Skip to main content

Mechanisms of Degradation of Myofibrillar and Nonmyofibrillar Protein in Heart

  • Chapter

Abstract

The degradation of cardiac proteins is known to be altered by many physiological and pathological interventions, but the precise intracellular processes that regulate proteolysis and the relative roles of different proteolytic pathways in degrading different classes of protein remain poorly understood. Agents that interfere with lysosomal function produce major decreases in total protein breakdown; thus, lysosomes and lysosomal proteinases seem to be important in proteolysis. However, these same agents cause no change in the degradation of myofibrillar proteins, suggesting that this class of proteins is not dependent on lysosomal pathways for its turnover.

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

Buying options

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   39.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Barrett, A. J. 1980. The many forms and functions of cellular proteinases. Fed. Proc. 39:9–14.

    PubMed  CAS  Google Scholar 

  2. Dean, R. T. 1980. Regulation and mechanisms of degradation of endogenous proteins by mammalian cells: General considerations. In: K. Wildenthal (ed.), Degradative Processes in Heart and Skeletal Muscle, 3rd ed., pp. 3–30. North-Holland, Amsterdam.

    Google Scholar 

  3. Hoh, J. F. Y., McGrath, P. A., and Hale, P. T. 1978. Electrophoretic analysis of multiple forms of rat cardiac myosin: Effects of hypophysectomy and thyroxine replacement. J. Mol. Cell. Cardiol. 10:1053–1076.

    Article  PubMed  CAS  Google Scholar 

  4. Libby, P., Ingwall, J. S., and Goldberg, A. L. 1979. Reduction of protein degradation and atrophy in cultured fetal mouse hearts by leupeptin. Am. J. Physiol. 237:E35-E39.

    Google Scholar 

  5. Mortimore, G. E., and Ward, W. F. 1976. Behavior of the lysosomal system during organ perfusion. An inquiry into the mechanism of hepatic proteolysis. In: J. T. Dingle and R. T. Dean (eds.), Lysosomes in Biology and Pathology, Vol. 5, pp. 157–184. North-Holland, Amsterdam.

    Google Scholar 

  6. Ord, J. M. 1980. The Effects of Various Hormones and Selective Inhibitors in the Turnover of Subclasses of Cardiac Protein. Ph.D. Thesis, University of Texas Health Science Center at Dallas, Dallas.

    Google Scholar 

  7. Rannels, D. E., Kao, R., and Morgan, H. E. 1975. Effect of insulin on protein turnover in heart muscle. J. Biol. Chem. 250:1694–1701.

    PubMed  CAS  Google Scholar 

  8. Ridout, R. M., Decker, R. S., and Wildenthal, K. 1978. Chloroquine-induced lysosomal abnormalities in cultured foetal mouse hearts. J. Mol. Cell. Cardiol. 10:175–183.

    Article  PubMed  CAS  Google Scholar 

  9. Ward, W. F., Chua, B. L., Li, J. B., Morgan, H. E., and Mortimore, G. E. 1979. Inhibition of basal and deprivation-induced proteolysis by leupeptin and pepstatin in perfused rat liver and heart. Biochem. Biophys. Res. Commun. 87:92–98.

    Article  PubMed  CAS  Google Scholar 

  10. Wibo, M., and Poole, B. 1974. Protein degradation in cultured cells. II. The uptake of chloroquine by rat fibroblasts and the inhibition of cellular protein degradation and cathepsin B,. J. Cell. Biol. 63:430–440.

    Article  PubMed  CAS  Google Scholar 

  11. Wildenthal, K. 1971. Long-term maintenance of spontaneously beating mouse hearts in organ culture. J. Appl. Physiol. 30:153–157.

    PubMed  CAS  Google Scholar 

  12. Wildenthal, K., and Crie, J. S. 1980. The role of lysosomes and lysosomal enzymes in cardiac protein turnover. Fed. Proc. 39:37–41.

    PubMed  CAS  Google Scholar 

  13. Wildenthal, K., and Crie, J. S. 1980. Lysosomes and cardiac protein catabolism. In: K. Wildenthal (ed.) Degradative Processes in Heart and Skeletal Muscle, 3rd ed., pp. 113–129. North-Holland, Amsterdam.

    Google Scholar 

  14. Wildenthal, K., Griffin, E. E., and Ingwall, J. S. 1976. Hormonal control of cardiac protein and amino acid balance. Circ. Res. 38(Suppl. 1): 138–144.

    Google Scholar 

  15. Wildenthal, K., Wakeland, J. R., Morton, P. C., and Griffin, E. E. 1978. Inhibition of protein degradation in mouse hearts by agents that cause lysosomal dysfunction. Circ. Res. 42:787–792.

    Article  PubMed  CAS  Google Scholar 

  16. Wildenthal, K., Wakeland, J. R., Ord, J. M., and Stull, J. T. 1980. Interference with lysosomal proteolysis fails to reduce cardiac myosin degradation. Biochem. Biophys. Res. Commun. 96:793–798.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1983 Springer Science+Business Media New York

About this chapter

Cite this chapter

Ord, J.M., Wakeland, J.R., Crie, J.S., Wildenthal, K. (1983). Mechanisms of Degradation of Myofibrillar and Nonmyofibrillar Protein in Heart. In: Chazov, E., Saks, V., Rona, G. (eds) Advances in Myocardiology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-4441-5_17

Download citation

  • DOI: https://doi.org/10.1007/978-1-4757-4441-5_17

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-4443-9

  • Online ISBN: 978-1-4757-4441-5

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics