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

Authors
ASAKURA A KIKUCHI M UCHIDA E HAYAKAWA T OTA Y
Citation
A. Asakura et al., THE ENHANCEMENT OF THE EXTRACELLULAR CARBOXYL-TERMINAL DOMAIN OF HUMAN GROWTH-HORMONE RECEPTOR ON GROWTH-HORMONE DEPENDENT RESPONSES OF 3T3-F442A CELLS, Biomedicine & pharmacotherapy, 48(1), 1994, pp. 35-39
Citations number
12
Categorie Soggetti
Pharmacology & Pharmacy","Medicine, Research & Experimental
Journal title
Biomedicine & pharmacotherapy → ACNP
ISSN journal
07533322
Volume
48
Issue
1
Year of publication
1994
Pages
35 - 39
Database
ISI
SICI code
0753-3322(1994)48:1<35:TEOTEC>2.0.ZU;2-V
Abstract
We have expressed the carboxyl-terminal domain (C domain) of the cytok ine 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, th e C domain was purified to homogeneity as a monomeric form. The purifi ed C domain appears to be folded properly judged by NMR spectrum and t he far-UV circular dichroism (CD) spectrum. The C domain did not exhib it ligand binding activity. However, the C domain enhanced the human g rowth hormone (hGH) dependent differentiation of preadipose 3T3-F442A cells into adipose cells and the phosphorylation of a 34 kDa membrane protein.