Immunocytochemical localization of fatty acid metabolizing heat-stable and heat-labile enoyl-coenzyme A (CoA) hydratases in liver and renal cortex

M. Bendayan, M. K. Reddy, T. Hashimoto, J. K. Reddy

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

Two enzymes, the heat-stable and the heat-labile enoyl-coenzyme A (CoA) hydratases, involved in the metabolism of fatty acids, were localized in liver and renal cortex using specific antibodies, immunofluorescence, and the protein A-gold immunocytochemical technique. The qualitative and quantitative results have demonstrated that the heat-stable enoyl-CoA hydratase is a mitochondrial membrane-associated protein of hepatocytes and of epithelial cells in proximal and distal renal tubules. The hepatic sinusoidal cells, as well as the endothelial and epithelial cells of the glomeruli, fail to demonstrate any specific labeling. The heat-labile enoyl-CoA hydratase, on the other hand, was detected in the peroxisomal matrix of hepatocyte and proximal tubule epithelial cells. Its distribution was identical to that of catalase. The significance of the differential distribution of peroxismal and mitochondrial enoyl-CoA hydratases is discussed in relation to their function.

Original languageEnglish (US)
Pages (from-to)509-516
Number of pages8
JournalJournal of Histochemistry and Cytochemistry
Volume31
Issue number4
DOIs
StatePublished - 1983

ASJC Scopus subject areas

  • Anatomy
  • Histology

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