Mechanisms of renal tubular cell hypertrophy: Mitogen-induced suppression of proteolysis

American Journal of Physiology - Cell Physiology

Volumn 273, Issue 3 42-3, 1997, Pages

  Franch, Harold A ^a   Curtis, Patryce V ^b   Mitch, William E ^b  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NONE

Author keywords

Calpains; Epidermal growth factor; Lysosomes; Proteasomes; Transforming growth factor

Indexed keywords

CALPAIN; EPIDERMAL GROWTH FACTOR; MITOGENIC AGENT; PROTEASOME; TRANSFORMING GROWTH FACTOR BETA1;

ANIMAL CELL; ARTICLE; CELL HYPERPLASIA; CONTROLLED STUDY; KIDNEY TUBULE CELL; LYSOSOME; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; RABBIT;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0030793837     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1997.273.3.c843     Document Type: Article

References (31)

1. 1 renal epithelial cells. Kidney Int. 45: 642-649, 1994.
2. Ballard, F. J., S. S. C. Wong, S. E. Knowles, N. C. Partridge, T. J. Martin, C. M. Wood, and J. M. Gunn. Insulin inhibition of protein degradation in cell monolayers. J. Cell. Physiol. 105: 335-346, 1980.
3. De Larco, J. E., and G. J. Todaro. Epithelioid and fibroblastic rat kidney cell clones: epidermal growth factor (EGF) and the effect of mouse sarcoma virus transformation. J. Cell. Physiol. 94: 335-342, 1978.
4. Dice, J. F., and S. R. Terlecky. Selective degradation of cytosolic proteins by lysosomes. In: Cellular Proteolytic Systems, edited by A. J. Ciechanover and A. L. Schwartz. New York: Wiley-Liss, 1994, p. 55-64.
5. Edelstein, C. L., E. D. Wieder, M. M. Yaqoob, P. E. Gengaro, T. J. Burke, R. A. Nemenoff, and R. W. Schrier. The role of cysteine proteases in hypoxia-induced rat renal proximal tubular injury. Proc. Natl. Acad. Sci. USA 92: 7662-7666, 1995.
6. Eleftheriades, E. G., J. B. Durand, A. G. Ferguson, G. L. Engelmann, S. B. Jones, and A. M. Samarel. Regulation of procollagen metabolism in the pressure-overloaded rat heart. J. Clin. Invest. 91: 1113-1122, 1993.
7. + antiport activity. Proc. Natl. Acad. Sci. USA 82: 6163-6166, 1985.
8. 4Cl-induced hypertrophy is mediated by weak base effects and is independent of cell cycle processes. Am. J. Physiol. 270 (Cell Physiol. 39): C932-C938, 1996.
9. Franch, H. A., J. W. Shay, R. J. Alpern, and P. A. Preisig. Involvement of pRB family in TGFβ-dependent epithelial cell hypertrophy. J. Cell Biol. 129: 245-254, 1995.
10. Furuno, K., and A. L. Goldberg. The activation of protein degradation in muscle by calcium or muscle injury does not involve a lysosomal mechanism. Biochem. J. 237: 859-864, 1986.
11. 4Cl. J. Clin. Invest. 84: 1767-1779, 1989.
12. Kanada, K., M. Tamai, K. Adachi, K. Oguma, K. Kashiwagi, S. Ohuma, E. Kominami, T. Towatari, and N. Katunuma. Characterization of three new analogs of E-64 and their therapeutic application. In: Proteinase Inhibitors: Medical and Biological Aspects, edited by N. Katunuma. Tokyo: Springer-Verlag, 1983, p. 25-36.
13. Hostetter, T. H. Progression of renal disease and renal hypertrophy. Annu. Rev. Physiol. 57: 263-278, 1995.
14. 1 cells. Kidney Int. 42: 595-601, 1992.
