1 , Issue.4 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 33
    • 34547634419 scopus 로고    scopus 로고
    • Distribution of 15 human kallikreins in tissues and biological fluids
    • Shaw J.L.V., Diamandis E.P. Distribution of 15 human kallikreins in tissues and biological fluids. Clin. Chem. 2007, 53(8):1423-1432.
    • (2007) Clin. Chem. , vol.53 , Issue.8 , pp. 1423-1432
    • Shaw, J.L.V.1    Diamandis, E.P.2
  • 34
    • 0034680333 scopus 로고    scopus 로고
    • Sequencing and expression analysis of the serine protease gene cluster located in chromosome 19q13 region
    • Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J., Moss P., Paeper B., Wang K. Sequencing and expression analysis of the serine protease gene cluster located in chromosome 19q13 region. Gene 2000, 257(1):119-130.
    • (2000) Gene , vol.257 , Issue.1 , pp. 119-130
    • Gan, L.1    Lee, I.2    Smith, R.3    Argonza-Barrett, R.4    Lei, H.5    McCuaig, J.6    Moss, P.7    Paeper, B.8    Wang, K.9
  • 35
    • 33847160705 scopus 로고    scopus 로고
    • Coordinated steroid hormone-dependent and independent expression of multiple kallikreins in breast cancer cell lines
    • Paliouras M., Diamandis E. Coordinated steroid hormone-dependent and independent expression of multiple kallikreins in breast cancer cell lines. Breast Cancer Res. Treat. 2007, 102(1):7-18.
    • (2007) Breast Cancer Res. Treat. , vol.102 , Issue.1 , pp. 7-18
    • Paliouras, M.1    Diamandis, E.2
  • 36
    • 2442428082 scopus 로고    scopus 로고
    • Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7
    • Caubet C., Jonca N., Brattsand M., Guerrin M., Bernard D., Schmidt R., Egelrud T., Simon M., Serre G. Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7. J. Invest. Dermatol. 2004, 122(5):1235-1244.
    • (2004) J. Invest. Dermatol. , vol.122 , Issue.5 , pp. 1235-1244
    • Caubet, C.1    Jonca, N.2    Brattsand, M.3    Guerrin, M.4    Bernard, D.5    Schmidt, R.6    Egelrud, T.7    Simon, M.8    Serre, G.9
  • 37
    • 0028326630 scopus 로고
    • The role of proteases in stratum corneum: involvement in stratum corneum desquamation
    • Suzuki Y., Nomura J., Koyama J., Horii I. The role of proteases in stratum corneum: involvement in stratum corneum desquamation. Arch. Dermatol. Res. 1994, 286(5):249-253.
    • (1994) Arch. Dermatol. Res. , vol.286 , Issue.5 , pp. 249-253
    • Suzuki, Y.1    Nomura, J.2    Koyama, J.3    Horii, I.4
  • 39
    • 0034128648 scopus 로고    scopus 로고
    • Stratum corneum tryptic enzyme in normal epidermis: a missing link in the desquamation process?
    • Ekholm I.E., Brattsand M., Egelrud T. Stratum corneum tryptic enzyme in normal epidermis: a missing link in the desquamation process?. J. Invest. Dermatol. 2000, 114(1):56-63.
    • (2000) J. Invest. Dermatol. , vol.114 , Issue.1 , pp. 56-63
    • Ekholm, I.E.1    Brattsand, M.2    Egelrud, T.3
  • 40
    • 47549100856 scopus 로고    scopus 로고
    • A potential role for tissue kallikrein-related peptidases in human cervico-vaginal physiology
    • Shaw J.L.V., Diamandis E.P. A potential role for tissue kallikrein-related peptidases in human cervico-vaginal physiology. Biol. Chem. 2008, 389(6):681-688.
    • (2008) Biol. Chem. , vol.389 , Issue.6 , pp. 681-688
    • Shaw, J.L.V.1    Diamandis, E.P.2
  • 44
    • 34247350818 scopus 로고    scopus 로고
    • Aberrant human tissue kallikrein levels in the stratum corneum and serum of patients with psoriasis: dependence on phenotype, severity and therapy
    • Komatsu N., Saijoh K., Kuk C., Shirasaki F., Takehara K., Diamandis E.P. Aberrant human tissue kallikrein levels in the stratum corneum and serum of patients with psoriasis: dependence on phenotype, severity and therapy. Br. J. Dermatol. 2007, 156(5):875-883.
    • (2007) Br. J. Dermatol. , vol.156 , Issue.5 , pp. 875-883
    • Komatsu, N.1    Saijoh, K.2    Kuk, C.3    Shirasaki, F.4    Takehara, K.5    Diamandis, E.P.6
  • 45
    • 62549139602 scopus 로고    scopus 로고
    • Premature terminal differentiation and a reduction in specific proteases associated with loss of ABCA12 in Harlequin ichthyosis
    • Thomas A.C., Tattersall D., Norgett E.E., O'Toole E.A., Kelsell D.P. Premature terminal differentiation and a reduction in specific proteases associated with loss of ABCA12 in Harlequin ichthyosis. Am. J. Pathol. 2009, 174(3):970-978.
