Phospholipid dependence of rat liver microsomal acyl:CoA synthetase and acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase
| Autor: | Kamen Koumanov, Albena B. Momchilova-Pankova, Tania Markovska, Svetlana E. Koshlukova |
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| Rok vydání: | 1992 |
| Předmět: |
Male
Saccharomyces cerevisiae Proteins Physiology Membrane Fluidity Membrane lipids Biophysics Phospholipid In Vitro Techniques chemistry.chemical_compound Membrane Lipids Phospholipase A2 Coenzyme A Ligases Membrane fluidity Animals Phospholipids Phosphatidylethanolamine biology technology industry and agriculture 1-Acylglycerophosphocholine O-Acyltransferase Rats Inbred Strains Cell Biology Rats Repressor Proteins chemistry Biochemistry Acyltransferase Dipalmitoylphosphatidylcholine Type C Phospholipases biology.protein Microsomes Liver lipids (amino acids peptides and proteins) Sphingomyelin Carrier Proteins Acyltransferases |
| Zdroj: | The Journal of membrane biology. 127(2) |
| ISSN: | 0022-2631 |
| Popis: | Investigations were performed on the influence of the phospholipid composition and physicochemical properties of the rat liver microsomal membranes on acyl-CoA synthetase and acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase activities. The phospholipid composition of the membranes was modified by incubation with different phospholipids in the presence of lipid transfer proteins or by partial delipidation with exogenous phospholipase C and subsequent enrichment with phospholipids. The results indicated that the incorporation of phosphatidylglycerol, phosphatidylserine and phosphatidylethanolamine induced a marked activation of acyl-CoA synthetase for both substrates used--palmitic and oleic acids. Sphingomyelin occurred as specific inhibitor for this activity especially for palmitic acid. Palmitoyl-CoA: and oleoyl-CoA: 1-acyl-sn-glycero-3-phosphocholine acyltransferase activities were found to depend on the physical state of the membrane lipids. The alterations in the membrane physical state were estimated using two different fluorescent probes--1,6-diphenyl-1,3,5-hexatriene and pyrene. In all cases of membrane fluidization this activity was elevated. On the contrary, in more rigid membranes obtained by incorporation of sphingomyelin and dipalmitoylphosphatidylcholine, acyltransferase activity was reduced for both palmitoyl-CoA and oleoyl-CoA. We suggest a certain similarity in the way of regulation of membrane-bound acyltransferase and phospholipase A2 which both participate in the deacylation-reacylation cycle. |
| Databáze: | OpenAIRE |
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