Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes最新文献

{"title":"Binding sites for exogenous and endogenous non-competitive inhibitors of the nicotinic acetylcholine receptor","authors":"Hugo Rubén Arias","doi":"10.1016/S0304-4157(98)00004-5","DOIUrl":"10.1016/S0304-4157(98)00004-5","url":null,"abstract":"<div><p><span>The nicotinic acetylcholine<span><span> receptor (AChR) is the paradigm of the neurotransmitter-gated ion channel superfamily. The pharmacological behavior of the AChR<span> can be described as three basic processes that progress sequentially. First, the neurotransmitter acetylcholine (ACh) binds the receptor. Next, the intrinsically coupled ion channel opens upon ACh binding with subsequent </span></span>ion flux activity. Finally, the AChR becomes desensitized, a process where the ion channel becomes closed in the prolonged presence of ACh. The existing equilibrium among these physiologically relevant processes can be perturbed by the pharmacological action of different drugs. In particular, non-competitive inhibitors (NCIs) inhibit the ion flux and enhance the desensitization rate of the AChR. The action of NCIs was studied using several drugs of exogenous origin. These include compounds such as chlorpromazine (CPZ), triphenylmethylphosphonium (TPMP</span></span>⁺<span>), the local anesthetics QX-222 and meproadifen, trifluoromethyl-iodophenyldiazirine (TID), phencyclidine (PCP), histrionicotoxin (HTX), quinacrine, and ethidium. In order to understand the mechanism by which NCIs exert their pharmacological properties several laboratories have studied the structural characteristics of their binding sites, including their respective locations on the receptor. One of the main objectives of this review is to discuss all available experimental evidence regarding the specific localization of the binding sites for exogenous NCIs. For example, it is known that the so-called luminal NCIs bind to a series of ring-forming amino acids in the ion channel. Particularly CPZ, TPMP</span>⁺<span><span>, QX-222, cembranoids, and PCP bind to the serine, the </span>threonine<span><span>, and the leucine ring, whereas TID and meproadifen bind to the </span>valine<span> and extracellular rings, respectively. On the other hand, quinacrine and ethidium, termed non-luminal NCIs, bind to sites outside the channel lumen. Specifically, quinacrine binds to a non-annular lipid domain located ∼7 Å from the lipid–water interface and ethidium binds to the vestibule of the AChR in a site located ∼46 Å away from the membrane surface and equidistant from both ACh binding sites. The non-annular lipid domain has been suggested to be located at the intermolecular interfaces of the five AChR subunits and/or at the interstices of the four (M1–M4) transmembrane domains<span>. One of the most important concepts in neurochemistry is that receptor proteins can be modulated by endogenous substances other than their specific agonists. Among membrane-embedded receptors, the AChR is one of the best examples of this behavior. In this regard, the AChR is non-competitively modulated by diverse molecules such as lipids (fatty acids and steroids), the neuropeptide substance P, and the neurotransmitter 5-hydroxytryptamine (5-HT). It is important to take into acco","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1376 2","pages":"Pages 173-220"},"PeriodicalIF":0.0,"publicationDate":"1998-08-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(98)00004-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20662391","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Phases and phase transitions of the phosphatidylcholines","authors":"Rumiana Koynova ,&nbsp;Martin Caffrey","doi":"10.1016/S0304-4157(98)00006-9","DOIUrl":"10.1016/S0304-4157(98)00006-9","url":null,"abstract":"<div><p><span>LIPIDAT (http://www.lipidat.chemistry.ohio-state.edu) is an Internet accessible, computerized relational database providing access to the wealth of information scattered throughout the literature concerning synthetic and biologically derived polar lipid polymorphic and mesomorphic phase behavior and molecular structures. Here, a review of the data subset referring to phosphatidylcholines is presented together with an analysis of these data. This subset represents ca. 60% of all LIPIDAT records. It includes data collected over a 43-year period and consists of 12,208 records obtained from 1573 articles in 106 different journals. An analysis of the data in the subset identifies trends in phosphatidylcholine phase behavior reflecting changes in lipid chain length, unsaturation (number, isomeric type and position of double bonds), asymmetry and branching, type of chain–glycerol linkage (ester, ether, amide), position of chain attachment to the glycerol backbone (1,2- vs. 1,3-) and head group modification. Also included is a summary of the data concerning the effect of pressure, pH, stereochemical purity, and different additives such as salts, </span>saccharides, amino acids and alcohols, on phosphatidylcholine phase behavior. Information on the phase behavior of biologically derived phosphatidylcholines is also presented. This review includes 651 references.