Effects of streptozotocin-induced diabetes on microsomal long-chain fatty acyl-CoA synthetase and hydrolase.
Streptozotocin-induced diabetes significantly decreased rat liver microsomal long-chain fatty acyl-CoA (LCA-CoA) hydrolase. The decrease was observed using either palmitoyl-CoA (35 per cent, p less than 0.01) or oleoyl-CoA (23 per cent, p less than 0.01) as the substrate for the enzyme. Under the same conditions, diabetes did not significantly alter activity of LCA-CoA synthetase. Daily subcutaneous injections of protamine zinc insulin (10-12 units/day) into the diabetic rats returned their blood glucose to normal but only partially corrected the LCA-CoA hydrolase activity and did not effect LCA-CoA synthetase activity. The decreased LCA-CoA hydrolase and the unchanged LCA-CoA synthetase activities in the diabetic rat liver were interpreted as factors that may contribute to elevation of fatty acyl-CoA levels in the diabetic liver.
D000818:Animals; D003066:Coenzyme A Ligases / Q000378:metabolism*; D003921:Diabetes Mellitus, Experimental / Q000201:enzymology*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D010170:Palmitoyl-CoA Hydrolase / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D013869:Thiolester Hydrolases / Q000378:metabolism*; D013997:Time Factors; D000098859:Long-Chain-Fatty-Acid-CoA Ligase
D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D013869:Thiolester Hydrolases; D010170:Palmitoyl-CoA Hydrolase; D003066:Coenzyme A Ligases; C090799:FAA2 protein, S cerevisiae; D000098859:Long-Chain-Fatty-Acid-CoA Ligase