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Matrix assembly of recombinant fibronectin polypeptide consisting of amino‐terminal 70 kDa and carboxyl‐terminal 37 kDa regions
Author(s) -
Ichihara-Tanaka Keiko,
Maeda Toshinaga,
Titani Koiti,
Sekiguchi Kiyotoshi
Publication year - 1992
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 - 10.1016/0014-5793(92)80236-a
Subject(s) - fibronectin , recombinant dna , terminal (telecommunication) , amino terminal , extracellular matrix , matrix (chemical analysis) , biochemistry , peptide sequence , chemistry , amino acid , microbiology and biotechnology , biology , gene , telecommunications , chromatography , computer science
Three different forms of recombinant human fibronectin polypeptides consisting of the amino‐terminal 70 kDa region, the carboxyl‐terminal 37 kDa region, or both, were expressed in mouse L cells. Although either the amino‐terminal or the carboxyl‐terminal region alone was only poorly incorporated into the extracellular matrix, the fused form of the polypeptide was highly capable of assembling into the matrix. These results indicate that matrix assembly of fibronectin requires both regions and can proceed in the absence of most of the type III repeats including the one containing the cell adhesive Arg‐Gly‐Asp sequence.