Abstract
The formation of coenzyme A thioesters from long-chain fatty acids represents a metabolic branch point. We have isolated, cloned and sequenced a long-chain fatty acyl CoA synthetase (LCFACoAS) that is localized to the endothelium of rabbit heart and aorta. Immunofluoresence and in situ hybridization studies show intense staining of the intimal layer of the aorta and coronary vessels. The microvessels, including the capillaries, of the coronary circulation also show intense immunofluoresence. The enzyme shares only about 30% to 70% homology with the primary amino acid sequence of the other known LCFACoAS. There is a region of 44 amino acids at the carboxy terminus, which is unique to the vascular enzyme. This domain contains the most hydrophobic region of the molecule, indicating that it may function as a membrane anchoring site. These results suggest that this LCFACoAS represents a novel isoform, whose functional significance remains to be determined.
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