Absence of the I-10 protein segment mediates restricted dimerization of the cartilage-specific fibronectin isoform.

The Journal of Biological Chemistry
H ChenJ N MacLeod

Abstract

The cartilage-specific (V + C)(-) fibronectin isoform does not efficiently heterodimerize with other V-region splice variants of fibronectin. To understand better the structural elements that determine this restricted dimerization profile, a series of truncated fibronectin expression constructs with various internal deletions in the V, III-15, or I-10 segments were constructed and co-transfected into COS-7 cells with either the V(+)C(+) or the (V + C)(-) isoform. SDS-PAGE and immunoblot analyses of the resulting conditioned media suggest that the I-10 segment must either be present in both monomeric subunits of fibronectin or absent from both subunits for efficient dimerization to occur. Further studies suggest that the I-10 segment specifically, not simply a balanced number of type I repeats at the carboxyl terminus of each monomeric subunit, plays an important role in determining different fibronectin dimerization patterns. Neither I-11 nor I-12 could be substituted for segment I-10 without significantly reducing the formation of heterodimers. Therefore, absence of segment I-10 explains why (V + C)(-) fibronectin is not found in heterodimeric configurations with other native V-region splice variants in cartilage. The unique d...Continue Reading

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Citations

Sep 13, 2002·Matrix Biology : Journal of the International Society for Matrix Biology·Nancy Burton-WursterJames N MacLeod
Aug 3, 2005·Matrix Biology : Journal of the International Society for Matrix Biology·Yong Mao, Jean E Schwarzbauer
Dec 17, 2002·The Journal of Biological Chemistry·Rina GendelmanGeorge Lust
Oct 4, 2003·The Journal of Biological Chemistry·Tomohiro KozakiKiyotoshi Sekiguchi

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