Proline isomerases at the crossroads of protein folding, signal transduction, and immunosuppression.
Identifieur interne : 001B47 ( Main/Exploration ); précédent : 001B46; suivant : 001B48Proline isomerases at the crossroads of protein folding, signal transduction, and immunosuppression.
Auteurs : J. Heitman [Suisse] ; N R Movva ; M N HallSource :
- The New biologist [ 1043-4674 ] ; 1992.
Descripteurs français
- KwdFr :
- Activation des lymphocytes (MeSH), Amino-acid isomerases (physiologie), Conformation des protéines (MeSH), Humains (MeSH), Immunosuppresseurs (pharmacologie), Lymphocytes T (immunologie), Modèles moléculaires (MeSH), Peptidylpropyl isomerase (MeSH), Protéines de liaison au tacrolimus (MeSH), Protéines de transport (génétique), Protéines de transport (physiologie), Saccharomyces cerevisiae (génétique), Transduction du signal (MeSH).
- MESH :
- génétique : Protéines de transport, Saccharomyces cerevisiae.
- immunologie : Lymphocytes T.
- pharmacologie : Immunosuppresseurs.
- physiologie : Amino-acid isomerases, Protéines de transport.
- Activation des lymphocytes, Conformation des protéines, Humains, Modèles moléculaires, Peptidylpropyl isomerase, Protéines de liaison au tacrolimus, Transduction du signal.
English descriptors
- KwdEn :
- Amino Acid Isomerases (physiology), Carrier Proteins (genetics), Carrier Proteins (physiology), Humans (MeSH), Immunosuppressive Agents (pharmacology), Lymphocyte Activation (MeSH), Models, Molecular (MeSH), Peptidylprolyl Isomerase (MeSH), Protein Conformation (MeSH), Saccharomyces cerevisiae (genetics), Signal Transduction (MeSH), T-Lymphocytes (immunology), Tacrolimus Binding Proteins (MeSH).
- MESH :
- chemical , genetics : Carrier Proteins.
- chemical , pharmacology : Immunosuppressive Agents.
- chemical , physiology : Amino Acid Isomerases, Carrier Proteins.
- genetics : Saccharomyces cerevisiae.
- immunology : T-Lymphocytes.
- Humans, Lymphocyte Activation, Models, Molecular, Peptidylprolyl Isomerase, Protein Conformation, Signal Transduction, Tacrolimus Binding Proteins.
Abstract
The immunosuppressants cyclosporin A (CsA), FK506, and rapamycin block T-cell activation by interfering with signal transduction. The institution of CsA therapy for prophylaxis against graft rejection revolutionized human organ transplants, and clinical trials with FK506 and rapamycin are in progress. The targets for these drugs, cyclophilin for CsA and FKBP for FK506 and rapamycin, are members of two unrelated families of ubiquitous, highly conserved, abundant proteins. Although unrelated, both cyclophilin and FKBP catalyze proline isomerization and may fold proteins. The structures of both cyclophilin and FKBP have been determined, in some cases in complex with drugs or substrates. The cyclophilin-CsA and FKBP-FK506 complexes prevent T-cell response to antigen, bind and modulate the activity of the protein phosphatase calcineurin, and prevent nuclear import of a subunit of NF-AT, a T-cell activation transcription factor. In contrast, rapamycin blocks T-cell responses to IL-2. Yeast genetic studies suggest that the FKBP-rapamycin target is a protein complex involved in cell cycle progression. Further studies should provide fundamental insights into T-cell activation, signal transduction, and protein folding, and hold the promise of more specific immunosuppressive therapies.
