Functional activities and nonenzymatic glycosylation of plasma proteinase inhibitors in diabetes.

Autor: Hall P, Tryon E, Nikolai TF, Roberts RC
Jazyk: angličtina
Zdroj: Clinica chimica acta; international journal of clinical chemistry [Clin Chim Acta] 1986 Oct 15; Vol. 160 (1), pp. 55-62.
DOI: 10.1016/0009-8981(86)90335-9
Abstrakt: The functional activity of three of the major plasma protease inhibitors, alpha 1-proteinase inhibitor, antithrombin III and alpha 2-antiplasmin, has been measured in a series of persons with diabetes mellitus and compared with healthy controls. The mean specific functional activity of both diabetic plasma antithrombin III (50.8 +/- 7.0 U/mg) and alpha 1-proteinase inhibitor (35.3 +/- 5.6 mU/mg) was found to be significantly lower than in healthy controls (57.9 +/- 6.0 U/mg) and (42.2 +/- 10.7 mU/mg). No difference was detected in alpha 2-antiplasmin activity or levels. The glycosylated protein fraction of 83% of diabetic plasmas showed the presence of less than 1% of the total alpha 1-proteinase inhibitor when isolated by phenylboronate affinity chromatography. Incubation of normal plasma with 250 nmol/l glucose (a level approximately 6 X higher than encountered in uncontrolled diabetes) resulted in a 17% and 6% decrease in antithrombin III and alpha 1-proteinase inhibitor activities. We conclude that the decrease in specific activity of alpha 1-proteinase inhibitor is not related to nonenzymatic glycosylation, but the decrease in antithrombin III specific activity may be related.
Databáze: MEDLINE