Tsuji T, Okada F, Yamaguchi K, Nakamura T
Department of Biology, Faculty of Science, Kyushu University, Fukuoka, Japan.
Proc Natl Acad Sci U S A. 1990 Nov;87(22):8835-9. doi: 10.1073/pnas.87.22.8835.
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.
掩盖蛋白(MP)可中和转化生长因子β1(TGF-β1)的活性,它由一个分子量为39,000的TGF-β1前体的二聚体N端部分和一个分子量为105,000 - 120,000的未知大亚基组成。通过确定其cDNA的核苷酸序列,阐明了MP大亚基推导的一级结构。该cDNA编码一个由1712个氨基酸残基组成的前原前体,计算分子量为186,596。成熟的大亚基似乎是通过蛋白水解从前原前体衍生而来,计算分子量为91,606。该前体有七个N-糖基化位点,以及一个包含18个表皮生长因子样结构域和四个富含半胱氨酸的内部重复序列的异常结构。大亚基mRNA在大鼠各种组织中的合成与TGF-β1 mRNA的表达平行。