An active site of growth hormone for eliciting the differentiation of preadipose 3T3-F442A cells to adipose cells
| Autor: | Morio Ikehara, Takao Hayakawa, Seiichi Uesugi, Satoshi Nishikawa, Minoru Morikawa, Akira Tanaka, Eriko Uchida, Yoshitaka Nishida, Ken-ichi Tomita, Seitaro Shimokawa, Hisashi Takasu |
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| Rok vydání: | 1990 |
| Předmět: |
Models
Molecular Protein Conformation Swine Cellular differentiation Mutant Molecular Sequence Data Biophysics Mutagenesis (molecular biology technique) Adipose tissue Biochemistry Cell Line chemistry.chemical_compound Mice Adipocyte Animals Humans Site-directed mutagenesis Receptor Molecular Biology Binding Sites biology Base Sequence Active site Cell Differentiation Cell Biology Recombinant Proteins chemistry Adipose Tissue Growth Hormone biology.protein Mutagenesis Site-Directed Oligonucleotide Probes hormones hormone substitutes and hormone antagonists |
| Zdroj: | Biochemical and biophysical research communications. 172(1) |
| ISSN: | 0006-291X |
| Popis: | Summary In order to elucidate the active sites of growth hormone for eliciting the differentiation of preadipose 3T3-F442A cells to adipocytes, four artificial mutant variants of human growth hormone(hGH) modified in the loop region of amino acid residues 54–74 were prepared in Escherichia coli by site-directed mutagenesis. Although the P59A (replacement of Pro59 with Ala) variant retained almost the same biological- and receptor binding-activity as hGH, the P61A (replacement of Pro61 with Ala) and the P59A–P61A (replacement of both Pro59 and Pro6l with Ala) both exhibited about half the activity, and the Δ (62–67) variant (deletion of the residues 62–67) exhibited only about 0.1% the activity of those of intact hGH. The results suggest that Pro61 may be involved in formation of the active conformation of hGH, but Pro59 may not, and that the amino acid residues around 62–67 may be critical for the specific biological features of hGH. |
| Databáze: | OpenAIRE |
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