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The two isoforms of the mouse somatostatin receptor (mSSTR2A and mSSTR2B) differ m coupling efficiency to adenylate cyclase and in agonist‐induced receptor desensitization
Author(s) -
Vanetti Mirko,
Vogt Gudrun,
Höllt Volker
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80349-y
Subject(s) - adenylate kinase , cyclase , desensitization (medicine) , agonist , chemistry , endocrinology , medicine , homologous desensitization , somatostatin , growth hormone releasing hormone receptor , receptor , coupling (piping) , gene isoform , somatostatin receptor , biology , biochemistry , hormone receptor , materials science , cancer , breast cancer , gene , metallurgy
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.