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Updated: Aug 9, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
P-selectin is acylated with palmitic acid and stearic acid at cysteine 766 through a thioester linkage
T Fujimoto1, E Stroud, R E Whatley
1W. K. Warren Medical Research Institute, Department of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City 73104.
Abstract:
We report that the adhesion receptor P-selectin can be metabolically labeled with [3H]palmitic acid in human platelets. Analysis of alkaline methanolysis products from labeled protein demonstrated that the radioactivity associated with P-selectin was covalently bound palmitic acid. [3H]Palmitic acid was cleaved by hydroxylamine treatment at neutral pH and by reducing agents, indicating that acylation occurred through a thioester linkage. Both stearic acid and palmitic acid were detected by gas chromatography-mass spectrometry analysis of alkaline hydrolysates of purified P-selectin. Deletion or mutation of Cys766 eliminated [3H] palmitic acid labeling of P-selectin in transfected COS-7 cells. We conclude that the cytoplasmic domain of P-selectin is acylated at Cys766 through a thioester bond. Fatty acid acylation may regulate intracellular trafficking or other functions of P-selectin.
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