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

FEBS Lett. 1993 Oct 4;331(3):260-6. doi: 10.1016/0014-5793(93)80349-y.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenylate Cyclase Toxin
  • Adenylyl Cyclases / metabolism
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • CHO Cells
  • Cricetinae
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / genetics
  • Mice
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides / chemistry
  • RNA Splicing
  • Receptors, Somatostatin / chemistry
  • Receptors, Somatostatin / metabolism*
  • Recombinant Proteins / metabolism
  • Signal Transduction
  • Somatostatin / metabolism*
  • Structure-Activity Relationship
  • Virulence Factors, Bordetella / pharmacology


  • Adenylate Cyclase Toxin
  • Membrane Glycoproteins
  • Oligodeoxyribonucleotides
  • Receptors, Somatostatin
  • Recombinant Proteins
  • Virulence Factors, Bordetella
  • Somatostatin
  • Adenylyl Cyclases