Lanthanide ion probes of calcium-binding sites on cellular membranes
Identifieur interne : 000842 ( Istex/Corpus ); précédent : 000841; suivant : 000843Lanthanide ion probes of calcium-binding sites on cellular membranes
Auteurs : Cristobal G. Dos RemediosSource :
- Cell Calcium [ 0143-4160 ] ; 1981.
English descriptors
- KwdEn :
- Acta, Acta crystallographica, Acta physiologica scandinavica, Alkaline conditions, American journal, Annual review, Archives internationales, Atomic number, Atpase, Atpase activity, Axonal membrane, Basic chemistry, Bind, Binding sites, Binding stoichiometry, Biochemistry, Biological chemistry, Biological membranes, Biological systems, Biophysical, Biophysical journal, Biophysical research communications, Biophysics, Biophysics acta, Blood cells, Canadian journal, Cardiac, Cardiac microsomes, Cardiac muscle, Cation, Cell biology, Cell calcium, Cell membranes, Cellular, Cellular cardiology, Cellular membranes, Charge density, Coordination number, Divalent, Dual action, Edax method, Electron microscopy, European journal, Extracellular, Febs letters, Fibre, Fluorescence enhancement, Freeze substitution, Frog, General physiology, Heavy metals, High concentrations, Inhibition, Inhibitor, Inorganic chemistry, Intracellular, Ion, Ionic, Ionic radii, Ionic radius, Ionic radius specificity, Ions bind, Ions form, Lanthanide, Lanthanide ions, Lanthanide series, Lanthanum, Liver mitochondria, Localization, Membrane, Membrane biology, Membrane function, Membrane functions, Mitochondrial, Mitochondrial membranes, Mitochondrion, Muscle fibres, Nerve terminals, Neuromuscular junction, Nodal membrane, Other cells, Other membranes, Outer surface, Physiology, Practical problems, Radius, Rapid diffusion, Relative effectiveness, Remedios, Resonance spectroscopy, Reticulum, Sarcolemma, Sarcoplasmic, Sarcoplasmic reticulum, Serious problem, Sialic acid, Skeletal muscle, Skeletal muscle fibres, Skeletal muscle sarcoplasmic reticulum, Smaller ions, Smooth muscle, Smooth muscle strips, Spectrophotometric determination, Stock solutions, Surface membrane, Transmitter release, Transport process, Trivalent, Trivalent cations, Twitch tension, Vesicle, York academy.
- Teeft :
- Acta, Acta crystallographica, Acta physiologica scandinavica, Alkaline conditions, American journal, Annual review, Archives internationales, Atomic number, Atpase, Atpase activity, Axonal membrane, Basic chemistry, Bind, Binding sites, Binding stoichiometry, Biochemistry, Biological chemistry, Biological membranes, Biological systems, Biophysical, Biophysical journal, Biophysical research communications, Biophysics, Biophysics acta, Blood cells, Canadian journal, Cardiac, Cardiac microsomes, Cardiac muscle, Cation, Cell biology, Cell calcium, Cell membranes, Cellular, Cellular cardiology, Cellular membranes, Charge density, Coordination number, Divalent, Dual action, Edax method, Electron microscopy, European journal, Extracellular, Febs letters, Fibre, Fluorescence enhancement, Freeze substitution, Frog, General physiology, Heavy metals, High concentrations, Inhibition, Inhibitor, Inorganic chemistry, Intracellular, Ion, Ionic, Ionic radii, Ionic radius, Ionic radius specificity, Ions bind, Ions form, Lanthanide, Lanthanide ions, Lanthanide series, Lanthanum, Liver mitochondria, Localization, Membrane, Membrane biology, Membrane function, Membrane functions, Mitochondrial, Mitochondrial membranes, Mitochondrion, Muscle fibres, Nerve terminals, Neuromuscular junction, Nodal membrane, Other cells, Other membranes, Outer surface, Physiology, Practical problems, Radius, Rapid diffusion, Relative effectiveness, Remedios, Resonance spectroscopy, Reticulum, Sarcolemma, Sarcoplasmic, Sarcoplasmic reticulum, Serious problem, Sialic acid, Skeletal muscle, Skeletal muscle fibres, Skeletal muscle sarcoplasmic reticulum, Smaller ions, Smooth muscle, Smooth muscle strips, Spectrophotometric determination, Stock solutions, Surface membrane, Transmitter release, Transport process, Trivalent, Trivalent cations, Twitch tension, Vesicle, York academy.