15. Ling, H., S. Vamvakas, G. Busch, J. Dammrich, L. Schramm, F. Lang, and A. Heidland. Suppressing role of transforming growth factor-β1 on cathepsin activity in cultured kidney tubule cells. Am. J. Physiol. 269 (Renal Fluid Electrolyte Physiol. 38): F911-F917, 1995.
16. Matrisian, L. M., K. D. Rodland, and B. E. Magun. Disruption of intracellular processing of epidermal growth factor by methylamine inhibits epidermal growth factor-induced DNA synthesis but not early morphological or transcriptional events. J. Biol. Chem. 262: 6908-6913, 1987.
17. Mitch, W. E., and A. L. Goldberg. Mechanisms of muscle wasting: the role of the ubiquitin-proteasome pathway. N. Engl. J. Med. 335: 1897-1905, 1996.
18. Norman, J. T., and L. G. Fine. Renal growth and hypertrophy. In: Textbook of Nephrology, edited by S. G. Massry and R. J. Glassock. Baltimore: Williams & Wilkins, 1995, p. 146-158.
19. Olbricht, C. J., and E. Geissinger. Renal hypertrophy in streptozotocin diabetic rats: role of proteolytic lysosomal enzymes. Kidney Int. 41: 966-972, 1992.
20. Oshima, M., S. Koizumi, K. Fujita, and G. Guroff. Nerve growth factor-induced decrease in the calpain activity of PC12 cells. J. Biol. Chem. 264: 20811-20816, 1989.
21. Palombella, V. J., O. J. Rando, A. L. Goldberg, and T. Maniatis. The ubiquitin-proteasome pathway is required for processing the NK-kB1 precursor protein and activation of NF-kB. Cell 78: 773-785, 1995.
22. Roberts, A. B., B. K. McCune, and M. B. Sporn. TGFβ1: regulation of extracellular matrix. Kidney Int. 41: 557-559, 1996.
23. Rocco, M. V., Y. Chen, S. Goldfarb, and F. N. Ziyadeh. Elevated glucose stimulates TGFβ gene expression and bioactivity in proximal tubule. Kidney Int. 41: 107-114, 1992.
24. Rock, K. L., C. Gramm, L. Rothstein, K. Clark, R. Stein, D. Lawrence, D. Hwang, and A. L. Goldberg. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78: 761-771, 1994.
25. Schaefer, L., T. Lorenz, J. Daemmrich, A. Heidland, and R. M. Schaefer. Role of proteinases in renal hypertrophy and matrix accumulation. Nephrol. Dial. Transplant. 10: 801-807, 1995.
26. Sharma, K., J. Guo, Y. Jin, and F. N. Ziyadeh. Neutralization of TGF-β by anti-TGF-β antibody attenuates kidney hypertrophy and the enhanced extracellular matrix expression in STZ-induced diabetic mice. Diabetes 45: 522-530, 1996.
27. Shechter, P., G. Boner, and R. Rabkin. Tubular cell protein degradation in early diabetic renal hypertrophy. J. Am. Soc. Nephrol. 4: 1582-1587, 1994.
28. Shechter, P., J. D. Shi, and R. Rabkin. Renal tubular cell protein breakdown in uninephrectomized and ammonium chloride-loaded rats. J. Am. Soc. Nephrol. 5: 1201-1207, 1994.
29. Tsao, T. C., J. D. Shi, G. E. Mortimore, E. J. Cragoe, and R. Rabkin. Modulation of kidney cell protein degradation by insulin. J. Lab. Clin. Med. 116: 369-376, 1990.
30. Wang, K. K. W., R. Nath, A. Posner, K. J. Raser, M. Buroker-Kilgore, I. Hajimohammadreza, A. W. Probert, F. W. Marcoux, Q. Ye, E. Tanko, M. Hatanka, M. Maki, H. Caner, J. L. Collins, A. Fergus, K. S. Lee, E. A. Lunney, S. J. Hays, and P. W. Yuen. An alpha-mercaptoacrylic acid derivative is a selective nonpeptide cell-permeable calpain inhibitor and is neuroprotective. Proc. Natl. Acad. Sci. USA 93: 6687-6692, 1996.
31. Wing, S. S., and A. L. Goldberg. Glucocorticiods activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E668-E676, 1993.