Abstract
Fibronectin binds specifically to fibrin and is covalently cross-linked to the fibrin α chain by activated factor XIII (XIIIa). This reaction is important for wound healing. Here we investigate XIIIa-catalyzed cross-linking of fibronectin and some of its fragments to a recombinant fragment representing the COOH-terminal 30kDa of the fibrin α chain (αC30K:His 368–Val 610). Only fibronectin and those fragments containing an intact NH2-terminus were able to form cross-linked complexes. As many as 10 of the 17 lysines in αC30K can serve as amine donors in this reaction. Analysis of the rate of XIIIa-catalyzed cross-linking of fibronectin NH2-terminal peptides and fragments with αC30K revealed that the presence of the first type I “finger” module accelerates the cross-linking reaction; addition of fingers 2–5 had no further effect.
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Matsuka, Y.V., Migliorini, M.M. & Ingham, K.C. Cross-Linking of Fibronectin to C-Terminal Fragments of the Fibrinogen α-Chain by Factor XIIIa. J Protein Chem 16, 739–745 (1997). https://doi.org/10.1023/A:1026307731751
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DOI: https://doi.org/10.1023/A:1026307731751