    • (2009) Am. J. Pathol. , vol.174 , Issue.3 , pp. 970-978
    • Thomas, A.C.1    Tattersall, D.2    Norgett, E.E.3    O'Toole, E.A.4    Kelsell, D.P.5
  • 48
    • 1542297612 scopus 로고    scopus 로고
    • Immunofluorometric quantification of human kallikrein 5 expression in ovarian cancer cytosols and its association with unfavorable patient prognosis
    • Diamandis E.P., Borgoño C.A., Scorilas A., Yousef G.M., Harbeck N., Dorn J., Schmalfeldt B., Schmitt M. Immunofluorometric quantification of human kallikrein 5 expression in ovarian cancer cytosols and its association with unfavorable patient prognosis. Tumour Biol. 2003, 24(6):299-309.
    • (2003) Tumour Biol. , vol.24 , Issue.6 , pp. 299-309
    • Diamandis, E.P.1    Borgoño, C.A.2    Scorilas, A.3    Yousef, G.M.4    Harbeck, N.5    Dorn, J.6    Schmalfeldt, B.7    Schmitt, M.8
  • 51
    • 79953309892 scopus 로고    scopus 로고
    • Impact of expression differences of kallikrein-related peptidases and of uPA and PAI-1 between primary tumor and omentum metastasis in advanced ovarian cancer
    • Dorn J., Harbeck N., Kates R., Gkazepis A., Scorilas A., Soosaipillai A., Diamandis E., Kiechle M., Schmalfeldt B., Schmitt M. Impact of expression differences of kallikrein-related peptidases and of uPA and PAI-1 between primary tumor and omentum metastasis in advanced ovarian cancer. Annals of Oncology 2010, 22(4):877-883.
    • (2010) Annals of Oncology , vol.22 , Issue.4 , pp. 877-883
    • Dorn, J.1    Harbeck, N.2    Kates, R.3    Gkazepis, A.4    Scorilas, A.5    Soosaipillai, A.6    Diamandis, E.7    Kiechle, M.8    Schmalfeldt, B.9    Schmitt, M.10
  • 55
    • 79953230837 scopus 로고    scopus 로고
    • Kallikrein-5 promotes cleavage of desmoglein-1 and loss of cell-cell cohesion in oral squamous cell carcinoma
    • Jiang R., Shi Z., Johnson J.J., Liu Y., Stack M.S. Kallikrein-5 promotes cleavage of desmoglein-1 and loss of cell-cell cohesion in oral squamous cell carcinoma. J. Biol. Chem. 2011, 286:9127-9135.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9127-9135
    • Jiang, R.1    Shi, Z.2    Johnson, J.J.3    Liu, Y.4    Stack, M.S.5
  • 56
    • 0036774212 scopus 로고    scopus 로고
    • Differential expression of Kallikrein gene 5 in cancerous and normal testicular tissues
    • Yousef G.M., Obiezu C.V., Jung K., Stephan C., Scorilas A., Diamandis E.P. Differential expression of Kallikrein gene 5 in cancerous and normal testicular tissues. Urology 2002, 60(4):714-718.
    • (2002) Urology , vol.60 , Issue.4 , pp. 714-718
    • Yousef, G.M.1    Obiezu, C.V.2    Jung, K.3    Stephan, C.4    Scorilas, A.5    Diamandis, E.P.6
  • 59
    • 46449093665 scopus 로고    scopus 로고
    • Kallikrein-related peptidases
    • Lundwall A., Brattsand M. Kallikrein-related peptidases. Cell Mol. Life Sci. 2008, 65(13):2019-2038.
    • (2008) Cell Mol. Life Sci. , vol.65 , Issue.13 , pp. 2019-2038
    • Lundwall, A.1    Brattsand, M.2
  • 60
    • 78149358426 scopus 로고    scopus 로고
    • Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs)
    • Goettig P., Magdolen V., Brandstetter H. Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs). Biochimie 2010, 92(11):1546-1567.
    • (2010) Biochimie , vol.92 , Issue.11 , pp. 1546-1567
    • Goettig, P.1    Magdolen, V.2    Brandstetter, H.3
  • 61
    • 47549091175 scopus 로고    scopus 로고
    • Human tissue kallikreins as promiscuous modulators of homeostatic skin barrier functions
    • Eissa A., Diamandis E.P. Human tissue kallikreins as promiscuous modulators of homeostatic skin barrier functions. Biol. Chem. 2008, 389(6):669-680.
    • (2008) Biol. Chem. , vol.389 , Issue.6 , pp. 669-680
    • Eissa, A.1    Diamandis, E.P.2
  • 62
    • 70450231593 scopus 로고    scopus 로고
    • Functional roles of human kallikrein-related peptidases
    • Sotiropoulou G., Pampalakis G., Diamandis E.P. Functional roles of human kallikrein-related peptidases. J. Biol. Chem. 2009, 284(48):32989-32994.
    • (2009) J. Biol. Chem. , vol.284 , Issue.48 , pp. 32989-32994
    • Sotiropoulou, G.1    Pampalakis, G.2    Diamandis, E.P.3
  • 63
    • 33947224164 scopus 로고    scopus 로고
    • Human tissue kallikreins: The cancer biomarker family
    • Paliouras M., Borgoño C., Diamandis E.P. Human tissue kallikreins: The cancer biomarker family. Cancer Lett. 2007, 249(1):61-79.
    • (2007) Cancer Lett. , vol.249 , Issue.1 , pp. 61-79
    • Paliouras, M.1    Borgoño, C.2    Diamandis, E.P.3


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