Plasmalogens in the retina: In situ hybridization of dihydroxyacetone phosphate acyltransferase (DHAP-AT) - the first enzyme involved in their biosynthesis - and comparative study of retinal and retinal pigment epithelial lipid composition
Plasmalogens in the retina: In situ hybridization of dihydroxyacetone phosphate acyltransferase (DHAP-AT) - the first enzyme involved in their biosynthesis - and comparative study of retinal and retinal pigment epithelial lipid composition
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DOI:
10.1016/j.exer.2006.09.009
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发表时间:
2007-01-01
影响因子:
3.4
通讯作者:
Bretillon, Lionel
中科院分区:
文献类型:
--
作者:
Acar, Niyazi;Gregoire, Stephane;Bretillon, Lionel
Plasmalogens (Pis) are phospholipids containing a vinyl-ether bond in the sn-1 position of the glycerol backbone. The physiological role of PIs is still enigmatic, especially within the eye where their deficiency leads to developmental abnormalities. In order to learn more about the functions of Pis in the posterior eye, we evaluated retinal PI content as well as the expression of the first enzyme involved in Pis biosynthesis, dihydroxyacetone phosphate acyltransferase (DHAP-AT) in the retina. In situ hybridization of DHAP-AT mRNA was performed on rat eye sections. The PI contents of calf retina and retinal pigment epithelium (RPE) samples were determined by high-performance liquid chromatography, thin-layer chromatography, and gas chromatography. DHAP-AT was highly expressed in the inner segment of photoreceptors and in the RPE, suggesting two distinct sites for PI biosynthesis. Plasmenyl-ethanolamine was the prominent class of Pis in both neural retina and RPE (28-29% of the total phospho-ethanolamine-glycerides). According to the nature of the alkenyl residue linked to the sn-1 position of Pls, the most striking finding was the greater proportion of octadecanal-aidehyde in the sn-1 position of plasmenyl-ethanolamine of the neural retina compared to all the other classes of Pis in the neural retina and the RPE. These findings might be relevant to the biological functions of Pis against oxidative stress and in the formation of lipid rafts. (c) 2006 Elsevier Ltd. All rights reserved.