Lysosomal vacuolar apparatus of cardiac myocytes in heart of starved and refed rabbits

Decker, R.S.; Decker, M.L.; Herring, G.H.; Morton, P.C.; Wildenthal, K.

Journal of Molecular and Cellular Cardiology 12(11): 1175-1189

1980


ISSN/ISBN: 0022-2828
DOI: 10.1016/0022-2828(80)90064-4
Accession: 070290538

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Abstract
The cardiac lysosomal changes that accompany prolonged starvation and refeeding were studied using biochemical, immunohistochemical and cytochemical techniques. Biochemical activities of lysosomal enzymes changed in a heterogeneous manner during starvation: cathepsin D increased significantly, acid phosphatase and .beta.-glucosaminidase were altered minimally and cathepsin B decreased significantly. During 1-3 days of refeeding, all activities returned toward normal except acid phosphatase. Morphological studies revealed that the increases in cathepsin D and acid phosphatase were localized in elements of the endoplasmic reticulum, Golgi complex and secondary lysosomes; upon refeeding these acid hydrolases were incorporated within autophagic vacuoles with simultaneous loss of staining within the endoplasmic reticulum. Different cardiac lysosomal proteinases evidently are not regulated in a coordinate manner during starvation. Changes in cathepsin D appear more likely to play an important metabolic role during the period of refeeding than during the period of starvation per se.