User:Jbrtn44/sandbox
Page to be edited: GABAA receptor
References/Sources:
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4243505/ (Neuroplasticity)
https://www.ncbi.nlm.nih.gov/pubmed/8783370 (Pharmacology)
https://www.ncbi.nlm.nih.gov/pubmed/16594261 (Pathophysiology)
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2574824/ (Alcohol binding)
https://www.ncbi.nlm.nih.gov/pubmed/22243744 (Extrasynaptic GABAa receptors)
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2834934/ (Depolarization)
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4243505/ (GABA d)
https://doi.org/10.1016/S0028-3908(01)00175-7 riluzole as a neuroprotective agent
Edit ideas for the page:
add a "3-D" cartoon picture that shows different binding sites of GABAA
add a section about the clinical significance of GABAA receptors, noting the types of drugs that are used in modern medicine that act on the channel and the physiological effects they have.
Add a section about neuroplasticity.
Delta subunit-
The δ-subunit is usually expressed in GABAA receptors associated with extrasynaptic activity. The most common GABAA subunits have the gamma subunit, which allows the receptor to bind benzodiazepines. For this reason, receptors containing δ-subunits are sometimes referred to as “benzodiazepine insensitive” GABAA receptors. The δ-subunit containing receptors are also known to be involved in the ventral tegmental area (VTA) pathway in the brain's hippocampus, which may mean that they have implications in learning, memory, and reward.[1]
Riluzole
the drug is also known to act allosterically on GABAa receptors. This action serves to postsynaptically potentiate GABAa receptor function. This action is implicated in the drug's neuroprotective qualities in its actions against ALS.[2]
Gabaa
subunits-
the section mentions the most common type of pentameric makeup, i would like to mention another.
Distribution
[edit]GABAA receptors are responsible for most of the physiological activities of GABA in the central nervous system, but the receptor subtypes vary significantly. Subunit composition can vary widely between regions and subtypes may be associated with specific functions. The minimal requirement to produce a GABA-gated ion channel is the inclusion of an α and a β subunit.[3] The most common GABAA receptor is a pentamer comprising two α's, two β's, and a γ (α1β2γ2). In neurons themselves, the type of GABAA receptor subunits and their densities can vary between cell bodies and dendrites.[4] Interestingly, GABAA receptors can also be found in other tissues, including leydig cells, placenta, immune cells, liver, bone growth plates and several other endocrine tissues. Subunit expression varies between 'normal' tissue and malignancies and GABAA receptors can influence cell proliferation.[5]
Isoform | Synaptic/Extrasynaptic | Anatomical location |
---|---|---|
α1β3γ2S | Both | Widespread |
α2β3γ2S | Both | Widespread |
α3β3γ2S | Both | Reticular thalamic nucleus |
α4β3γ2S | Both | Thalamic relay cells |
α5β3γ2S | Both | Hippocampal pyramidal cells |
α6β3γ2S | Both | Cerebellar granule cells |
α1β2γ2S | Both | Widespread, most abundant |
α4β3δ | Extrasynaptic | Thalamic relay cells |
α6β3δ | Extrasynaptic | Cerebellar granule cells |
α1β2 | Extrasynaptic | Widespread |
α1β3 | Extrasynaptic | Thalamus, hypothalamus |
α1β2δ | Extrasynaptic | Hippocampus |
α4β2δ | Extrasynaptic | Hippocampus |
α3β3θ | Extrasynaptic | Hypothalamus |
α3β3ε | Extrasynaptic | Hypothalamus |
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- Peer Review by Caden Duffy: These sources look really good. I didn't notice any problem with them. I'll check back in a couple of days after you have written summaries on a few of them. Biophysics Editor (talk) 15:30, 26 October 2017 (UTC)
- I like the idea of adding a "3-D" picture showing the binding sites of GABAa. It would really clarify for those non-scientists what it is, and how it functions. It looks like they already have some written about the clinical significance and a few examples of drugs that act on the channel. What specific types of drugs are you looking to include? -Caden
- ^ Oiki, S; Koeppe, R E; Andersen, O S (1995-03-14). "Voltage-dependent gating of an asymmetric gramicidin channel". Proceedings of the National Academy of Sciences of the United States of America. 92 (6): 2121–2125. ISSN 0027-8424. PMID 7534411.
- ^ He, Y.; Benz, A.; Fu, T.; Wang, M.; Covey, D.F.; Zorumski, C.F.; Mennerick, S. "Neuroprotective agent riluzole potentiates postsynaptic GABAA receptor function". Neuropharmacology. 42 (2): 199–209. doi:10.1016/s0028-3908(01)00175-7.
- ^ Connolly, Christopher N.; Krishek, Belinda J.; McDonald, Bernard J.; Smart, Trevor G.; Moss, Stephen J. (1996-01-05). "Assembly and Cell Surface Expression of Heteromeric and Homomeric -Aminobutyric Acid Type A Receptors". Journal of Biological Chemistry. 271 (1): 89–96. doi:10.1074/jbc.271.1.89. ISSN 0021-9258. PMID 8550630.
{{cite journal}}
: CS1 maint: unflagged free DOI (link) - ^ Lorenzo, Louis-Etienne; Russier, Michaël; Barbe, Annick; Fritschy, Jean-Marc; Bras, Hélène (2007-09-10). "Differential organization of γ-aminobutyric acid type A and glycine receptors in the somatic and dendritic compartments of rat abducens motoneurons". The Journal of Comparative Neurology. 504 (2): 112–126. doi:10.1002/cne.21442. ISSN 1096-9861.
- ^ "GABA receptors and the immune system - OpenThesis". www.openthesis.org. Retrieved 2017-12-12.
- ^ Mortensen, Martin; Patel, Bijal; Smart, Trevor G. (2012). "GABA Potency at GABAA Receptors Found in Synaptic and Extrasynaptic Zones". Frontiers in Cellular Neuroscience. 6. doi:10.3389/fncel.2012.00001. ISSN 1662-5102.
{{cite journal}}
: CS1 maint: unflagged free DOI (link)