Abstract
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
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenylate Cyclase Toxin
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Adenylyl Cyclases / metabolism
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Amino Acid Sequence
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Animals
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Base Sequence
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CHO Cells
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Cricetinae
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Membrane Glycoproteins / chemistry
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Membrane Glycoproteins / genetics
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Mice
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Molecular Sequence Data
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Oligodeoxyribonucleotides / chemistry
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RNA Splicing
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Receptors, Somatostatin / chemistry
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Receptors, Somatostatin / metabolism*
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Recombinant Proteins / metabolism
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Signal Transduction
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Somatostatin / metabolism*
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Structure-Activity Relationship
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Virulence Factors, Bordetella / pharmacology
Substances
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Adenylate Cyclase Toxin
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Membrane Glycoproteins
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Oligodeoxyribonucleotides
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Receptors, Somatostatin
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Recombinant Proteins
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Virulence Factors, Bordetella
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Somatostatin
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Adenylyl Cyclases