Structure and function of somatostatin receptors in growth hormone control

in Journal of Endocrinology
Authors:
I Shimon
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S Melmed
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Introduction

The two naturally occurring bioactive peptides, somatostatin (SRIF)-14 and SRIF-28 are physiological regulators of pituitary growth hormone (GH), pancreatic endocrine secretions, and gastrointestinal motility and hormone secretion (Brazeau et al. 1972, Mandarino et al. 1981). These biological effects are mediated through specific high-affinity G-protein-coupled receptors containing seven transmembrane domains. Five distinct SRIF receptor (SSTR) subtypes are located on different chromosomes (Bruno et al. 1992, Yasuda et al. 1992, Roher et al. 1993, Xu et al. 1993, Yamada et al. 1992a,b, 1993), and consist of 364–418-amino acid proteins (39–46 kDa) which display 42–60% identity among the different subtypes and 81–97% homology with rodent receptors (Reisine & Bell 1995). The SSTRs interact with different G-proteins (Rens-Domiano et al. 1992, Law et al. 1993) to inhibit adenylate cyclase activity. Receptor subtypes are also associated with other signal-transduction mechanisms, including cationic channel conductance reduction and tyrosine phosphatase activation (Reisine & Bell

 

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