Glycosylation of human fibrinogen in vivo |
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Authors: | A. Lütjens A. A. te Velde E. A. v. d. Veen J. v. d. Meer |
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Affiliation: | (1) Department of Clinical Chemistry, Andreas Hospital, The Netherlands;(2) Department of Internal Medicine, Free University Hospital, Amsterdam, The Netherlands |
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Abstract: | Summary Fibrinogen was purified from plasma from 22 nondiabetic and 26 poorly controlled Type 1 (insulin-dependent) diabetic subjects. In non-diabetic subjects, 0.95±0.17 mol glucose was bound per mol fibrinogen, whereas in the diabetic subjects 1.33±0.21 mol glucose was bound per mol fibrinogen (mean ± SD, p<0.001). Comparison of the amount of bound glucose, when estimated by two different methods, suggested that lysine is the site of glycosylation. It is currently unknown whether this increased glycosylation of fibrinogen alters its function. |
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Keywords: | Fibrinogen glycosylation Type 1 diabetes |
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