Cross-linking of fibronectin to C-terminal fragments of the fibrinogen alpha-chain by factor XIIIa.
Fibronectin binds specifically to fibrin and is covalently cross-linked to the fibrin alpha 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 30 kDa of the fibrin alpha chain (alpha C30K: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 alpha C30K 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 alpha C30K 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.
Matsuka
Y V
YV
Holland Laboratory, American Red Cross, Rockville, Maryland 20855, USA.
Migliorini
M M
MM
Ingham
K C
KC
D000595:Amino Acid Sequence; D002384:Catalysis; D003432:Cross-Linking Reagents / Q000494:pharmacology*; D005340:Fibrinogen / Q000378:metabolism*; D005353:Fibronectins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D011503:Transglutaminases / Q000494:pharmacology*
D003432:Cross-Linking Reagents; D005353:Fibronectins; D010446:Peptide Fragments; D011994:Recombinant Proteins; D005340:Fibrinogen; D011503:Transglutaminases