Skip to main content
Log in

Influence of protein nutrition on calpain activity of mouse kidney: Modulation by calpastatin

  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Abstract

The effect of protein depletion and refeeding with a normal diet on calpain activity was examined in mouse kidney soluble homogenate. In terms of units per gram of protein, it increased 2.9 times with depletion and decreased upon refeeding. After a DEAE-Sephacel chromatography, the homogenate yielded three enzymatic activities. Their sum, assessed as total calpain activity, was higher than the activity measured before fractionation and did not appreciably change during protein depletion and refeeding. Because the proportion of total activity displayed by the complete homogenate increased with depletion and decreased with refeeding, a low calpastatin content in depleted kidney was envisaged. This was confirmed by direct estimations: depleted kidney had 6 times less calpastatin compared to both normal and 16 h refed tissue. We concluded that a decrease in calpastatin content contributes to an increased calpain activity related to degradable protein in protein depleted kidney. In view of this, it seems not unlikely that the in vivo rate of protein breakdown depicted by kidney during protein depletion and refeeding is in part effected through modulation of the calpain proteolytic system. (Mol Cell Biochem 166: 95-99, 1997)

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Bur, JA, Conde RD: Decreased rate of protein breakdown during nutritional recovery of mouse kidney. Am J Physiol 243: E360-E364, 1982

    Google Scholar 

  2. Mortimore GE: Regulation of the lysospmal pathway in intracellular protein degradation. In HL Segal, M Rothstein and E Bergamini, (eds). Protein Metabolism in Aging. Wiley-Liss Inc., New York, 1990, p. 117

    Google Scholar 

  3. Ciechanover A, Gropper R, Schwartz AL: The ubiquitin-activating enzyme is required for lysosomal degradation of cellular proteins under stress. Biomed Biochim Acta 50: 321–332, 1991

    Google Scholar 

  4. Mayer RJ, Lowe J, Landon M, McDermott H, Tuckwell J, Doherty F, Laszlo L: Ubiquitin and the lysosome system: Molecular immunopathology reveals the connection. Biomed Acta 50: 333–341, 1991

    Google Scholar 

  5. Murachi T: Calpain and calpastatin. Trends Biochem Sci 8: 167–169, 1983

    Google Scholar 

  6. Pontremolli S, Melloni E: Extralysosomal protein degradation. Ann Rev Biochem 55: 455–481, 1986

    Google Scholar 

  7. Schollmeyer JE: Calpain II involvement in mitosis. Science 240: 911–913, 1989

    Google Scholar 

  8. Suzuki K, Imajoh S, Emori V, Kawasaki H, Minami V, Ohno S: Calcium-activated neutral protease and its endogenous inhibitor. FEBS Lett 220: 271–277, 1987

    Google Scholar 

  9. Saido TC, Mizuno K, Suzuki K: Proteolysis of protein kinase C by calpain: Effect of acidic phospholipids. Biomed Biochim Acta 50: 485–489, 1991

    Google Scholar 

  10. Goicoechea SM, Tabares ML, Sabas ME, Pucciarelli MG, Conde RD: Effect of dietary level of protein on the activity of mouse liver calpain. Horm Metab Res 26: 175–180, 1994

    Google Scholar 

  11. Udenfriend S, Stein S, Bohlen P, Dairman W, Leingruber W, Weigele M: Fluorescamine: A reagent for assay of amino acids, peptides, proteins and primary amines in the picomole range. Science 178: 871–872, 1972

    Google Scholar 

  12. De Santis E, Pompili E, De Renzis G, Bondi AM, Menghi G, Collier WL, Fumagalli L: Calpain inhibitor in rabbit skeletal muscle: an immunochemical study. Histochemistry 97: 263–267, 1992

    Google Scholar 

  13. Nakamura M, Inomata M, Imajoh S, Suzuki K, Kawashima S: Fragmentation of an endogenous inhibitor upon complex formation with high-and low-Ca2+-requiring forms of calcium-activated neutral protease from rabbit skeletal muscle. J Biochem 90: 1583–1589, 1989

    Google Scholar 

  14. Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685, 1970

    Google Scholar 

  15. Goa J: A micro-biuret method for protein determination. Scand J Clin Lab Invest 5: 218–222, 1953

    Google Scholar 

  16. Clark, AF, De Martino GN, Croall, DE: Fractionation and quantification of calcium dependent proteinase activity from small tissue samples. Biochem J 235: 279–282, 1986

    Google Scholar 

  17. Suzuki K, Ohno S, Emori V, Imajob S, Kawasaki H: Calcium-activated neutral protease (CANP) and its biological and medical implications. Progress in Clinical Biochemistry and Medicine, Berlin, Springer-Verlag, 1987, vol. 5, p. 43

    Google Scholar 

  18. Cassta RO, Sanllorenti PM, Conde RD: Proteolytie activities in kidney and liver during refeeding of protein depleted mice. Acta Physiol Pharmacol Latinoam 39: 235–244, 1989

    Google Scholar 

  19. Fagan, JM, Wajnberg EW, Culbert L, Waxman LI: ATP depletion stimulates calcium dependent protein breakdown in chick skeletal muscle. Am J Physiol 262: E637-E643, 1992

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Goicoechea, S.M., Conde, R.D. Influence of protein nutrition on calpain activity of mouse kidney: Modulation by calpastatin. Mol Cell Biochem 166, 95–99 (1997). https://doi.org/10.1023/A:1006814724232

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1006814724232

Navigation