Fatty acylation of human platelet proteins: evidence for myristoylation of a 50 kDa peptide.
Fatty acid acylation of platelet proteins was studied by measuring incorporation of [3H]palmitate and [3H]myristate after incubation at 37 degrees C for 4 h. About ten major radiolabeled proteins were detected after SDS-polyacrylamide gel electrophoresis and fluorography, for both fatty acids. Cleavage by hydroxylamine treatment indicated an ester bond of either palmitate or myristate to these proteins. Nevertheless, a single 50 kDa peptide was specifically modified by an amide-linked myristate. The functions of acylated proteins in platelets are still unknown, but their relation with DLPC-induced shape changes and vesicle shedding is excluded.
Vidal
M
M
URA 530 CNRS, USTL, Montpellier, France.
Murgue
B
B
Bassé
F
F
Bienvenüe
A
A
D000215:Acylation; D001792:Blood Platelets / Q000378:metabolism* / Q000648:ultrastructure; D001798:Blood Proteins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005227:Fatty Acids / Q000378:metabolism*; D006801:Humans; D008855:Microscopy, Electron, Scanning; D019814:Myristic Acid; D009227:Myristic Acids / Q000378:metabolism; D010713:Phosphatidylcholines / Q000378:metabolism
D001798:Blood Proteins; D005227:Fatty Acids; D009227:Myristic Acids; D010713:Phosphatidylcholines; D019814:Myristic Acid; C015153:1,2-dilauroylphosphatidylcholine