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

Niyazi Acar, Stephane Gregoire, Agnes Andre, Pierre Juaneda, Corinne Joffre, Alain M. Bron, Catherine P. Creuzot-Garcher, Lionel Bretillon
Experimental Eye Research. 2007-01-01; 84(1): 143-151
DOI: 10.1016/j.exer.2006.09.009

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1. Exp Eye Res. 2007 Jan;84(1):143-51. Epub 2006 Nov 1.

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.

Acar N(1), Gregoire S, Andre A, Juaneda P, Joffre C, Bron AM, Creuzot-Garcher CP,
Bretillon L.

Author information:
(1)National Institute for Research on Agronomy, UMR FLAVIC, Eye and Nutrition
Research Group, and Department of Ophthalmology, University Hospital, Dijon
Cedex, France.

Plasmalogens (Pls) are phospholipids containing a vinyl-ether bond in the sn-1
position of the glycerol backbone. The physiological role of Pls is still
enigmatic, especially within the eye where their deficiency leads to
developmental abnormalities. In order to learn more about the functions of Pls in
the posterior eye, we evaluated retinal Pl content as well as the expression of
the first enzyme involved in Pls biosynthesis, dihydroxyacetone phosphate
acyltransferase (DHAP-AT) in the retina. In situ hybridization of DHAP-AT mRNA
was performed on rat eye sections. The Pl 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 Pl biosynthesis. Plasmenyl-ethanolamine was the
prominent class of Pls 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-aldehyde in the sn-1 position of plasmenyl-ethanolamine
of the neural retina compared to all the other classes of Pls in the neural
retina and the RPE. These findings might be relevant to the biological functions
of Pls against oxidative stress and in the formation of lipid rafts.

DOI: 10.1016/j.exer.2006.09.009
PMID: 17081518 [Indexed for MEDLINE]

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