| Literature DB >> 2350783 |
T Kanzaki1, A Olofsson, A Morén, C Wernstedt, U Hellman, K Miyazono, L Claesson-Welsh, C H Heldin.
Abstract
TGF-beta occurs in a latent complex of high Mr. We report the cDNA cloning and an initial structural and functional characterization of a component of the large latent TGF-beta 1 complex, denoted TGF-beta 1 binding protein (TGF-beta 1-BP). Most of the sequence of fibroblast TGF-beta 1-BP is made up of cysteine-rich repeats of two different kinds; there are 16 EGF-like repeats and three repeats with a distant resemblance to EGF, but of a distinct type hitherto not found in any other protein. beta-hydroxylated asparagine residues were identified in two of the EGF-like repeats. TGF-beta 1-BP purified from human platelets is considerably smaller than the fibroblast form (125-160 kd vs. 170-190 kd), suggesting that there is alternative splicing of the TGF-beta 1-BP gene or that TGF-beta 1-BP undergoes cell-specific proteolysis. TGF-beta 1-BP was found not to bind and inactive TGF-beta 1; its role in the latent complex is discussed.Entities:
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Year: 1990 PMID： 2350783 DOI： 10.1016/0092-8674(90)90069-q
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582