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Gβγ that interacts with adenylyl cyclase in opioid tolerance originates from a Gs protein by Hoau‐Yan Wang; Lindsay H. Burns is a Neuroscience article available to read on EtoBox.

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## Abstract We previously demonstrated that chronic morphine induces a change in G protein coupling by the mu opioid receptor (MOR) from Gi/o to Gs, concurrent with the instatement of an interaction between Gβγ and adenylyl cyclase types II and IV. These two signaling changes confer excitatory effects on the cell in place of the typical inhibition by opioids and are associated with morphine tolerance and dependence. Both signaling changes and these behavioral manifestations of chronic morphine are attenuated by cotreatment with ultra‐low‐dose naloxone. In the present work, using striatum from chronic morphine‐treated rats, we isotyped the Gβ within Gs and Go heterotrimers that coupled to MOR and compared these to the Gβ isotype of the Gβγ that interacted with adenylyl cyclase II or IV after chronic morphine treatment. Isotyping results show that chronic morphine causes a Gs heterotrimer associated with MOR to release its Gβγ to interact with adenylyl cyclase. These data suggest that the switch to Gs coupling by MOR in response to chronic morphine, which is attenuated by ultra‐low‐dose opioid antagonist cotreatment, leads to a two‐pronged stimulation of adenylyl cyclase utilizing bo

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Author
Hoau‐Yan Wang; Lindsay H. Burns
Publisher
John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0022-3034)
Published
2006
Language
EN
Field
Neuroscience (Life Sciences)

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