MOLECULAR-CLONING OF THE LARGE SUBUNIT OF TRANSFORMING GROWTH-FACTOR TYPE-BETA MASKING PROTEIN AND EXPRESSION OF THE MESSENGER-RNA IN VARIOUS RAT-TISSUES

被引:145
作者
TSUJI, T
OKADA, F
YAMAGUCHI, K
NAKAMURA, T
机构
[1] KYUSHU UNIV,FAC SCI,DEPT BIOL,FUKUOKA 812,JAPAN
[2] KYOWA HAKKO KOGYO CO LTD,TOKYO RES LABS,MACHIDA,TOKYO 194,JAPAN
关键词
binding protein; cysteine-rich internal repeat; epidermal growth factor-like domain; primary structure;
D O I
10.1073/pnas.87.22.8835
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Masking protein (MP), which neutralizes the activity of transforming growth factor type β1 (TGF-β1), is composed of a dimeric N-terminal part of a TGF-β1 precursor of M(r) 39,000 and an unknown large subunit of M(r) 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 M(r) of 186,596. The mature large subunit seems to be derived proteolytically from a prepro-precursor and the calculated M(r) 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-β1 mRNA in various rat tissues.
引用
收藏
页码:8835 / 8839
页数:5
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