The lipidation profile of aquaporin-0 correlates with the acyl composition of phosphoethanolamine lipids in lens membranes
| Autor: | John M. Sanderson, Vian S. Ismail, Roy A. Quinlan, Antal Tapodi, Jackie A. Mosely |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Lipoylation Lysine Biophysics Gene Expression Aquaporin Lipid-anchored protein Arachidonic Acids Biology Aquaporins Biochemistry Young Adult 03 medical and health sciences chemistry.chemical_compound Aminolysis Lens Crystalline Side chain Animals Humans Eye Proteins Phosphatidylethanolamine Membranes 030102 biochemistry & molecular biology Cell Biology Lens Fiber 030104 developmental biology Membrane chemistry Ethanolamines Cattle lipids (amino acids peptides and proteins) Protein Processing Post-Translational |
| Zdroj: | Biochimica et Biophysica Acta (BBA)-Biomembranes, 2016, Vol.1858(11), pp.2763-2768 [Peer Reviewed Journal] |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/j.bbamem.2016.06.026 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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