메뉴 건너뛰기




Volumn 24, Issue 10, 2010, Pages 3744-3755

The cystatin M/E-cathepsin L balance is essential for tissue homeostasis in epidermis, hair follicles, and cornea

Author keywords

Differentiation; Mouse models; Proteases; Skin barrier; Transglutaminases

Indexed keywords

CATHEPSIN L; CYSTATIN M; LEGUMAIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 3; PROTEINASE; UNCLASSIFIED DRUG; CST6 PROTEIN, MOUSE; CTSL PROTEIN, MOUSE; CYSTEINE PROTEINASE; PRIMER DNA;

EID: 77957854397     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.10-155879     Document Type: Article
Times cited : (37)

References (38)
  • 2
    • 57649155302 scopus 로고    scopus 로고
    • Proteases: Multifunctional enzymes in life and disease
    • Lopez-Otin, C., and Bond, J. S. (2008) Proteases: multifunctional enzymes in life and disease. J. Biol. Chem. 283, 30433-30437
    • (2008) J. Biol. Chem. , vol.283 , pp. 30433-30437
    • Lopez-Otin, C.1    Bond, J.S.2
  • 3
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: Successes, failures and future prospects
    • Turk, B. (2006) Targeting proteases: successes, failures and future prospects. Nat. Rev. Drug Discov. 5, 785-799
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 785-799
    • Turk, B.1
  • 4
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: Multifunctional enzymes in cancer
    • Mohamed, M. M., and Sloane, B. F. (2006) Cysteine cathepsins: multifunctional enzymes in cancer. Nat. Rev. Cancer 6, 764-775
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 5
    • 12344301866 scopus 로고    scopus 로고
    • Epidermal differentiation: The role of proteases and their inhibitors
    • Zeeuwen, P. L. (2004) Epidermal differentiation: the role of proteases and their inhibitors. Eur. J. Cell Biol. 83, 761-773
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 761-773
    • Zeeuwen, P.L.1
  • 6
    • 67349129706 scopus 로고    scopus 로고
    • The biology of cystatin M/E and its cognate target proteases
    • Zeeuwen, P. L., Cheng, T., and Schalkwijk, J. (2009) The biology of cystatin M/E and its cognate target proteases. J. Invest. Dermatol. 129, 1327-1338
    • (2009) J. Invest. Dermatol. , vol.129 , pp. 1327-1338
    • Zeeuwen, P.L.1    Cheng, T.2    Schalkwijk, J.3
  • 7
    • 0031030180 scopus 로고    scopus 로고
    • Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer
    • Sotiropoulou, G., Anisowicz, A., and Sager, R. (1997) Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer. J. Biol. Chem. 272, 903-910
    • (1997) J. Biol. Chem. , vol.272 , pp. 903-910
    • Sotiropoulou, G.1    Anisowicz, A.2    Sager, R.3
  • 8
    • 0033516575 scopus 로고    scopus 로고
    • Inhibition of mammalian legumain by some cystatins is due to a novel second reactive site
    • Alvarez-Fernandez, M., Barrett, A. J., Gerhartz, B., Dando, P. M., Ni, J., and Abrahamson, M. (1999) Inhibition of mammalian legumain by some cystatins is due to a novel second reactive site. J. Biol. Chem. 274, 19195-19203
    • (1999) J. Biol. Chem. , vol.274 , pp. 19195-19203
    • Alvarez-Fernandez, M.1    Barrett, A.J.2    Gerhartz, B.3    Dando, P.M.4    Ni, J.5    Abrahamson, M.6
  • 9
    • 0035018513 scopus 로고    scopus 로고
    • Cystatin M/E expression is restricted to differentiated epidermal keratinocytes and sweat glands: A new skin-specific proteinase inhibitor that is a target for cross-linking by transglutaminase
