PMID: 6165350Jan 1, 1981Paper

Negatively charged sites and calcium binding in the isolated rat heart sarcolemma

Basic Research in Cardiology
M P MatsukuboN S Dhalla

Abstract

Colloidal iron staining, calcium binding and enzyme activities were studied in the isolated rat heart sarcolemma. Colloidal iron staining of the sarcolemma revealed a high density of negatively charged sites associated with the cell surface. This membrane fraction was found to have calcium binding activity at both low (0.1 mM) and high (1.25 mM) concentrations of calcium. Pretreatment of the sarcolemma with either trypsin, phospholipase C or neuraminidase, was associated with a reduction in colloidal iron staining as well as decreased calcium-binding activity at high concentrations of calcium. Calcium binding at low concentrations was decreased by both trypsin and neuraminidase. Mg2+ ATPase, Ca2+ ATPase, and Na+-K+ ATPase activities were altered by neuraminidase and trypsin treatments, whereas phospholipase C treatment altered Na+-K+ ATPase only. It is concluded that both surface negative charge and calcium-binding sites associated with the isolated rat heart sarcolemma are contributed by a mosaic of biomolecules including proteins, phospholipids and glycoproteins, and alterations in the surface charge may influence the activities of membrane-bound enzymes.

References

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Citations

Dec 1, 1988·Molecular and Cellular Biochemistry·P K Singal, J G Tong
Jan 1, 1982·The International Journal of Biochemistry·V PanagiaN S Dhalla
Sep 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·G N PierceN S Dhalla
Jan 15, 1990·Biochimica Et Biophysica Acta·M KanekoN S Dhalla
Jan 1, 1990·Circulation Research·Y TairaN S Dhalla
Nov 1, 1984·Circulation Research·M B Frankis, G E Lindenmayer
Jul 1, 1983·Basic Research in Cardiology·M P MoffatN S Dhalla
Sep 1, 1983·The American Journal of Physiology·G N Pierce, N S Dhalla

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