Open AccessCloning and characterization of a fourth human somatostatin receptor.
Author(s) -
Lucia Rohrer,
Friedrich Raulf,
Christian Berthou,
Reinhard Buettner,
Ferdinand Hofstaedter,
Roland Schüle
Publication year - 1993
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.90.9.4196
Subject(s) - somatostatin receptor 3 , somatostatin receptor 1 , somatostatin , somatostatin receptor , somatostatin receptor 2 , receptor , enzyme linked receptor , g protein coupled receptor , biology , peptide sequence , 5 ht5a receptor , microbiology and biotechnology , biochemistry , endocrinology , gene
We have isolated a gene coding for a fourth human somatostatin (somatotropin release-inhibiting factor) receptor. This additional somatostatin receptor (hSSTR4) is specifically expressed in human fetal and adult brain and lung tissue. The deduced amino acid sequence of the receptor displays both sequence and structural homology to three cloned somatostatin receptors as well as to other members of the family of GTP-binding-protein-coupled seven-helix transmembrane-spanning receptors. Pharmacological characterization of the expressed receptor reveals specific, high-affinity binding of somatostatin 14 and somatostatin 28. Surprisingly, several well-characterized synthetic somatostatin analogs fail to exhibit high-affinity binding to hSSTR4, indicating the existence of pharmacologically different receptor subtypes. Our data suggest that the diverse biological effects exerted by somatostatin are mediated by a family of receptors with discrete patterns of expression and different pharmacological properties.