THE ENHANCEMENT OF THE EXTRACELLULAR CARBOXYL-TERMINAL DOMAIN OF HUMAN GROWTH-HORMONE RECEPTOR ON GROWTH-HORMONE DEPENDENT RESPONSES OF 3T3-F442A CELLS

被引：1
作者：
ASAKURA, A
KIKUCHI, M
UCHIDA, E
HAYAKAWA, T
OTA, Y
机构：
[1] PROT ENGN RES INST,SUITA,OSAKA 565,JAPAN
[2] NATL INST HYG SCI,SETAGAYA KU,TOKYO 158,JAPAN
来源：
BIOMEDICINE & PHARMACOTHERAPY | 1994年 / 48卷 / 01期
关键词：
HUMAN GROWTH HORMONE RECEPTOR; EXTRACELLULAR DOMAIN; ADIPOSE CONVERSION ASSAY;
D O I：
10.1016/0753-3322(94)90188-0
中图分类号：
R-3 [医学研究方法]; R3 [基础医学];
学科分类号：
1001 ;
摘要：
We have expressed the carboxyl-terminal domain (C domain) of the cytokine receptor homologous (CRH) region of human growth hormone receptor (hGHR) as a protein fused with maltose binding protein (MBP) in E coli. Following proteolytic cleavage by restriction protease factor Xa, the C domain was purified to homogeneity as a monomeric form. The purified C domain appears to be folded properly judged by NMR spectrum and the far-UV circular dichroism (CD) spectrum. The C domain did not exhibit ligand binding activity. However, the C domain enhanced the human growth hormone (hGH) dependent differentiation of preadipose 3T3-F442A cells into adipose cells and the phosphorylation of a 34 kDa membrane protein.
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页码：35 / 39
页数：5
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