Phosphorylation: a Molecular Switch in Opioid Tolerance.
From: Department of Biopharmaceutical Sciences and Cancer Center, University of Illinois, Chicago, IL 60612, USA. zjwang@uic.edu
Life sciences
- Publish Date: Sep 2006
- ISSN: 0024-3205
- Volume: 79
- Issue: 18
- Pages: 1681-91
- Medium: Print
- Language: English
- Citation (JAMA): Wang Zaijie Jim, Wang Lili X, et al. Phosphorylation: a Molecular Switch in Opioid Tolerance.. Life Sci. Sep 2006;79:1681-91
Abstract
Protein phosphorylation is a key posttranslational modification mechanism controlling the conformation and activity of many proteins. Increasing evidence has implicated an essential role of phosphorylation by several major protein kinases in promoting and maintaining opioid tolerance. We review some of the most recent studies on protein kinase C (PKC), cyclic AMP dependent protein kinase A (PKA), calcium/calmodulin-dependent protein kinase II (CaMKII), protein kinase G (PKG), and G protein receptor kinase (GRK). These kinases act as the molecular switches to modulate opioid tolerance. Pharmacological interventions at one or more of the protein kinases and phosphatases may provide valuable strategies to improve opioid analgesia by attenuating tolerance to these drugs.
Mesh Headings (Keywords): Animals, Drug Tolerance, Mice, Narcotics, Phosphorylation, Protein Kinases, Rabbits
Check for Full Text / PubMed Unique Identifier (PMID): 16831450
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