    • Zeeuwen, P. L., Vlijmen-Willems, I. M., Jansen, B. J., Sotiropoulou, G., Curfs, J. H., Meis, J. F., Janssen, J. J., van Ruissen, F., and Schalkwijk, J. (2001) Cystatin M/E expression is restricted to differentiated epidermal keratinocytes and sweat glands: a new skin-specific proteinase inhibitor that is a target for cross-linking by transglutaminase. J. Invest. Dermatol. 116, 693-701
    • (2001) J. Invest. Dermatol. , vol.116 , pp. 693-701
    • Zeeuwen, P.L.1    Vlijmen-Willems, I.M.2    Jansen, B.J.3    Sotiropoulou, G.4    Curfs, J.H.5    Meis, J.F.6    Janssen, J.J.7    Van Ruissen, F.8    Schalkwijk, J.9
  • 10
    • 0036848352 scopus 로고    scopus 로고
    • A null mutation in the cystatin M/E gene of ichq mice causes juvenile lethality and defects in epidermal cornification
    • Zeeuwen, P. L., Vlijmen-Willems, I. M., Hendriks, W., Merkx, G. F., and Schalkwijk, J. (2002) A null mutation in the cystatin M/E gene of ichq mice causes juvenile lethality and defects in epidermal cornification. Hum. Mol. Genet. 11, 2867-2875
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2867-2875
    • Zeeuwen, P.L.1    Vlijmen-Willems, I.M.2    Hendriks, W.3    Merkx, G.F.4    Schalkwijk, J.5
  • 13
    • 33744915019 scopus 로고    scopus 로고
    • Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site: A novel clue for the role of cystatin M/E in epidermal cornification
    • Cheng, T., Hitomi, K., van Vlijmen-Willems, I. M., de Jongh, G. J., Yamamoto, K., Nishi, K., Watts, C., Reinheckel, T., Schalkwijk, J., and Zeeuwen, P. L. (2006) Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site: a novel clue for the role of cystatin M/E in epidermal cornification. J. Biol. Chem. 281, 15893-15899
    • (2006) J. Biol. Chem. , vol.281 , pp. 15893-15899
    • Cheng, T.1    Hitomi, K.2    Van Vlijmen-Willems, I.M.3    De Jongh, G.J.4    Yamamoto, K.5    Nishi, K.6    Watts, C.7    Reinheckel, T.8    Schalkwijk, J.9    Zeeuwen, P.L.10
  • 14
    • 33845740609 scopus 로고    scopus 로고
    • Colocalization of cystatin M/E and cathepsin V in lamellar granules and corneodesmosomes suggests a functional role in epidermal differentiation
    • Zeeuwen, P. L., Ishida-Yamamoto, A., van Vlijmen-Willems, I. M., Cheng, T., Bergers, M., Iizuka, H., and Schalkwijk, J. (2007) Colocalization of cystatin M/E and cathepsin V in lamellar granules and corneodesmosomes suggests a functional role in epidermal differentiation. J. Invest. Dermatol. 127, 120-128
    • (2007) J. Invest. Dermatol. , vol.127 , pp. 120-128
    • Zeeuwen, P.L.1    Ishida-Yamamoto, A.2    Van Vlijmen-Willems, I.M.3    Cheng, T.4    Bergers, M.5    Iizuka, H.6    Schalkwijk, J.7
  • 18
    • 0041876230 scopus 로고    scopus 로고
    • Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice
    • Shirahama-Noda, K., Yamamoto, A., Sugihara, K., Hashimoto, N., Asano, M., Nishimura, M., and Hara-Nishimura, I. (2003) Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice. J. Biol. Chem. 278, 33194-33199
    • (2003) J. Biol. Chem. , vol.278 , pp. 33194-33199
    • Shirahama-Noda, K.1    Yamamoto, A.2    Sugihara, K.3    Hashimoto, N.4    Asano, M.5    Nishimura, M.6    Hara-Nishimura, I.7
  • 19
    • 54349119307 scopus 로고    scopus 로고
    • Cysteine peptidases, clan CA, cathepsin L
    • 2nd Ed. (Barrett, A. J., Rawlings, N. D., and Woessner, J. F., eds) Elsevier Academic Press, London