Abstract
Abstract: The chemical basis for the similarity between the lanthanide series of ions and calcium is outlined together with the experimental difficulties associated with the use of these ions. A number of properties of the lanthanide ions are highlighted which make them potentially valuable probe elements. In this context the use of lanthanum and the lanthanide ions in probing calcium sites on cellular membranes is reviewed. In most instances, the lanthanide ions displace membranebound Ca and inhibit Ca-mediated membrane function, but, unlike Ca, these ions do not appear to be transported across cellular membranes (mitochondria may be an exception). Generally two relationships can be demonstrated between the inhibition of the Ca-mediated function and the atomic number of the lanthanide ion. Extracellular membranes appear to respond selectively to Tm(III) while intracellular membranes lack the Tm peak and instead exhibit a broad trend in which the smaller ions are the least effective inhibitors.
Url:
DOI: 10.1016/0143-4160(81)90044-0
Links to Exploration step
ISTEX:261886BEA73820905C625137B57A36E97AC88FB7Le document en format XML
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A number of properties of the lanthanide ions are highlighted which make them potentially valuable probe elements. In this context the use of lanthanum and the lanthanide ions in probing calcium sites on cellular membranes is reviewed. In most instances, the lanthanide ions displace membranebound Ca and inhibit Ca-mediated membrane function, but, unlike Ca, these ions do not appear to be transported across cellular membranes (mitochondria may be an exception). Generally two relationships can be demonstrated between the inhibition of the Ca-mediated function and the atomic number of the lanthanide ion. Extracellular membranes appear to respond selectively to Tm(III) while intracellular membranes lack the Tm peak and instead exhibit a broad trend in which the smaller ions are the least effective inhibitors.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>lanthanide</json:string><json:string>cation</json:string><json:string>mitochondrion</json:string><json:string>vesicle</json:string><json:string>fibre</json:string><json:string>sarcoplasmic</json:string><json:string>lanthanide ions</json:string><json:string>reticulum</json:string><json:string>trivalent</json:string><json:string>biochemistry</json:string><json:string>ion</json:string><json:string>atpase</json:string><json:string>remedios</json:string><json:string>acta</json:string><json:string>cardiac</json:string><json:string>skeletal muscle</json:string><json:string>divalent</json:string><json:string>ionic radius</json:string><json:string>ionic 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review</json:string><json:string>localization</json:string><json:string>ionic</json:string><json:string>bind</json:string></teeft></keywords><author><json:item><name>Cristobal G. dos Remedios</name><affiliations><json:string>Muscle Research Unit, Department of Anatomy, The University of Sydney, N.S.W., 2006, Australia.</json:string></affiliations></json:item></author><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>The chemical basis for the similarity between the lanthanide series of ions and calcium is outlined together with the experimental difficulties associated with the use of these ions. A number of properties of the lanthanide ions are highlighted which make them potentially valuable probe elements. In this context the use of lanthanum and the lanthanide ions in probing calcium sites on cellular membranes is reviewed. In most instances, the lanthanide ions displace membranebound Ca and inhibit Ca-mediated membrane function, but, unlike Ca, these ions do not appear to be transported across cellular membranes (mitochondria may be an exception). Generally two relationships can be demonstrated between the inhibition of the Ca-mediated function and the atomic number of the lanthanide ion. Extracellular membranes appear to respond selectively to Tm(III) while intracellular membranes lack the Tm peak and instead exhibit a broad trend in which the smaller ions are the least effective inhibitors.