Inhibition of blood coagulation factor XIIIa-mediated cross-linking between fibronectin and collagen by polyamines
✍ Scribed by Mosher, Deane F. ;Schad, Peter E. ;Kleinman, Hynda K.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1979
- Tongue
- English
- Weight
- 608 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0091-7419
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✦ Synopsis
Soluble fibronectin is found in body fluids and media of cultured adherent cells. Insoluble fibronectin is found in tissue stroma and in extracellular niatrices of cultured cells. Fibronectin is a substrate for factor XIII, (plasma transglutaminase) and can be cross-linked t o collagen and t o the 0: chain of fibrin.
We have used sodium dodecyl sulfate-polyacrylaniide gel electrophoresis t o investigate the possibility that factor XIII, -mediated cross-linking is influenced by polyamines. Sperinidine inhibited cross-linking between fibronectin and type I collagen, isolated a1 (I) collagen chains. o r iodinated cyanogen bromide fragment 7 of a1 (1) chains ('251-al (I)-CB7). Half-maximal inhibition of crosslinking between '251iyl (I)-CB7 and fibronectin was observed when 0.1 mM spermine o r spermidine was present. Spermidine, 0.7 niM, partially inhibited cross-linking between fibronectin and the a chain of fibrin but failed t o inhibit cross-linking between the fibrin monomers of a fibrin clot. Spermidine also failed t o inhibit cross-linking between fibronectin molecules when aggregation of fibronectin was induced with dithiothreitol. In contrast, 0.7 mM nionodansplcadaverine inhibited fibronectin-Lollagen, fibronectin-fibrin, fibronectinfibronectin, and fibrin-fibrin cross-linking. Spermidine o r spermine, 0.7 m M , enhanced the cross-linking between molecules of partially amidinated fibronectin, suggesting that N ' . -(di-y-glutamy1)-polyamine cross-linkages were formed. Spermidme and spermine failed t o enhance cross-linking between monomers of aniidinated fibrin. These results indicate that physiologic concentrations of polyamines specifically disturb transglutaminase-catalyzed cross-linking between fibronectin and collagen.