Activity of growth hormone peptides bGH 96-133 and hGH 95-133 in 3T3-F442A cells Journal Article

  


Authors: Sonenberg, M.; Guller, S.; Wu, K. Y.; Corin, R. E.; Allen, D. L.
Article Title: Activity of growth hormone peptides bGH 96-133 and hGH 95-133 in 3T3-F442A cells
Abstract: Chemically synthesized bovine growth hormone (bGH) bGH 96-133 and its human homologue, hGH 95-133, have similar in vitro biological activities. Unlike native GH, bGH 96-133 and hGH 95-133 were completely without adipogenic or anti-insulin activity at doses up to 10 μM. bGH 96-133 had insulin-like activity, with a 100% increase in glucose uptake at 10 μM. bGH was anti-mitogenic and bGH 96-133 and hGH 95-133 were mitogenic (EC50 ~ 180 nM and maximal response at 1-2 μM). Only bGH 96-133 and hGH 95-133 displaced [125I]hGH 95-133 binding from 3T3-F442A fibroblasts with a Kd between 60-120 nM. bGH, hGH, insulin and IGF-I were without effect on [125I]hGH 95-133 binding. bGH 96-133 and hGH 95-133 did not significantly inhibit [125I]hGH or [125I]IGF-I binding. These experiments indicate that GH containing peptides bGH 96-133 and hGH 95-133 have mitogenic and insulin-like activity without the adipogenic, anti-insulin or anti-mitogenic activity of bGH. These peptides have a specific binding site which appears to be distinct from the GH, insulin and IGF-I receptors. © 1994.
Keywords: nonhuman; comparative study; animal cell; mouse; animal; mice; cell division; mitogenesis; protein binding; dose-response relationship, drug; growth hormone; kinetics; iodine 125; peptide fragments; human growth hormone; fibroblast; insulin; binding site; glucose; binding sites; cattle; insulin-like growth factor i; glucose transport; cell strain 3t3; 3t3 cells; hormone synthesis; binding; binding, competitive; adipocytes; hormone action; peptide hormone; human; priority journal; article; support, u.s. gov't, p.h.s.; growth hormone peptide; insulin like; insulin like activity
Journal Title: Molecular and Cellular Endocrinology
Volume: 99
Issue: 2
ISSN: 0303-7207
Publisher: Elsevier Ireland Ltd.  
Date Published: 1994-03-01
Start Page: 193
End Page: 199
Language: English
DOI: 10.1016/0303-7207(94)90008-6
PROVIDER: scopus
PUBMED: 8206327
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028278531&doi=10.1016%2f0303-7207%2894%2990008-6&partnerID=40&md5=9fd843e927cc81bdfe4266043880527f
Notes: Export Date: 14 January 2019 -- Article -- CODEN: MCEND C2 -- Source: Scopus
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  1. Martin Sonenberg
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