11-cis-Acyl-CoA:retinol O-acyltransferase activity in the primary culture of chicken Muller cells.
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Muniz A, Villazana-Espinoza ET, Thackeray B, Tsin AT
11-cis-Acyl-CoA:retinol O-acyltransferase activity in the primary culture of chicken Muller cells.
Biochemistry. 2006 Oct 10;45(40):12265-73.
- PubMed ID
- 17014079 [ View in PubMed]
- Abstract
A novel retinoid cycle has recently been identified in the cone-dominated chicken retina, and this cone cycle accumulates 11-cis-retinyl esters upon light adaptation. The purpose of this study is to investigate how 11-cis-retinyl esters are formed in the retina. Primary cultures of chicken Muller cells and cell membrane were incubated with all-trans- or 11-cis-retinol to study retinyl ester synthesis. In Muller cells, esterification of 11-cis-retinol was four times greater than esterification of all-trans-retinol. In the presence of palmitoyl-CoA and CRALBP, Muller cell membranes synthesized 11-cis-retinyl ester from 11-cis-retinol at a rate which was 20-fold higher than that of all-trans-retinyl ester. In the absence of CRALBP, 11-cis-retinyl ester synthesis was greatly reduced (by 7-fold). In the absence of palmitoyl-CoA, retinyl ester synthesis was not observed. Muller cell membranes incubated with radiolabeled palmitoyl-CoA resulted in the transfer of the labeled acyl group to retinol. This acyl transfer was greatly reduced in the presence of progesterone, a known ARAT inhibitor. 11-cis-ARAT activity remained unchanged when assayed in the presence of all-trans-retinol, suggesting a distinct catalytic activity from that of all-trans-ARAT. Apparent kinetic rates for 11-cis-ARAT were 0.135 nmol min(-)(1) mg(-)(1) (V(max)) and 11.25 microM (K(M)) and for all-trans-ARAT were 0.0065 nmol min(-)(1) mg(-)(1) (V(max)) and 28.88 microM (K(M)). Our data indicate that Muller cells in the chicken retina possess 11-cis-ARAT activity, thus providing an explanation for the accumulation of 11-cis-retinyl esters in the cone cycle.
DrugBank Data that Cites this Article
- Drug Carriers
Drug Carrier Kind Organism Pharmacological Action Actions Vitamin A Retinaldehyde-binding protein 1 Protein Humans UnknownBinderDetails