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Nicotinic Acetylcholine Receptor Expression
Published by Anonymous on 2007/9/30 (2340 reads)
1: AAPS J. 2006 Jan 13;7(4):E885-94.


Neuronal nicotinic acetylcholine receptor expression and function on nonneuronal cells.

Gahring LC, Rogers SW.

Geriatric Research Education and Clinical Center, Salt Lake City VAMC, Salt Lake City, Utah 84132, USA. Lorise.Gahring@hsc.utah.edu

Of the thousands of proven carcinogens and toxic agents contained within a cigarette, nicotine, while being the addictive agent, is often viewed as the least harmful of these compounds. Nicotine is a lipophilic molecule whose effects on neuronal nicotinic acetylcholine receptors (nAChR) have been primarily focused on its physiologic impact within the confines of the brain and peripheral nervous system. However, recently, many studies have found neuronal nAChRs to be expressed on many different nonneuronal cell types throughout the body, where increasing evidence suggests they have important roles in determining the consequences of nicotine use on multiple organs systems and diseases as diverse as ulcerative colitis, chronic pulmonary obstructive disease, and diabetes, as well as the neurologic disorders of Parkinson's and Alzheimer's disease. This review highlights current evidence for the expression of peripheral nAChRs in cells other than neurons and how they participate in fundamental processes, such as inflammation. Understanding these processes may offer novel therapeutic strategies to approach inflammatory diseases, as well as precautions in the design of interventional drugs.

Publication Types:
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

PMID: 16594641 [PubMed - indexed for MEDLINE]

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2: J Clin Invest. 2003 Jan;111(1):31-3.


Comment on:
J Clin Invest. 2003 Jan;111(1):81-90.

Nicotine exposure and bronchial epithelial cell nicotinic acetylcholine receptor expression in the pathogenesis of lung cancer.

Minna JD.

Hamon Center for Therapeutic Oncology Research and Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA. john.minna@utsouthwestern.edu

Publication Types:
Comment
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 12511585 [PubMed - indexed for MEDLINE]

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3: Biochem Soc Trans. 1994 Aug;22(3):740-5.


Expression and ligand specificity of acetylcholinesterase and the nicotinic receptor: a tale of two cholinergic sites.

Taylor P, Radić Z, Kreienkamp HJ, Maeda R, Luo Z, Fuentes ME, Vellom D, Pickering N.

Department of Pharmacology, University of California, San Diego, La Jolla 92093.

The functional design of the nAChR and AChE rather than their recognition capacities requires divergence in structure of the two binding sites. The receptor requires co-operativity to link ligand occupation to the response, rapid conformational transitions of activation, and slower transitions of desensitization. Hence, its binding sites have evolved at subunit interfaces. By contrast, AChE functions with a large kcat and a comparatively large Km. To do so, it must force acetylcholine through a low-energy transition site that features tetrahedral rather than the ground-state, trigonal conformation around the carbonyl carbon. This requires a high affinity (KD approximately 10(-17) M) for the enzyme complex of the transient transition state. Interestingly, the three-finger peptide toxins (alpha-bungarotoxin and fasciculin), though closely homologous, use different interaction sites on the receptor (the agonist recognition site) and AChE (a peripheral site). Finally, although the two proteins show co-ordinated expression during muscle differentiation, the receptor relies primarily on transcriptional control while AChE expression is post-transcriptional, being controlled by mRNA stability.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 7821676 [PubMed - indexed for MEDLINE]
 

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