The lipidation profile of aquaporin-0 correlates with the acyl composition of phosphoethanolamine lipids in lens membranes

Vian S. Ismail, Jackie A. Mosely, Antal Tapodi, Roy A. Quinlan, John M. Sanderson

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

The lens fiber major intrinsic protein (otherwise known as aquaporin-0 (AQP0), MIP26 and MP26) has been examined by mass spectrometry (MS) in order to determine the speciation of acyl modifications to the side chains of lysine residues and the N-terminal amino group. The speciation of acyl modifications to the side chain of one specific, highly conserved lysine residue (K238) and the N-terminal amino group of human and bovine AQP0 revealed, in decreasing order of abundance, oleoyl, palmitoyl, stearoyl, eicosenoyl, dihomo-γ-linolenoyl, palmitoleoyl and eicosadienoyl modifications. In the case of human AQP0, an arachidonoyl modification was also found at the N-terminus. The relative abundances of these modifications mirror the fatty acid composition of lens phosphatidylethanolamine lipids. This lipid class would be expected to be concentrated in the inner leaflet of the lens fiber membrane to which each of the potential AQP0 lipidation sites is proximal. Our data evidence a broad lipidation profile that is both species and site independent, suggesting a chemical-based ester aminolysis mechanism to explain such modifications.

Original languageEnglish
Pages (from-to)2763-2768
Number of pages6
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1858
Issue number11
DOIs
Publication statusPublished - 1 Nov 2016

Bibliographical note

Funding Information:
The authors thank the Ministry of Higher Education and Scientific Research (grant number 1391 ) of the Kurdistan Regional Government for funding (VSI). The financial support of Fight for Sight UK (grant numbers 1584/1585 ) and the Leverhulme Trust ( RPG-2012-554 , RAQ) is gratefully acknowledged.

Publisher Copyright:
© 2016

Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.

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