Signal transduction by the growth hormone receptor

Journal Article · Sat Dec 31 04:00:00 EST 1994 · Proceedings of the Society for Experimental Biology and Medicine

DOI:https://doi.org/10.3181/00379727-206-43745· OSTI ID:466618

Waters, M J; Rowlinson, S W; Clarkson, R W ^[1]

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1. Univ. of Queensland (Australia); and others

It has been proposed that dimerization of identical receptor subunits by growth hormone (GH) is the mechanism of signal transduction across the cell membrane. We present here data with analogs of porcine GH (pGH), with GH receptors (GHR) mutated in the dimerization domain and with monoclonal antibodies to the GHR which indicate that dimerization is necessary but not sufficient for transduction. We also report nuclear uptake of GH both in vivo and in vitro, along with nuclear localization of the receptor and GH-binding protein (GHBP). This suggests that GH acts directly at the nucleus, and one possible target for this action is a rapid increase in transcription of C/EBP delta seen in 3T3-F442A cells in response to GH. This tyrosine kinase-dependent event may be an archetype for induction of other immediate early gene transcription factors which then interact to determine the programming of the subsequent transcriptional response to GH. 29 refs., 1 fig., 1 tab.

• Sponsoring Organization: USDOE
• OSTI ID: 466618
• Journal Information: Proceedings of the Society for Experimental Biology and Medicine, Journal Name: Proceedings of the Society for Experimental Biology and Medicine Vol. 206; ISSN PSEBAA; ISSN 0037-9727
• Country of Publication: United States
• Language: English

Related Subjects

55 BIOLOGY AND MEDICINE
BASIC STUDIES
ALANINES
AMINO ACIDS
BIOASSAY
BIOLOGICAL LOCALIZATION
CELL NUCLEI
DIMERIZATION
DNA SEQUENCING
DNA-CLONING
GENE REGULATION
LTH
MONOCLONAL ANTIBODIES
MUTAGENESIS
PHOSPHOTRANSFERASES
RECEPTORS
STH
STRUCTURE-ACTIVITY RELATIONSHIPS
SWINE
TRANSCRIPTION
TRANSCRIPTION FACTORS
TYROSINE
UPTAKE