Abstract
Previous electron microscopy (EM) studies revealed that the proteolytically prepared, truncated, bovine fibrinogen αC-domain (Aα223-539 fragment) upon transfer from acidic to neutral pH formed ordered oligomers which could mimic α polymers of cross-linked fibrin. In this study, we demonstrated that although its recombinant analog, bAα224-538, as well as the full-length version of the αC-domain (bAα224-568), upon similar treatment also formed oligomers with ordered structure, both were monomeric when kept in neutral pH buffer. To search further for conditions for their oligomerization, we treated bAα224-568 with factor XIIIa, purified the cross-linked soluble fraction, and confirmed that it consisted of oligomers. Similar cross-linked oligomers were obtained with the recombinant human αC-domain (residues Aα221-610). In a cell adhesion assay, the adhesion of human umbilical vein endothelial cells (HUVEC) to the αC-domains substantially increased upon oligomerization. These results demonstrate that the recombinant αC-domains can form stable oligomers which may mimic properties of the αC-domains in cross-linked fibrin.
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