Title
Characterization of a rat <tex>$C_{6}$</tex> glioma-secreted follistatin-related protein (FRP) : cloning and sequence of the human homolog Characterization of a rat <tex>$C_{6}$</tex> glioma-secreted follistatin-related protein (FRP) : cloning and sequence of the human homolog
Author
Faculty/Department
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences . Biomedical Sciences
Publication type
article
Publication
Berlin ,
Subject
Chemistry
Biology
Source (journal)
European journal of biochemistry. - Berlin
Volume/pages
225(1994) :3 , p. 937-946
ISSN
0014-2956
ISI
A1994PP67900018
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
A protein was isolated from rat C-6 glioma-conditioned medium and was biochemically characterized. The heparin-binding protein has a native molecular mass of 55-75000 Da, a molecular mass of 40-48000 Da under denaturing conditions, and a pI of 5.0-6.0. Based on the determined partial amino acid sequences, the full length cDNA encoding the rat and human proteins were cloned. The cDNA sequences identified the isolated rat and human protein as the homologue of a recently reported mouse osteoblast-transforming-growth-factor-beta(1)-inducible protein, encoded by the TSC-36 gene [Shibanuma, M., Mashimo, J., Mita, A., Kuroki, T. and Nose, K. (1993) Eur. J. Biochem. 217, 13-19]. Analysis of the human, rat and mouse amino acid sequences indicates that these proteins are highly conserved (>92% sequence identity). Sequence similarities with follistatin and the follistatin-like domain of agrin are revealed. The relationship with follistatin and agrin points to possible common functions for the cloned follistatin-related proteins (FRP). The protein has no effect on the inhibitory action of transforming growth factor-beta(1), on CCl-64 cell growth.
E-info
https://repository.uantwerpen.be/docman/iruaauth/819169/6b74344.pdf
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