PubMed: 1515410
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Heitman</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Biocenter of the University of Basel, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Department of Biochemistry, Biocenter of the University of Basel</wicri:regionArea><wicri:noRegion>Biocenter of the University of Basel</wicri:noRegion></affiliation></author><author><name sortKey="Movva, N R" sort="Movva, N R" uniqKey="Movva N" first="N R" last="Movva">N R Movva</name></author><author><name sortKey="Hall, M N" sort="Hall, M N" uniqKey="Hall M" first="M N" last="Hall">M N Hall</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1992">1992</date><idno type="RBID">pubmed:1515410</idno><idno type="pmid">1515410</idno><idno type="wicri:Area/Main/Corpus">001B48</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001B48</idno><idno type="wicri:Area/Main/Curation">001B48</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001B48</idno><idno type="wicri:Area/Main/Exploration">001B48</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Proline isomerases at the crossroads of protein folding, signal transduction, and immunosuppression.</title><author><name sortKey="Heitman, J" sort="Heitman, J" uniqKey="Heitman J" first="J" last="Heitman">J. Heitman</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Biocenter of the University of Basel, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Department of Biochemistry, Biocenter of the University of Basel</wicri:regionArea><wicri:noRegion>Biocenter of the University of Basel</wicri:noRegion></affiliation></author><author><name sortKey="Movva, N R" sort="Movva, N R" uniqKey="Movva N" first="N R" last="Movva">N R Movva</name></author><author><name sortKey="Hall, M N" sort="Hall, M N" uniqKey="Hall M" first="M N" last="Hall">M N Hall</name></author></analytic><series><title level="j">The New biologist</title><idno type="ISSN">1043-4674</idno><imprint><date when="1992" type="published">1992</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Isomerases (physiology)</term><term>Carrier Proteins (genetics)</term><term>Carrier Proteins (physiology)</term><term>Humans (MeSH)</term><term>Immunosuppressive Agents (pharmacology)</term><term>Lymphocyte Activation (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Peptidylprolyl Isomerase (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Signal Transduction (MeSH)</term><term>T-Lymphocytes (immunology)</term><term>Tacrolimus Binding Proteins (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation des lymphocytes (MeSH)</term><term>Amino-acid isomerases (physiologie)</term><term>Conformation des protéines (MeSH)</term><term>Humains (MeSH)</term><term>Immunosuppresseurs (pharmacologie)</term><term>Lymphocytes T (immunologie)</term><term>Modèles moléculaires (MeSH)</term><term>Peptidylpropyl isomerase (MeSH)</term><term>Protéines de liaison au tacrolimus (MeSH)</term><term>Protéines de transport (génétique)</term><term>Protéines de transport (physiologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Carrier Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Immunosuppressive Agents</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Amino Acid Isomerases</term><term>Carrier Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de transport</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Lymphocytes T</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>T-Lymphocytes</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Immunosuppresseurs</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Amino-acid isomerases</term><term>Protéines de transport</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Lymphocyte Activation</term><term>Models, Molecular</term><term>Peptidylprolyl Isomerase</term><term>Protein Conformation</term><term>Signal Transduction</term><term>Tacrolimus Binding Proteins</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation des lymphocytes</term><term>Conformation des protéines</term><term>Humains</term><term>Modèles moléculaires</term><term>Peptidylpropyl isomerase</term><term>Protéines de liaison au tacrolimus</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The immunosuppressants cyclosporin A (CsA), FK506, and rapamycin block T-cell activation by interfering with signal transduction. The institution of CsA therapy for prophylaxis against graft rejection revolutionized human organ transplants, and clinical trials with FK506 and rapamycin are in progress. The targets for these drugs, cyclophilin for CsA and FKBP for FK506 and rapamycin, are members of two unrelated families of ubiquitous, highly conserved, abundant proteins. Although unrelated, both cyclophilin and FKBP catalyze proline isomerization and may fold proteins. The structures of both cyclophilin and FKBP have been determined, in some cases in complex with drugs or substrates. The cyclophilin-CsA and FKBP-FK506 complexes prevent T-cell response to antigen, bind and modulate the activity of the protein phosphatase calcineurin, and prevent nuclear import of a subunit of NF-AT, a T-cell activation transcription factor. In contrast, rapamycin blocks T-cell responses to IL-2. Yeast genetic studies suggest that the FKBP-rapamycin target is a protein complex involved in cell cycle progression. Further studies should provide fundamental insights into T-cell activation, signal transduction, and protein folding, and hold the promise of more specific immunosuppressive therapies.