</abstract><qualityIndicators><score>6.8</score><pdfVersion>1.2</pdfVersion><pdfPageSize>530 x 706 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>0</keywordCount><abstractCharCount>999</abstractCharCount><pdfWordCount>7555</pdfWordCount><pdfCharCount>46570</pdfCharCount><pdfPageCount>23</pdfPageCount><abstractWordCount>150</abstractWordCount></qualityIndicators><title>Lanthanide ion probes of calcium-binding sites on cellular membranes</title><pii><json:string>0143-4160(81)90044-0</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Inorganic Chemistry</title><language><json:string>unknown</json:string></language><volume>vol 2</volume></serie><host><title>Cell Calcium</title><language><json:string>unknown</json:string></language><publicationDate>1981</publicationDate><issn><json:string>0143-4160</json:string></issn><pii><json:string>S0143-4160(00)X0107-8</json:string></pii><volume>2</volume><issue>1</issue><pages><first>29</first><last>51</last></pages><genre><json:string>journal</json:string></genre></host><categories><wos><json:string>science</json:string><json:string>cell biology</json:string></wos><scienceMetrix><json:string>health sciences</json:string><json:string>biomedical research</json:string><json:string>biochemistry & molecular biology</json:string></scienceMetrix><inist><json:string>sciences appliquees, technologies et medecines</json:string><json:string>sciences biologiques et medicales</json:string><json:string>sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1981</publicationDate><copyrightDate>1981</copyrightDate><doi><json:string>10.1016/0143-4160(81)90044-0</json:string></doi><id>261886BEA73820905C625137B57A36E97AC88FB7</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/261886BEA73820905C625137B57A36E97AC88FB7/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/261886BEA73820905C625137B57A36E97AC88FB7/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/261886BEA73820905C625137B57A36E97AC88FB7/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a">Lanthanide ion probes of calcium-binding sites on cellular membranes</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1981</date></publicationStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Lanthanide ion probes of calcium-binding sites on cellular membranes</title><author xml:id="author-0000"><persName><forename type="first">Cristobal G.</forename><surname>dos Remedios</surname></persName><affiliation>Muscle Research Unit, Department of Anatomy, The University of Sydney, N.S.W., 2006, Australia.</affiliation></author><idno type="istex">261886BEA73820905C625137B57A36E97AC88FB7</idno><idno type="DOI">10.1016/0143-4160(81)90044-0</idno><idno type="PII">0143-4160(81)90044-0</idno></analytic><monogr><title level="j">Cell Calcium</title><title level="j" type="abbrev">YCECA</title><idno type="pISSN">0143-4160</idno><idno type="PII">S0143-4160(00)X0107-8</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1981"></date><biblScope unit="volume">2</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="29">29</biblScope><biblScope unit="page" to="51">51</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1981</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>The chemical basis for the similarity between the lanthanide series of ions and calcium is outlined together with the experimental difficulties associated with the use of these ions. A number of properties of the lanthanide ions are highlighted which make them potentially valuable probe elements. In this context the use of lanthanum and the lanthanide ions in probing calcium sites on cellular membranes is reviewed. In most instances, the lanthanide ions displace membranebound Ca and inhibit Ca-mediated membrane function, but, unlike Ca, these ions do not appear to be transported across cellular membranes (mitochondria may be an exception). Generally two relationships can be demonstrated between the inhibition of the Ca-mediated function and the atomic number of the lanthanide ion. Extracellular membranes appear to respond selectively to Tm(III) while intracellular membranes lack the Tm peak and instead exhibit a broad trend in which the smaller ions are the least effective inhibitors.</p></abstract></profileDesc><revisionDesc><change when="1980-11-27">Modified</change><change when="1981">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/261886BEA73820905C625137B57A36E97AC88FB7/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>YCECA</jid><aid>81900440</aid><ce:pii>0143-4160(81)90044-0</ce:pii><ce:doi>10.1016/0143-4160(81)90044-0</ce:doi><ce:copyright type="unknown" year="1981"></ce:copyright></item-info><head><ce:title>Lanthanide ion probes of calcium-binding sites on cellular membranes</ce:title><ce:author-group><ce:author><ce:given-name>Cristobal G.