    • Kirschke, H. (2004) Cysteine peptidases, clan CA, cathepsin L. In Handbook of Proteolytic Enzymes, 2nd Ed. (Barrett, A. J., Rawlings, N. D., and Woessner, J. F., eds) pp. 1097-1102, Elsevier Academic Press, London
    • (2004) Handbook of Proteolytic Enzymes , pp. 1097-1102
    • Kirschke, H.1
  • 22
    • 0033607637 scopus 로고    scopus 로고
    • Transglutaminase type 1 and its cross-linking activity are concentrated at adherens junctions in simple epithelial cells
    • Hiiragi, T., Sasaki, H., Nagafuchi, A., Sabe, H., Shen, S. C., Matsuki, M., Yamanishi, K., and Tsukita, S. (1999) Transglutaminase type 1 and its cross-linking activity are concentrated at adherens junctions in simple epithelial cells. J. Biol. Chem. 274, 34148-34154
    • (1999) J. Biol. Chem. , vol.274 , pp. 34148-34154
    • Hiiragi, T.1    Sasaki, H.2    Nagafuchi, A.3    Sabe, H.4    Shen, S.C.5    Matsuki, M.6    Yamanishi, K.7    Tsukita, S.8
  • 23
    • 54849408758 scopus 로고    scopus 로고
    • Identification of preferred substrate sequences for transglutaminase 1: Development of a novel peptide that can efficiently detect cross-linking enzyme activity in the skin
    • Sugimura, Y., Hosono, M., Kitamura, M., Tsuda, T., Yamanishi, K., Maki, M., and Hitomi, K. (2008) Identification of preferred substrate sequences for transglutaminase 1: development of a novel peptide that can efficiently detect cross-linking enzyme activity in the skin. FEBS J. 275, 5667-5677
    • (2008) FEBS J. , vol.275 , pp. 5667-5677
    • Sugimura, Y.1    Hosono, M.2    Kitamura, M.3    Tsuda, T.4    Yamanishi, K.5    Maki, M.6    Hitomi, K.7
  • 24
    • 0030761999 scopus 로고    scopus 로고
    • Identification and sequence analysis of two new members of the SKALP/elafin and SPAI-2 gene family: Biochemical properties of the transglutaminase substrate motif and suggestions for a new nomenclature
    • Zeeuwen, P. L., Hendriks, W., de Jong, W. W., and Schalkwijk, J. (1997) Identification and sequence analysis of two new members of the SKALP/elafin and SPAI-2 gene family: biochemical properties of the transglutaminase substrate motif and suggestions for a new nomenclature. J. Biol. Chem. 272, 20471-20478
    • (1997) J. Biol. Chem. , vol.272 , pp. 20471-20478
    • Zeeuwen, P.L.1    Hendriks, W.2    De Jong, W.W.3    Schalkwijk, J.4
  • 31
    • 0035097894 scopus 로고    scopus 로고
    • Elevated expression of transglutaminase 1 and keratinization-related proteins in conjunctiva in severe ocular surface disease
    • Nakamura, T., Nishida, K., Dota, A., Matsuki, M., Yamanishi, K., and Kinoshita, S. (2001) Elevated expression of transglutaminase 1 and keratinization-related proteins in conjunctiva in severe ocular surface disease. Invest. Ophthalmol. Vis. Sci. 42, 549-556
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 549-556
    • Nakamura, T.1    Nishida, K.2    Dota, A.3    Matsuki, M.4    Yamanishi, K.5    Kinoshita, S.6
  • 32
    • 0031764610 scopus 로고    scopus 로고
    • Progressive ataxia, myoclonic epilepsy and cerebellar apoptosis in cystatin B-deficient mice
    • Pennacchio, L. A., Bouley, D. M., Higgins, K. M., Scott, M. P., Noebels, J. L., and Myers, R. M. (1998) Progressive ataxia, myoclonic epilepsy and cerebellar apoptosis in cystatin B-deficient mice. Nat. Genet. 20, 251-258
    • (1998) Nat. Genet. , vol.20 , pp. 251-258
    • Pennacchio, L.A.1    Bouley, D.M.2    Higgins, K.M.3    Scott, M.P.4    Noebels, J.L.5    Myers, R.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.