作者: P. Dournaud , A. Slama , A. Beaudet , J. Epelbaum
DOI: 10.1016/S0924-8196(00)80003-2
关键词: Internal medicine 、 Anterior pituitary 、 Binding site 、 Chemistry 、 Somatostatin 、 Somatostatin receptor 2 、 Endocrinology 、 Biochemistry 、 Somatostatin receptor 、 Somatostatin receptor 1 、 Somatostatin binding 、 Somatostatin receptor 3
摘要: Publisher Summary Somatostatin (somatotropin release-inhibiting factor, SRIF) was initially characterized as a 14-amino acid hypothalamic neurohormonal peptide involved in the inhibitory control of growth hormone (GH) secretion from anterior pituitary somatotrophs. binding sites were first identified clonal cell line (GH4C1) by radioligand studies using monoiodinated somatostatin analog (tyrosine-substituted position eleven). Brain subsequently and shown to be sensitive guanine nucleotides divalent cations that indicated they coupled trimeric G proteins. Numerous physiological pharmacological have pointed existence multiplicity brain receptor subtypes. classified into two subclasses, based on differential analogs such octreotide. The octreotide-sensitive insensitive also differentiated their ionic requirements millimolar magnesium 120 sodium, respectively. This chapter tabulates affinities maximal capacities most commonly used radioactive ligands for SRIF1 SRIF2 sites. focuses more recent data concerning selective distribution individual sst subtypes gathered autoradiography, situ hybridization, immunohistochemistry.