</ce:given-name><ce:surname>dos Remedios</ce:surname></ce:author><ce:affiliation><ce:textfn>Muscle Research Unit, Department of Anatomy, The University of Sydney, N.S.W., 2006, Australia.</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="25" month="7" year="1980"></ce:date-received><ce:date-revised day="27" month="11" year="1980"></ce:date-revised><ce:date-accepted day="11" month="12" year="1980"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The chemical basis for the similarity between the lanthanide series of ions and calcium is outlined together with the experimental difficulties associated with the use of these ions. A number of properties of the lanthanide ions are highlighted which make them potentially valuable probe elements. In this context the use of lanthanum and the lanthanide ions in probing calcium sites on cellular membranes is reviewed. In most instances, the lanthanide ions displace membranebound Ca and inhibit Ca-mediated membrane function, but, unlike Ca, these ions do not appear to be transported across cellular membranes (mitochondria may be an exception). Generally two relationships can be demonstrated between the inhibition of the Ca-mediated function and the atomic number of the lanthanide ion. Extracellular membranes appear to respond selectively to Tm(III) while intracellular membranes lack the Tm peak and instead exhibit a broad trend in which the smaller ions are the least effective inhibitors.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Lanthanide ion probes of calcium-binding sites on cellular membranes</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Lanthanide ion probes of calcium-binding sites on cellular membranes</title></titleInfo><name type="personal"><namePart type="given">Cristobal G.</namePart><namePart type="family">dos Remedios</namePart><affiliation>Muscle Research Unit, Department of Anatomy, The University of Sydney, N.S.W., 2006, Australia.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1981</dateIssued><dateModified encoding="w3cdtf">1980-11-27</dateModified><copyrightDate encoding="w3cdtf">1981</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The chemical basis for the similarity between the lanthanide series of ions and calcium is outlined together with the experimental difficulties associated with the use of these ions. A number of properties of the lanthanide ions are highlighted which make them potentially valuable probe elements. In this context the use of lanthanum and the lanthanide ions in probing calcium sites on cellular membranes is reviewed. In most instances, the lanthanide ions displace membranebound Ca and inhibit Ca-mediated membrane function, but, unlike Ca, these ions do not appear to be transported across cellular membranes (mitochondria may be an exception). Generally two relationships can be demonstrated between the inhibition of the Ca-mediated function and the atomic number of the lanthanide ion. Extracellular membranes appear to respond selectively to Tm(III) while intracellular membranes lack the Tm peak and instead exhibit a broad trend in which the smaller ions are the least effective inhibitors.</abstract><relatedItem type="host"><titleInfo><title>Cell Calcium</title></titleInfo><titleInfo type="abbreviated"><title>YCECA</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">198102</dateIssued></originInfo><identifier type="ISSN">0143-4160</identifier><identifier type="PII">S0143-4160(00)X0107-8</identifier><part><date>198102</date><detail type="volume"><number>2</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>123</end></extent><extent unit="pages"><start>29</start><end>51</end></extent></part></relatedItem><identifier type="istex">261886BEA73820905C625137B57A36E97AC88FB7</identifier><identifier type="ark">ark:/67375/6H6-25QMVM8W-H</identifier><identifier type="DOI">10.1016/0143-4160(81)90044-0</identifier><identifier type="PII">0143-4160(81)90044-0</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/document/261886BEA73820905C625137B57A36E97AC88FB7/metadata/json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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