Nonenzymatic glycation of human blood platelet proteins

I. Cohen; D. Burk; R. J. Fullerton; A. Veis; D. Green

doi:10.1016/0049-3848(89)90066-2

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 journal › Article › peer-review

25 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 language	English (US)
Pages (from-to)	341-349
Number of pages	9
Journal	Thrombosis research
Volume	55
Issue number	3
DOIs	https://doi.org/10.1016/0049-3848(89)90066-2
State	Published - Aug 1 1989

Keywords

Diabetes
Nonenzymatic Glycation
Platelets

ASJC Scopus subject areas

Hematology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/0049-3848(89)90066-2

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title = "Nonenzymatic glycation of human blood platelet proteins",

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.",

keywords = "Diabetes, Nonenzymatic Glycation, Platelets",

author = "I. Cohen and D. Burk and Fullerton, {R. J.} and A. Veis and D. Green",

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T1 - Nonenzymatic glycation of human blood platelet proteins

AU - Cohen, I.

AU - Burk, D.

AU - Fullerton, R. J.

AU - Veis, A.

AU - Green, D.

PY - 1989/8/1

Y1 - 1989/8/1

N2 - 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.

AB - 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.

KW - Diabetes

KW - Nonenzymatic Glycation

KW - Platelets

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ER -

Nonenzymatic glycation of human blood platelet proteins

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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