Importance of lysosomal cysteine proteases in lung disease

被引：78
作者：
Wolters P.J. [1 ]
Chapman H.A. [1 ]
机构：
[1] Department of Medicine, Cardiovascular Research Institute, University of California, San Francisco, CA
来源：
Respiratory Research | / 1卷 / 3期
关键词：
asthma; cathepsin; emphysema; extracellular matrix; invariant chain;
D O I：
10.1186/rr29
中图分类号：
学科分类号：
摘要：
The human lysosomal cysteine proteases are a family of 11 proteases whose members include cathepsins B, C, H, L, and S. The biology of these proteases was largely ignored for decades because of their lysosomal location and the belief that their function was limited to the terminal degradation of proteins. In the past 10 years, this view has changed as these proteases have been found to have specific functions within cells. This review highlights some of these functions, specifically their roles in matrix remodeling and in regulating the immune response, and their relationship to lung diseases. © Current Science Ltd.
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  • [1] Chapman Jr H.A., Shi G.P., Protease injury in the development of COPD: Thomas A, Neff Lecture. Chest, 117, pp. 295S-299S, (2000)
  • [2] Riese R.J., Chapman H.A., Cathepsins and compartmentalization in antigen presentation, Curr Opin Immunol, 12, pp. 107-113, (2000)
  • [3] Hart T.C., Hart P.S., Bowden D.W., Michalec M.D., Callison S.A., Walker S.J., Zhang Y., Firatli E., Mutations of the cathepsin C gene are responsible for Papillon-Lefevre syndrome, J Med Genet, 36, pp. 881-887, (1999)
  • [4] Gelb B.D., Shi G.P., Chapman H.A., Desnick R.J., Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency, Science, 273, pp. 1236-1238, (1996)
  • [5] Toomes C., James J., Wood A.J., Wu C.L., McCormick D., Lench N., Hewitt C., Moynihan L., Roberts E., Woods C.G., Markham A., Wong M., Widmer R., Ghaffar K.A., Pemberton M., Hussein I.R., Temtamy S.A., Davies R., Read A.P., Sloan P., Dixon M.J., Thakker N.S., Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis, Nat Genet, 23, pp. 421-424, (1999)
  • [6] Pham C.T.N., Armstrong R.J., Zimonjic D.B., Popescu N.C., Payan D.G., Ley T.J., Molecular cloning, chromosomal localization, and expression of murine dipeptidyl peptidase I, J Biol Chem, 272, pp. 10695- 10703, (1997)
  • [7] Rao N.V., Rao G.V., Hoidal J.R., Human dipeptidyl-peptidase I, Gene characterization, localization, and expression. J Biol Chem, 272, pp. 10260-10265, (1997)
  • [8] Wolters P.J., Raymond W.W., Blount J.L., Caughey G.H., Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I, J Biol Chem, 273, pp. 15514-15520, (1998)
  • [9] Drake F.H., Dodds R.A., James I.E., Connor J.R., Debouck C., Richardson S., Lee-Rykaczewski E., Coleman L., Rieman D., Barthlow R., Hastings G., Gowen M., Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts, J Biol Chem, 271, pp. 12511- 12516, (1996)
  • [10] Buhling F., Gerber A., Hackel C., Kruger S., Kohnlein T., Bromme D., Reinhold D., Ansorge S., Welte T., Expression of cathepsin K in lung epithelial cells, Am J Resp Cell Mol Biol, 20, pp. 612-619, (1999)
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