Open AccessMolecular cloning of the large subunit of transforming growth factor type beta masking protein and expression of the mRNA in various rat tissues.
Author(s) -
Takashi Tsuji,
Fumio Okada,
Kazuo Yamaguchi,
Toshikazu Nakamura
Publication year - 1990
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.87.22.8835
Subject(s) - complementary dna , protein subunit , messenger rna , microbiology and biotechnology , biology , peptide sequence , beta (programming language) , protein primary structure , amino acid , cloning (programming) , glycosylation , transforming growth factor beta , tgf beta receptor 2 , transforming growth factor , growth factor , biochemistry , tgf alpha , gene , computer science , programming language , receptor
Masking protein (MP), which neutralizes the activity of transforming growth factor type beta 1 (TGF-beta 1), is composed of a dimeric N-terminal part of a TGF-beta 1 precursor of Mr 39,000 and an unknown large subunit of Mr 105,000-120,000. The deduced primary structure of the MP large subunit was elucidated by determining the nucleotide sequence of its cDNA. The cDNA encodes a prepro-precursor of 1712 amino acid residues with a calculated Mr of 186,596. The mature large subunit seems to be derived proteolytically from a prepro-precursor and the calculated Mr is 91,606. The precursor has seven N-linked glycosylation sites and an unusual structure containing 18 epidermal growth factor-like domains and four cysteine-rich internal repeats. The large subunit mRNA is synthesized in parallel with the expression of TGF-beta 1 mRNA in various rat tissues.