Special Issue "Oligomerization & Trafficking of Opioid Receptors"
A special issue of Cells (ISSN 2073-4409).
Deadline for manuscript submissions: closed (15 October 2013)
Dr. Catia Sternini
David Geffen School of Medicine at UCLA, CURE Bldg.115 Room 221, VAGLAHS, 11301 Wilshire Blvd., Los Angeles, CA 90073, USA
Dr. Alexander E. Kalyuzhny
Neuroscience, UMN Twin Cities, 6-145 Jackson Hall, 321 Church St SE, Minneapolis, MN 55455, USA
Phone: +1 612 624 2991
Interests: physiology of pain; antinociceptive brainstem circuit; cellular localization, trafficking and oligomerization of opioid receptors; drugs of abuse; cytokines and cytokine receptors
It has been found that mu-, delta- and kappa-opioid receptors that belong to G-protein-coupled receptors (GPCRs receptor group can form oligomeric complexes with each other (e.g., DOR-KOR, DOR-MOR) when co-expressed by the same cell. Pharmacological studies indicate that oligomers of opioid receptors react differently to opioid ligands in comparison to their corresponding homomers. Oligomerizatin can be both cell- and tissue-specific and can reflect a pathophysiological condition. There is a suggestion to treat oligomeric opioid receptors as a novel drug target group for which different opioid compounds have to be developed. In addition to differences in ligand selectivity and potency, it appears that desensitization/trafficking of oligomeric opioid receptors is controlled differently compared to homomeric receptors. Oligomerization of of opioid receptors represents a significant challenge in developing potent opioid analgesic compounds of high specificity and minimal negative side effects such as tolerance and dependence. In spite of recent advances in unraveling the process of oligomerization of opioid receptors the mechanisms underlying dynamic interactions between different types of opioid receptors to form heteromers/oligomers are not fully understood. It is not clear, for example, how many specific intracellular factors serve as shaperons that regulate oligomerization of opioid receptors and what controls their plasma membrane-cytoplasm cycling dynamics.
In this special guest issue on " Oligomerization & Trafficking of Opioid Receptors" in the Journal Cells, research articles, technical notes as well as reviews are grouped together to shed light on the mechanisms regulating oligomerization of opioid receptors and their trafficking within the cell. The intent of this special issue is to serve as a forum allowing cell biologists and pharmacologists to exchange their experimental data and theories that can help better understand cellular and biochemical mechanisms of the opioid receptor function.
Dr. Catia Sternini
Dr. Alexander E. Kalyuzhny
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- mu-, delta- and kappa-opioid receptors
- bivalent opioid ligand
- FRET & BRET studies of oligomerization
- immunocytochemical analysis of oligomerization
- tolerance and dependence
- trafficking & desensitization of opioid receptors
- signal transduction
Cells 2013, 2(4), 689-714; doi:10.3390/cells2040689
Received: 21 August 2013; in revised form: 30 September 2013 / Accepted: 9 October 2013 / Published: 11 October 2013| Download PDF Full-text (261 KB)
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Title: Pharmacological Profiles of Oligomerized Mu-Opioid Receptors
Authors: Cynthia Wei-Sheng Lee 1,2 and Ing-Kang Ho 1,3,4
Affiliations: 1 Center for Drug Abuse and Addiction, China Medical University Hospital, Taichung, Taiwan
2 China Medical University, Taichung, Taiwan
3 Graduate Institute of Clinical Medical Science, China Medical University, Taichung, Taiwan
4 Center for Neuropsychiatric Research, National Health Research Institutes, Zhunan, Miaoli County, Taiwan; E-Mail: email@example.com
Abstract: We demonstrated that the drugs used in maintenance therapy for heroin addicts, methadone and buprenorphine, exert initially different yet eventually convergent adaptive changes of adenylate cyclase activity in HEK293 cells coexpressing human μ-opioid and opioid receptor-like 1 receptors. Bivalent ligands targeted to the oligomerized opioid receptors might be the key to developing analgesics without undesired side effects and obtaining effective treatment for opioid addicts. In this review we will update the biological effects of mu-opioids on homo- or hetero-oligomerized μ-opioid receptor and discuss potential mechanisms through which bivalent ligands exert beneficial effects including adenylate cyclase regulation and receptor-mediated signaling pathways.
Last update: 6 June 2013