Caspases Connect Cell-Death Signaling to Organismal Homeostasis.
Identifieur interne : 002266 ( PubMed/Curation ); précédent : 002265; suivant : 002267Caspases Connect Cell-Death Signaling to Organismal Homeostasis.
Auteurs : Lorenzo Galluzzi [France] ; Alejandro L Pez-Soto [Espagne] ; Sharad Kumar [Australie] ; Guido Kroemer [Suède]Source :
- Immunity [ 1097-4180 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
- physiologie : Caspases.
- Animaux, Homéostasie, Humains, Mort cellulaire, Transduction du signal.
English descriptors
- KwdEn :
- MESH :
- chemical , physiology : Caspases.
- Animals, Cell Death, Homeostasis, Humans, Signal Transduction.
Abstract
Some forms of regulated cell death, such as apoptosis, are precipitated by the activation of cysteine proteases of the caspase family, including caspase 8, 9, and 3. Other caspases, such as caspase 1 and 4, are well known for their pro-inflammatory functions but regulate cell death in a limited number of pathophysiological settings. Accumulating evidence suggests that the most conserved function of mammalian caspases is not to control cell death sensu stricto, but to regulate inflammatory and immune reactions to dying cells and infectious challenges. Here, we review the molecular and cellular mechanisms though which mammalian caspases connect cell-death signaling to the maintenance of organismal homeostasis.
DOI: 10.1016/j.immuni.2016.01.020
PubMed: 26885855
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Electronic address: deadoc@vodafone.it.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Equipe 11 labellisée Ligue contre le Cancer, Centre de Recherche des Cordeliers, 75006 Paris, France; INSERM, U1138, 75006 Paris, France; Université Paris Descartes/Paris V, Sorbonne Paris Cité, 75006 Paris, France; Université Pierre et Marie Curie/Paris VI, 75006 Paris, France; Gustave Roussy Comprehensive Cancer Institute, 94805 Villejuif</wicri:regionArea></affiliation></author><author><name sortKey="L Pez Soto, Alejandro" sort="L Pez Soto, Alejandro" uniqKey="L Pez Soto A" first="Alejandro" last="L Pez-Soto">Alejandro L Pez-Soto</name><affiliation wicri:level="1"><nlm:affiliation>Equipe 11 labellisée Ligue contre le Cancer, Centre de Recherche des Cordeliers, 75006 Paris, France; INSERM, U1138, 75006 Paris, France; Université Paris Descartes/Paris V, Sorbonne Paris Cité, 75006 Paris, France; Université Pierre et Marie Curie/Paris VI, 75006 Paris, France; Gustave Roussy Comprehensive Cancer Institute, 94805 Villejuif, France; Hospital Universitario Central de Asturia, Área de Inmunología. Universidad de Oviedo, IUOPA, 33006 Oviedo, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Equipe 11 labellisée Ligue contre le Cancer, Centre de Recherche des Cordeliers, 75006 Paris, France; INSERM, U1138, 75006 Paris, France; Université Paris Descartes/Paris V, Sorbonne Paris Cité, 75006 Paris, France; Université Pierre et Marie Curie/Paris VI, 75006 Paris, France; Gustave Roussy Comprehensive Cancer Institute, 94805 Villejuif, France; Hospital Universitario Central de Asturia, Área de Inmunología. Universidad de Oviedo, IUOPA, 33006 Oviedo</wicri:regionArea></affiliation></author><author><name sortKey="Kumar, Sharad" sort="Kumar, Sharad" uniqKey="Kumar S" first="Sharad" last="Kumar">Sharad Kumar</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Cancer Biology, University of South Australia, 5000 Adelaide, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Centre for Cancer Biology, University of South Australia, 5000 Adelaide</wicri:regionArea></affiliation></author><author><name sortKey="Kroemer, Guido" sort="Kroemer, Guido" uniqKey="Kroemer G" first="Guido" last="Kroemer">Guido Kroemer</name><affiliation wicri:level="1"><nlm:affiliation>Equipe 11 labellisée Ligue contre le Cancer, Centre de Recherche des Cordeliers, 75006 Paris, France; INSERM, U1138, 75006 Paris, France; Université Paris Descartes/Paris V, Sorbonne Paris Cité, 75006 Paris, France; Université Pierre et Marie Curie/Paris VI, 75006 Paris, France; Metabolomics and Cell Biology Platforms, Gustave Roussy Comprehensive Cancer Institute, 94805 Villejuif, France; Pôle de Biologie, Hôpital Européen Georges Pompidou, Assistance Publique-Hôpitaux de Paris, 75015 Paris, France; Department of Women's and Children's Health, Karolinska University Hospital, 17176 Stockholm, Sweden. Electronic address: kroemer@orange.fr.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Equipe 11 labellisée Ligue contre le Cancer, Centre de Recherche des Cordeliers, 75006 Paris, France; INSERM, U1138, 75006 Paris, France; Université Paris Descartes/Paris V, Sorbonne Paris Cité, 75006 Paris, France; Université Pierre et Marie Curie/Paris VI, 75006 Paris, France; Metabolomics and Cell Biology Platforms, Gustave Roussy Comprehensive Cancer Institute, 94805 Villejuif, France; Pôle de Biologie, Hôpital Européen Georges Pompidou, Assistance Publique-Hôpitaux de Paris, 75015 Paris, France; Department of Women's and Children's Health, Karolinska University Hospital, 17176 Stockholm</wicri:regionArea></affiliation></author></analytic><series><title level="j">Immunity</title><idno type="eISSN">1097-4180</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Caspases (physiology)</term><term>Cell Death</term><term>Homeostasis</term><term>Humans</term><term>Signal Transduction</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Caspases (physiologie)</term><term>Homéostasie</term><term>Humains</term><term>Mort cellulaire</term><term>Transduction du signal</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Caspases</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Caspases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Death</term><term>Homeostasis</term><term>Humans</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Homéostasie</term><term>Humains</term><term>Mort cellulaire</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Some forms