Dysregulated proteolytic balance as the basis of excess extracellular matrix in fibrotic disease

American Journal of Physiology - Regulatory Integrative and Comparative Physiology

Volumn 272, Issue 6 41-6, 1997, Pages

  Peters, Craig A ^a,b   Freeman, Michael R ^a,b   Fernandez, Cecilia A ^a   Shepard, Jennifer ^a   Wiederschain, Dmitri G ^a   Moses, Marsha A ^a,b  

^a BOSTON CHILDREN S HOSPITAL   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

Bladder; Fetal; Fibrosis; Metalloproteinases; Obstruction; Tissue inhibitors of metalloproteinases

Indexed keywords

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BILE SECRETION; BLADDER OBSTRUCTION; COLLAGEN METABOLISM; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; EXTRACELLULAR MATRIX; FIBROBLAST; FIBROSIS; GENE EXPRESSION REGULATION; GLOMERULUS FILTRATION RATE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; SHEEP;

EID: 0030837010     PISSN: 03636119     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpregu.1997.272.6.r1960     Document Type: Article

References (18)

1. Aimes, R. T., and J. P. Quigley. Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. J. Biol. Chem. 270: 5872-5876, 1995.
2. Bergman, I., and R. Loxley. Two improved and simplified methods for the spectrophotometric determination of hydroxyproline. Anal. Biochem. 35: 1961-1965, 1963.
3. Birkedal-Hansen, H. Proteolytic remodeling of extracellular matrix. Curr. Opin. Cell Biol. 7: 728-735, 1995.
4. Bou, G. G., J. Osman, C. Black, and I. Olsen. Excess matrix accumulation in scleroderma is caused partly by differential regulation of stromelysin and TIMP-1 synthesis. Clin. Chim. Acta 231: 69-78, 1994.
5. Braunhut, S. J., and M. A. Moses. Retinoids modulate endothelial cell production of matrix-degrading proteases and tissue inhibitors of metalloproteinases (TIMP). J. Biol. Chem. 269: 13472-13479, 1994.
6. Chomczynski, P., and N. Sacchi. Single-step method of RNA isolation by acid guanidinium thiocyanate phenol-chloroform extraction. Anal. Biochem. 162: 156-159, 1987.
7. Diamond, J. R. Macrophages and progressive renal disease in experimental hydronephrosis. Am. J. Kidney Dis. 26: 133-140, 1995.
8. Eddy, A. A., and C. M. Giachelli. Renal expression of genes that promote interstitial inflammation and fibrosis in rats with protein-overload proteinuria. Kidney Int. 47: 1546-1557, 1995.
9. Freeman, M. R., D. J. Bagli, C. C. Lamb, P. D. Guthrie, T. Uchida, R. E. Slavin, and L. W. K. Chung. Culture of a prostatic cell line in basement membrane gels results in an enhancement of malignant properties and constitutive alterations in gene expression. J. Cell. Physiol. 158: 325-336, 1994.
10. Fukuda, Y., M. Imoto, Y. Koyama, Y. Miyazawa, I. Nakano, M. Hattori, F. Urano, S. Kodama, K. Iwata, and T. Hayakawa. Immunohistochemical study on tissue inhibitors of metalloproteinases in normal and pathological human livers. Gastroenterol. Jpn. 26: 37-41, 1991.
11. Giles, K. W., and A. Myers. An improved diphenylamine method for the estimation of deoxyribonucleic acid. Nature 206: 93-95, 1965.
12. Goldberg, M. J., M. A. Moses, and P. C. W. Tsang. Identification of matrix metalloproteinases and metalloproteinase inhibitors in bovine corpora lutea and their variation during the estrous cycle. J. Anim. Sci. 74: 849-857, 1996.
13. Herron, G. S., M. J. Banda, E. J. Clark, J. Gavrilovic, and Z. Werb. Secretion of metalloproteinases by stimulated capillary endothelial cells. II. Expression of collagenase and stromelysin activities is regulated by endogenous inhibitors. J. Biol. Chem. 261: 2814-2818, 1986.
14. Johnson-Wint, B. A quantitative collagen film collagenase assay for large numbers of samples. Anal. Biochem. 104: 175-181, 1980.
15. Juengel, J. L., G. W. Smith, M. F. Smith, R. S. Youngquist, and H. A. Garverick. Pattern of protein production by bovine corpora lutea during luteolysis and characterization of expression of two major secretory products of regressing corpora lutea. J. Reprod. Fertil. 100: 515-520, 1994.
16. Karim, M. A., A. G. Ferguson, B. T. Wakim, and A. M. Samarel. In vivo collagen turnover during development of thyroxine-induced left ventricular hypertrophy. Am. J. Physiol. 260 (Cell Physiol. 29): C316-C326, 1991.
17. Lafuma, C., R. A. El Nabout, F. Crechet, A. Hovnanian, and M. Martin. Expression of 72-kDa gelatinase (MMP-2), collagenase (MMP-1), and tissue metalloproteinase inhibitor (TIMP) in primary pig skin fibroblast cultures derived from radiation-induced skin fibrosis. J. Invest. Dermatol. 102: 945-950, 1994.
18. Minoja, M., G. Hirschman, C. Jones, L. Agodoa, and G. Striker. Incidence and causes of ESRD in children in the USA (Abstract). J. Am. Soc. Nephrol. 6: 396, 1995.