Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8299246 | Biochimica et Biophysica Acta (BBA) - Bioenergetics | 2008 | 6 Pages |
Abstract
Native uncoupling protein 1 was purified from rat brown adipose tissue of cold-acclimated rats and rats kept at room temperature, in the presence of phosphatase inhibitors. The purified protein from cold-acclimated animals was digested with trypsin and immobilized metal affinity chromatography was used to select for phosphopeptides. Tandem mass spectroscopic analysis of the peptides derived from uncoupling protein 1, suggests phosphorylation of serine 3 or 4 and identified phosphorylation of serine 51. Furthermore, we were able to demonstrate that antibodies to phosphoserine detect full-length UCP 1 and that the proportion of phosphoserine on UCP1, purified from cold-acclimated rats, was significantly greater than that on UCP 1 from rats kept at room temperature (90 ± 4% compared to 62 ± 8%, p = 0.013), respectively). We conclude that uncoupling protein 1 is a phosphoprotein and that cold-acclimation increases the proportion of UCP1 that is serine phosphorylated.
Keywords
octyl-POEUCPFBSHTPBATTFAIMACACNTBSBSAbovine serum albuminAcetonitrileTrifluoroacetic acidCovalent modificationSDS-PAGEsodium dodecylsulphate polyacrylamide gel electrophoresisbrown adipose tissueTris-buffered salineUncoupling protein-1foetal bovine serumTandem mass spectroscopySerine phosphorylationHydroxyapatiteUncoupling proteinimmobilized metal affinity chromatography
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Authors
Audrey M. Carroll, Richard K. Porter, Nick A. Morrice,