</p></div>","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1376 1","pages":"Pages 91-145"},"PeriodicalIF":0.0,"publicationDate":"1998-06-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(98)00006-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20584883","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"P-type calcium ATPases in higher plants – biochemical, molecular and functional properties","authors":"David E. Evans ,&nbsp;Lorraine E. Williams","doi":"10.1016/S0304-4157(97)00009-9","DOIUrl":"10.1016/S0304-4157(97)00009-9","url":null,"abstract":"","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1376 1","pages":"Pages 1-25"},"PeriodicalIF":0.0,"publicationDate":"1998-06-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(97)00009-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20584573","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Microtubule-based membrane movement","authors":"Jon Lane ,&nbsp;Viki Allan","doi":"10.1016/S0304-4157(97)00010-5","DOIUrl":"10.1016/S0304-4157(97)00010-5","url":null,"abstract":"","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1376 1","pages":"Pages 27-55"},"PeriodicalIF":0.0,"publicationDate":"1998-06-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(97)00010-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20583256","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Polarized trafficking of plasma membrane proteins: emerging roles for coats, SNAREs, GTPases and their link to the cytoskeleton","authors":"Benjamin Aroeti,&nbsp;Hana Okhrimenko,&nbsp;Vanda Reich,&nbsp;Ena Orzech","doi":"10.1016/S0304-4157(98)00005-7","DOIUrl":"10.1016/S0304-4157(98)00005-7","url":null,"abstract":"","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1376 1","pages":"Pages 57-90"},"PeriodicalIF":0.0,"publicationDate":"1998-06-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(98)00005-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20583700","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The influenza virus hemagglutinin: a model protein in the study of membrane fusion","authors":"João Ramalho-Santos ,&nbsp;Maria C. Pedroso de Lima","doi":"10.1016/S0304-4157(98)00002-1","DOIUrl":"10.1016/S0304-4157(98)00002-1","url":null,"abstract":"","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1376 1","pages":"Pages 147-154"},"PeriodicalIF":0.0,"publicationDate":"1998-06-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(98)00002-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20584107","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A computer perspective of membranes: molecular dynamics studies of lipid bilayer systems","authors":"D.P Tieleman,&nbsp;S.J Marrink,&nbsp;H.J.C Berendsen","doi":"10.1016/S0304-4157(97)00008-7","DOIUrl":"10.1016/S0304-4157(97)00008-7","url":null,"abstract":"","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1331 3","pages":"Pages 235-270"},"PeriodicalIF":0.0,"publicationDate":"1997-11-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(97)00008-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20437085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ligand conduction and the gated-pore mechanism of transmembrane transport","authors":"Ian C West","doi":"10.1016/S0304-4157(97)00007-5","DOIUrl":"10.1016/S0304-4157(97)00007-5","url":null,"abstract":"","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1331 3","pages":"Pages 213-234"},"PeriodicalIF":0.0,"publicationDate":"1997-11-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(97)00007-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20437084","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Influence of pH gradients on the transbilayer transport of drugs, lipids, peptides and metal ions into large unilamellar vesicles","authors":"Pieter R Cullis ,&nbsp;Michael J Hope ,&nbsp;Marcel B Bally ,&nbsp;Thomas D Madden ,&nbsp;Lawrence D Mayer ,&nbsp;David B Fenske","doi":"10.1016/S0304-4157(97)00006-3","DOIUrl":"10.1016/S0304-4157(97)00006-3","url":null,"abstract":"","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1331 2","pages":"Pages 187-211"},"PeriodicalIF":0.0,"publicationDate":"1997-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(97)00006-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20261481","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Surface plasmon resonance spectroscopy as a tool for investigating the biochemical and biophysical properties of membrane protein systems. I: Theoretical principles","authors":"Zdzislaw Salamon ,&nbsp;H.Angus Macleod ,&nbsp;Gordon Tollin","doi":"10.1016/S0304-4157(97)00004-X","DOIUrl":"10.1016/S0304-4157(97)00004-X","url":null,"abstract":"","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1331 2","pages":"Pages 117-129"},"PeriodicalIF":0.0,"publicationDate":"1997-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(97)00004-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20261478","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}