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1515410</PMID><DateCompleted><Year>1992</Year><Month>10</Month><Day>02</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1043-4674</ISSN><JournalIssue CitedMedium="Print"><Volume>4</Volume><Issue>5</Issue><PubDate><Year>1992</Year><Month>May</Month></PubDate></JournalIssue><Title>The New biologist</Title><ISOAbbreviation>New Biol</ISOAbbreviation></Journal><ArticleTitle>Proline isomerases at the crossroads of protein folding, signal transduction, and immunosuppression.</ArticleTitle><Pagination><MedlinePgn>448-60</MedlinePgn></Pagination><Abstract><AbstractText>The immunosuppressants cyclosporin A (CsA), FK506, and rapamycin block T-cell activation by interfering with signal transduction. The institution of CsA therapy for prophylaxis against graft rejection revolutionized human organ transplants, and clinical trials with FK506 and rapamycin are in progress. The targets for these drugs, cyclophilin for CsA and FKBP for FK506 and rapamycin, are members of two unrelated families of ubiquitous, highly conserved, abundant proteins. Although unrelated, both cyclophilin and FKBP catalyze proline isomerization and may fold proteins. The structures of both cyclophilin and FKBP have been determined, in some cases in complex with drugs or substrates. The cyclophilin-CsA and FKBP-FK506 complexes prevent T-cell response to antigen, bind and modulate the activity of the protein phosphatase calcineurin, and prevent nuclear import of a subunit of NF-AT, a T-cell activation transcription factor. In contrast, rapamycin blocks T-cell responses to IL-2. Yeast genetic studies suggest that the FKBP-rapamycin target is a protein complex involved in cell cycle progression. Further studies should provide fundamental insights into T-cell activation, signal transduction, and protein folding, and hold the promise of more specific immunosuppressive therapies.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Heitman</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Biocenter of the University of Basel, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Movva</LastName><ForeName>N R</ForeName><Initials>NR</Initials></Author><Author ValidYN="Y"><LastName>Hall</LastName><ForeName>M N</ForeName><Initials>MN</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>New Biol</MedlineTA><NlmUniqueID>9000976</NlmUniqueID><ISSNLinking>1043-4674</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007166">Immunosuppressive Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.1.1.-</RegistryNumber><NameOfSubstance UI="D000591">Amino Acid Isomerases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.2.1.-</RegistryNumber><NameOfSubstance UI="D022021">Tacrolimus Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.2.1.8</RegistryNumber><NameOfSubstance UI="D019696">Peptidylprolyl Isomerase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000591" MajorTopicYN="N">Amino Acid Isomerases</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007166" MajorTopicYN="N">Immunosuppressive Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008213" MajorTopicYN="N">Lymphocyte Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019696" MajorTopicYN="N">Peptidylprolyl Isomerase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013601" MajorTopicYN="N">T-Lymphocytes</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D022021" MajorTopicYN="N">Tacrolimus Binding Proteins</DescriptorName></MeshHeading></MeshHeadingList><NumberOfReferences>121</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1992</Year><Month>5</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1992</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1992</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1515410</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country></list><tree><noCountry><name sortKey="Hall, M N" sort="Hall, M N" uniqKey="Hall M" first="M N" last="Hall">M N Hall</name><name sortKey="Movva, N R" sort="Movva, N R" uniqKey="Movva N" first="N R" last="Movva">N R Movva</name></noCountry><country name="Suisse"><noRegion><name sortKey="Heitman, J" sort="Heitman, J" uniqKey="Heitman J" first="J" last="Heitman">J. 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