The two isoforms of the mouse somatostatin receptor (mSSTR2A and mSSTR2B) differ m coupling efficiency to adenylate cyclase and in agonist‐induced receptor desensitization

FEBS Letters

Höllt, Volker¹  Vogt, Gudrun¹  Vanetti, Mirko¹ 

[1] Department of Physiology, Physiologisches Institut, Universität München, Pettenkoferstraße 12, D-80336 München, Germany

关键词: Somatostatin receptor 2 (mSSTR2);    Isoform;    Coupling;    Adenylate cyclase;    Desensitization;   

DOI  :  10.1016/0014-5793(93)80349-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The somatostatin receptor 2 (mSSTR2) is alternatively spliced into two isoforms (mSSTR2A and mSSTR2B) which differ at the C-terminus. Both receptors bind somatostatin peptides with a similar high affinity when stably expressed in CHO-K1 cells. However, the spliced form (mSSTR2B) mediates a more efficient inhibition of adenylate cyclase and is much more resistant to agonist-induced reduction of binding than the longer form (mSSTR2A). These findings indicate that alternative splicing may be a physiological mechanism to modulate receptor desensitization and G-protein coupling of mSSTR2.

【 授权许可】

Unknown