Increased acylation of lysophosphatidylcholine in microsomes of trembler mouse peripheral nerves
| Autor: | Claude Cassagne, Anthony M. Heape, Hélène Juguelin, Françoise Boiron-Sargueil |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
biology
Cell Biology Trembler biology.organism_classification Cellular and Molecular Neuroscience chemistry.chemical_compound Transacylation Lysophosphatidylcholine medicine.anatomical_structure chemistry Biochemistry Peripheral nervous system biology.protein Microsome medicine lipids (amino acids peptides and proteins) Specific activity Sciatic nerve Bovine serum albumin |
| Zdroj: | Neurochemistry international. 13(3) |
| ISSN: | 0197-0186 |
| Popis: | We report here the presence of a Stearoyl-CoA: [1-palmitoyl]-glycerophosphorylcholine (LPC) transacylase activity in the microsomal fraction of normal and Trembler mouse sciatic nerves. Under the experimental conditions studied as a function of incubation time, protein concentration, acyl-CoA and LPC concentrations, the transacylase specific activity was 2–3 times higher in the microsomes of the mutant's nerves than in those of the control. The addition of 5 mM ATP-Mg to the incubation medium, in the absence of bovine serum albumin, leads to a 90% decrease of the stearoyl-CoA thioesterase activity, but increases the transacylation by only 10–20%. This may be due to the low value (10 μM) of the apparent Km for C18-CoA observed for the mutant's transacylase. In microsomes from control nerves, transacylation requires exogenous LPC, whereas in Trembler mouse sciatic nerve microsomes, the transacylase can use endogenous LPC. |
| Databáze: | OpenAIRE |
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