Inhibition of heparin-catalyzed human antithrombin III activity by nonenzymatic glycosylation. Possible role in fibrin deposition in diabetes

M. Brownlee, H. Vlassara, A. Cerami

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69 Citations (Scopus)

Abstract

The effect of nonenzymatic glycosylation on the biologic function of human antithrombin III was evaluated using a chromogenic thrombin substrate assay in the presence of catalytic amounts of heparin. Experimental conditions that increased the rate of nonenzymatic protein glycosylation were associated with decreases in the thrombin-inhibiting activity of antithrombin III. This glycosylation-induced inhibition of heparin-catalyzed antithrombin III activity was completely reversible by preassay incubation with excess sodium heparin. These observations provide a biochemical explanation for the heparin-reversible, accelerated fibrinogen disappearance rate induced by hyperglycemia in diabetic patients. Defective inhibition of the coagulation cascade induced by excessive nonenzymatic glycosylation of antithrombin III in vivo could contribute to accumulation of fibrin in various diabetic tissues.

Original languageEnglish (US)
Pages (from-to)532-535
Number of pages4
JournalDiabetes
Volume33
Issue number6
StatePublished - 1984
Externally publishedYes

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Antithrombin III
Fibrin
Glycosylation
Heparin
Thrombin
Chromogenic Compounds
Hyperglycemia
Fibrinogen

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Internal Medicine

Cite this

Inhibition of heparin-catalyzed human antithrombin III activity by nonenzymatic glycosylation. Possible role in fibrin deposition in diabetes. / Brownlee, M.; Vlassara, H.; Cerami, A.

In: Diabetes, Vol. 33, No. 6, 1984, p. 532-535.

Research output: Contribution to journalArticle

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