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J. Biol. Chem., Vol. 266, Issue 17, 10851-10858, 06, 1991
MA Chernousov, FJ Fogerty, VE Koteliansky and DF Mosher
Cultured fibroblasts bind soluble protomeric fibronectin and mediate its
conversion to insoluble disulfide-bonded multimers. The disulfide- bonded
multimers are deposited in fibrillar pericellular matrix. Antifibronectin
monoclonal antibodies were analyzed to identify domains of fibronectin
required for assembly into matrix. Two antibodies, L8 and 9D2, inhibited
binding and insolubilization of 125I-labeled plasma fibronectin by
fibroblasts but did not inhibit binding of labeled amino- terminal 70-kDa
fragment of fibronectin to matrix assembly sites. Immunoblotting of
fibronectin fragments showed that the epitope for 9D2 is in the first type
III homology sequence (III-1) whereas the epitope for L8 requires that the
last type I sequence of the gelatin binding region (I-9) be contiguous to
III-1 and is sensitive to reduction of disulfides in I-9. A 56-kDa
gelatin-binding thermolysin fragment of fibronectin that contains III-1 and
the L8 and 9D2 epitopes inhibited binding of fibronectin to cell layers
10-fold better than a 40-kDa gelatin-binding fragment that lacks III-1 and
the antigenic sites. This 56-kDa fragment, however, did not bind
specifically to cell layers. These results indicate that the I-9 and III-1
modules of fibronectin form a functional unit that mediates an interaction,
perhaps between protomers, important in the assembly of fibronectin.
Role of the I-9 and III-1 modules of fibronectin in formation of an extracellular fibronectin matrix
Institute of Experimental Cardiology, USSR Cardiology Research Center, Academy of Medical Sciences, Moscow.
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