Deglycosylation of fibrinogen accelerates polymerization and increases lateral aggregation of fibrin fibers

Fibrinogen, the major structural precursor of blood clots, was deglycosylated by peptide-N-(N-acetyl-beta-glucosaminyl)asparagine amidase without denaturation of the polypeptide chains. Deglycosylated fibrinogen behaved normally in clinical coagulation assays, although it is less soluble than normal...

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Bibliographic Details
Published in:The Journal of biological chemistry 1988-10, Vol.263 (29), p.15056-15063
Main Authors: Langer, B G, Weisel, J W, Dinauer, P A, Nagaswami, C, Bell, W R
Format: Article
Language:English
Subjects:
Biological and medical sciences
Blood coagulation. Blood cells
Factor XII - metabolism
Factor XIII Deficiency - blood
Fibrin - metabolism
Fibrin - ultrastructure
Fibrinogen - isolation & purification
Fibrinogen - metabolism
Fibrinogen - ultrastructure
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods, hemostasis, fibrinolysis
Glycosylation
Humans
Kinetics
Macromolecular Substances
Microscopy, Electron
Microscopy, Electron, Scanning
Models, Molecular
Molecular and cellular biology
Thrombin - metabolism
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Summary:Fibrinogen, the major structural precursor of blood clots, was deglycosylated by peptide-N-(N-acetyl-beta-glucosaminyl)asparagine amidase without denaturation of the polypeptide chains. Deglycosylated fibrinogen behaved normally in clinical coagulation assays, although it is less soluble than normal fibrinogen. However, the turbidity of clots formed from deglycosylated fibrinogen always rose faster and higher than that of clots from normal fibrinogen. Scanning and transmission electron microscopy demonstrated that fibrin made from clots of deglycosylated fibrinogen consisted of thicker, less-branched fiber bundles in a more porous network. Moreover, the degree of lateral aggregation was directly related to clot turbidity and inversely related to branching. Deglycosylation promoted turbidity development, lateral aggregation, and porosity of clots under all conditions tested. All other steps in the coagulation pathways appeared to be unaffected by the absence of carbohydrate. These results suggest that carbohydrate constitutively affects the behavior of deglycosylated fibrinogens by 1) contributing a repulsive force that promotes fibrinogen solubility and limits fibrin assembly and 2) sensitizing fibrin to conditions that influence assembly and clot structure.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)68145-1