of regulated cell death, such as apoptosis, are precipitated by the activation of cysteine proteases of the caspase family, including caspase 8, 9, and 3. Other caspases, such as caspase 1 and 4, are well known for their pro-inflammatory functions but regulate cell death in a limited number of pathophysiological settings. Accumulating evidence suggests that the most conserved function of mammalian caspases is not to control cell death sensu stricto, but to regulate inflammatory and immune reactions to dying cells and infectious challenges. Here, we review the molecular and cellular mechanisms though which mammalian caspases connect cell-death signaling to the maintenance of organismal homeostasis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26885855</PMID><DateCreated><Year>2016</Year><Month>02</Month><Day>18</Day></DateCreated><DateCompleted><Year>2016</Year><Month>06</Month><Day>30</Day></DateCompleted><DateRevised><Year>2016</Year><Month>02</Month><Day>18</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1097-4180</ISSN><JournalIssue CitedMedium="Internet"><Volume>44</Volume><Issue>2</Issue><PubDate><Year>2016</Year><Month>Feb</Month><Day>16</Day></PubDate></JournalIssue><Title>Immunity</Title><ISOAbbreviation>Immunity</ISOAbbreviation></Journal><ArticleTitle>Caspases Connect Cell-Death Signaling to Organismal Homeostasis.</ArticleTitle><Pagination><MedlinePgn>221-31</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.immuni.2016.01.020</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S1074-7613(16)30007-3</ELocationID><Abstract><AbstractText>Some forms of regulated cell death, such as apoptosis, are precipitated by the activation of cysteine proteases of the caspase family, including caspase 8, 9, and 3. Other caspases, such as caspase 1 and 4, are well known for their pro-inflammatory functions but regulate cell death in a limited number of pathophysiological settings. Accumulating evidence suggests that the most conserved function of mammalian caspases is not to control cell death sensu stricto, but to regulate inflammatory and immune reactions to dying cells and infectious challenges. Here, we review the molecular and cellular mechanisms though which mammalian caspases connect cell-death signaling to the maintenance of organismal homeostasis.</AbstractText><CopyrightInformation>Copyright © 2016 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Galluzzi</LastName><ForeName>Lorenzo</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Equipe 11 labellisée Ligue contre le Cancer, Centre de Recherche des Cordeliers, 75006 Paris, France; INSERM, U1138, 75006 Paris, France; Université Paris Descartes/Paris V, Sorbonne Paris Cité, 75006 Paris, France; Université Pierre et Marie Curie/Paris VI, 75006 Paris, France; Gustave Roussy Comprehensive Cancer Institute, 94805 Villejuif, France. Electronic address: deadoc@vodafone.it.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>López-Soto</LastName><ForeName>Alejandro</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Equipe 11 labellisée Ligue contre le Cancer, Centre de Recherche des Cordeliers, 75006 Paris, France; INSERM, U1138, 75006 Paris, France; Université Paris Descartes/Paris V, Sorbonne Paris Cité, 75006 Paris, France; Université Pierre et Marie Curie/Paris VI, 75006 Paris, France; Gustave Roussy Comprehensive Cancer Institute, 94805 Villejuif, France; Hospital Universitario Central de Asturia, Área de Inmunología. Universidad de Oviedo, IUOPA, 33006 Oviedo, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kumar</LastName><ForeName>Sharad</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Centre for Cancer Biology, University of South Australia, 5000 Adelaide, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kroemer</LastName><ForeName>Guido</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Equipe 11 labellisée Ligue contre le Cancer, Centre de Recherche des Cordeliers, 75006 Paris, France; INSERM, U1138, 75006 Paris, France; Université Paris Descartes/Paris V, Sorbonne Paris Cité, 75006 Paris, France; Université Pierre et Marie Curie/Paris VI, 75006 Paris, France; Metabolomics and Cell Biology Platforms, Gustave Roussy Comprehensive Cancer Institute, 94805 Villejuif, France; Pôle de Biologie, Hôpital Européen Georges Pompidou, Assistance Publique-Hôpitaux de Paris, 75015 Paris, France; Department of Women's and Children's Health, Karolinska University Hospital, 17176 Stockholm, Sweden. Electronic address: kroemer@orange.fr.</Affiliation></AffiliationInfo></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="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Immunity</MedlineTA><NlmUniqueID>9432918</NlmUniqueID><ISSNLinking>1074-7613</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="D020169">Caspases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020169" MajorTopicYN="N">Caspases</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016923" MajorTopicYN="Y">Cell Death</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006706" MajorTopicYN="Y">Homeostasis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">apoptosome</Keyword><Keyword MajorTopicYN="N">damage-associated molecular pattern</Keyword><Keyword MajorTopicYN="N">inflammasome</Keyword><Keyword MajorTopicYN="N">mitochondrial outer-membrane permeabilization</Keyword><Keyword MajorTopicYN="N">necroptosis</Keyword><Keyword MajorTopicYN="N">pyroptosis</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>09</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>2</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>2</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>7</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26885855</ArticleId><ArticleId IdType="pii">S1074-7613(16)30007-3</ArticleId><ArticleId IdType="doi">10.1016/j.immuni.2016.01.020</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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