Nonenzymatic glycation of human blood platelet proteins

I. Cohen*, D. Burk, R. J. Fullerton, A. Veis, D. Green

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

We studied 11 diabetic patients, all of whom had severe atherothrombotic disease, and 11 normal controls. Overall glycation was assessed by the extent of incorporation of [3H]-NaBH4 into fructosyl lysine separated from whole platelet proteins following aminoacid analysis. Fructosyl lysine represented 5.7% ± 1.0 S.D. of the total radioactivity in the normal whole platelet samples. Increased glycation was observed in platelets from 5 of the 11 diabetics. Platelet glycation did not correlate with glycation of hemoglobin or albumin. The pattern of glycation of various platelet proteins in whole platelets, as determined by the incorporation of [3H]-NaBH4 into electrophoretically separated proteins did not display selectivity, although myosin and glycoproteins IIb and IIIa showed relatively increased levels of [3H]-NaBH4 incorporation. Artificially glycated platelet membranes exhibited glycation mainly in proteins corresponding to the electrophoretic mobility of myosin, glycoproteins IIb and IIIa.

Original languageEnglish (US)
Pages (from-to)341-349
Number of pages9
JournalThrombosis research
Volume55
Issue number3
DOIs
StatePublished - Aug 1 1989

Keywords

  • Diabetes
  • Nonenzymatic Glycation
  • Platelets

ASJC Scopus subject areas

  • Hematology

Fingerprint Dive into the research topics of 'Nonenzymatic glycation of human blood platelet proteins'. Together they form a unique fingerprint.

Cite this