| First Author | Vanetti M | Year | 1993 |
| Journal | FEBS Lett | Volume | 331 |
| Issue | 3 | Pages | 260-6 |
| PubMed ID | 8104154 | Mgi Jnum | J:15494 |
| Mgi Id | MGI:63614 | Doi | 10.1016/0014-5793(93)80349-y |
| Citation | Vanetti M, et al. (1993) 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 331(3):260-6 |
| abstractText | 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. |
