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Tenascin‐C induced stimulation of chondrogenesis is dependent on the presence of the C‐terminal fibrinogen‐like globular domain
Author(s) -
Murphy Lyn I.,
Fischer Doris,
Chiquet-Ehrismann Ruth,
Mackie Eleanor J.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01936-0
Subject(s) - chondrogenesis , extracellular matrix , tenascin c , stimulation , tenascin , gene isoform , microbiology and biotechnology , chemistry , fibrinogen , mesenchymal stem cell , fibronectin , biology , biochemistry , endocrinology , gene
The relationship between structure of tenascin‐C (Tn‐C), a multi‐domain extracellular matrix protein, and its stimulation of chondrogenesis was examined using recombinant Tn‐C isoforms (full length or with specific domains deleted) as substrata for undifferentiated chicken mesenchymal cells. Of the Tn‐C variants tested, only Tn‐C lacking the fibrinogen‐like domain or Tn‐C comprised solely of fibrinogen‐like domains failed to stimulate chondrogenesis. The ability of variants to stimulate chondrogenesis was not dependent on their ability to support adhesion or stimulate proliferation. These results demonstrate that the fibrinogen‐like domain of Tn‐C is necessary but not sufficient for induction of chondrogenesis.