Elsevier

Clinica Chimica Acta

Volume 160, Issue 1, 15 October 1986, Pages 55-62
Clinica Chimica Acta

Short communication
Functional activities and nonenzymatic glycosylation of plasma proteinase inhibitors in diabetes

https://doi.org/10.1016/0009-8981(86)90335-9Get rights and content

Abstract

The functional activity of three of the major plasma protease inhibitors, α1-proteinase inhibitor, antithrombin III and α2-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 α1-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 α2-antiplasmin activity or levels. The glycosylated protein fraction of 83% of diabetic plasmas showed the presence of less than 1% of the total α1-proteinase inhibitor when isolated by phenylboronate affinity chromatography. Incubation of normal plasma with 250 mmol/l glucose (a level approximately 6 × higher than encountered in uncontrolled diabetes) resulted in a 17% and 6% decrease in antithrombin III and α1-proteinase inhibitor activities. We conclude that the decrease in specific activity of α1-proteinase inhibitor is not related to nonenzymatic glycosylation, but the decrease in antithrombin III specific activity may be related.

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