
pmid: 2350783
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.
Blood Platelets, Base Sequence, Molecular Sequence Data, Intracellular Signaling Peptides and Proteins, Gene Expression, Nucleic Acid Hybridization, DNA, Blotting, Northern, Peptide Fragments, Cell Line, Latent TGF-beta Binding Proteins, Transforming Growth Factors, Animals, Humans, Amino Acid Sequence, RNA, Messenger, Asparagine, Cloning, Molecular, Carrier Proteins, Repetitive Sequences, Nucleic Acid
Blood Platelets, Base Sequence, Molecular Sequence Data, Intracellular Signaling Peptides and Proteins, Gene Expression, Nucleic Acid Hybridization, DNA, Blotting, Northern, Peptide Fragments, Cell Line, Latent TGF-beta Binding Proteins, Transforming Growth Factors, Animals, Humans, Amino Acid Sequence, RNA, Messenger, Asparagine, Cloning, Molecular, Carrier Proteins, Repetitive Sequences, Nucleic Acid
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