Document Detail


The somatostatin receptors SSTR1 and SSTR2 are coupled to inhibition of adenylyl cyclase in Chinese hamster ovary cells via pertussis toxin-sensitive pathways.
MedLine Citation:
PMID:  7907016     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Somatostatin exerts multiple effects throughout the body by binding to specific somatostatin receptors. Two classes of somatostatin receptors, SRIF1 and SRIF2, have been distinguished biochemically and pharmacologically. Two cDNAs have been recently isolated that encode somatostatin receptors 1 and 2 (SSTR1 and SSTR2, respectively). The pharmacological characteristics of receptors expressing these cDNAs resemble those of the SRIF2 and SRIF1 classes of somatostatin receptors, respectively. We stably expressed the rat homologs of both receptors in Chinese hamster ovary (CHO) cells (type K1). These transfected cell lines recognized the endogenous ligands SS14 and SS28 with high affinity, whereas the synthetic analog MK678 identified only SSTR2. In preparations of CHO-SSTR1 or CHO-SSTR2 cells, SS14 and SS28 inhibited forskolin-stimulated adenylyl cyclase activity by approximately 35%, with ED50 values in the nanomolar range. The adenylyl cyclase inhibition was dependent upon the guanine nucleotide GTP and could be ablated with pertussis toxin preincubation. The present data indicate that SSTR1 and SSTR2 are coupled to inhibition of adenylyl cyclase via pertussis toxin- sensitive G-proteins.
Authors:
R E Hershberger; B L Newman; T Florio; J Bunzow; O Civelli; X J Li; M Forte; P J Stork
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Endocrinology     Volume:  134     ISSN:  0013-7227     ISO Abbreviation:  Endocrinology     Publication Date:  1994 Mar 
Date Detail:
Created Date:  1994-04-07     Completed Date:  1994-04-07     Revised Date:  2005-11-17    
Medline Journal Info:
Nlm Unique ID:  0375040     Medline TA:  Endocrinology     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1277-85     Citation Subset:  AIM; IM    
Affiliation:
Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland 97201.
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MeSH Terms
Descriptor/Qualifier:
Adenylate Cyclase / antagonists & inhibitors*
Adenylate Cyclase Toxin*
Animals
Blotting, Northern
CHO Cells
Cloning, Molecular
Cricetinae
Cricetulus
GTP-Binding Proteins / physiology
Guanylyl Imidodiphosphate / pharmacology
Pertussis Toxin*
Receptors, Somatostatin / genetics,  physiology*
Somatostatin / metabolism
Virulence Factors, Bordetella / pharmacology*
Chemical
Reg. No./Substance:
0/Adenylate Cyclase Toxin; 0/Receptors, Somatostatin; 0/Virulence Factors, Bordetella; 34273-04-6/Guanylyl Imidodiphosphate; 51110-01-1/Somatostatin; EC 2.4.2.31/Pertussis Toxin; EC 3.6.1.-/GTP-Binding Proteins; EC 4.6.1.1/Adenylate Cyclase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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