The enhancement of the extracellular carboxyl-terminal domain of human growth hormone receptor on growth hormone dependent responses of 3T3-F442A cells.
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.
Asakura
A
A
Protein Engineering Research Institute, Osaka, Japan.
Kikuchi
M
M
Uchida
E
E
Hayakawa
T
T
Ota
Y
Y
D017667:Adipocytes / Q000378:metabolism; D000818:Animals; D005110:Extracellular Space / Q000737:chemistry*; D005347:Fibroblasts / Q000378:metabolism; D013006:Growth Hormone / Q000378:metabolism*; D006801:Humans; D051379:Mice; D010443:Peptide Chain Termination, Translational; D011986:Receptors, Somatotropin / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
D011986:Receptors, Somatotropin; D013006:Growth Hormone