Lysosomal cysteine cathepsins: signaling pathways in apoptosis
Identifieur interne : 000384 ( Istex/Corpus ); précédent : 000383; suivant : 000385Lysosomal cysteine cathepsins: signaling pathways in apoptosis
Auteurs : Veronika Stoka ; Vito Turk ; Boris TurkSource :
- Biological Chemistry [ 14374315 ] ; 2007.
English descriptors
- Teeft :
- Apoptosis, Biochem, Biol, Caspase, Cathepsin, Cathepsins, Cell biol, Cell death, Chem, Cirman, Cleavage, Cysteine, Cysteine cathepsins, Cytochrome, Family members, Guicciardi, Inhibitor, Intrinsic pathway, Kagedal, Lysosomal, Lysosomal cathepsin, Lysosomal cathepsins, Lysosomal membrane, Lysosomal membrane permeabilization, Lysosomal permeabilization, Lysosomal proteases, Lysosome, Mitochondrial, Mitochondrion, Pathway, Permeabilization, Protease, Receptor, Reiners, Stoka.
Abstract
Apoptosis is the major mechanism by which eukaryotic organisms eliminate potentially dangerous, superfluous and damaged cells. Initially, nuclei and mitochondria were found to be the key organelles involved in the process. However, recent data suggest that lysosomes and the endoplasmic reticulum also play important roles in the process. A number of different stimuli were found to directly or indirectly target the lysosomal membrane, thereby inducing lysosomal permeabilization and the release of cysteine cathepsins and the aspartic protease cathepsin D into the cytosol. Once in the cytosol, cathepsins can trigger cell death by different mechanisms. Here we discuss the different signaling pathways used by lysosomal proteases to trigger apoptosis and their potential role in physiological processes.
Url:
DOI: 10.1515/BC.2007.064
Links to Exploration step
ISTEX:ED3A6E841955D5FB1A5382706A9B2709BCA394F1Le document en format XML
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Stefan Institute, SI-1000 Ljubljana, Slovenia</mods:affiliation></affiliation></author><author><name sortKey="Turk, Vito" sort="Turk, Vito" uniqKey="Turk V" first="Vito" last="Turk">Vito Turk</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Biology, J. Stefan Institute, SI-1000 Ljubljana, Slovenia</mods:affiliation></affiliation></author><author><name sortKey="Turk, Boris" sort="Turk, Boris" uniqKey="Turk B" first="Boris" last="Turk">Boris Turk</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Biology, J. Stefan Institute, SI-1000 Ljubljana, Slovenia</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="abbrev">Biological Chemistry</title><idno type="eISSN">14316730</idno><idno type="ISSN">14374315</idno><imprint><publisher>Walter de Gruyter</publisher><date type="e-published">2007</date><biblScope unit="vol">388</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="555">555</biblScope><biblScope unit="page" to="560">560</biblScope><biblScope unit="ref-count">60</biblScope><biblScope unit="fig-count">2</biblScope><biblScope unit="table-count">0</biblScope></imprint><idno type="ISSN">14374315</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">14374315</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Apoptosis</term><term>Biochem</term><term>Biol</term><term>Caspase</term><term>Cathepsin</term><term>Cathepsins</term><term>Cell biol</term><term>Cell death</term><term>Chem</term><term>Cirman</term><term>Cleavage</term><term>Cysteine</term><term>Cysteine cathepsins</term><term>Cytochrome</term><term>Family members</term><term>Guicciardi</term><term>Inhibitor</term><term>Intrinsic pathway</term><term>Kagedal</term><term>Lysosomal</term><term>Lysosomal cathepsin</term><term>Lysosomal cathepsins</term><term>Lysosomal membrane</term><term>Lysosomal membrane permeabilization</term><term>Lysosomal permeabilization</term><term>Lysosomal proteases</term><term>Lysosome</term><term>Mitochondrial</term><term>Mitochondrion</term><term>Pathway</term><term>Permeabilization</term><term>Protease</term><term>Receptor</term><term>Reiners</term><term>Stoka</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Apoptosis is the major mechanism by which eukaryotic organisms eliminate potentially dangerous, superfluous and damaged cells. 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Stefan Institute, SI-1000 Ljubljana, Slovenia</aff></contrib></contrib-group><author-notes><corresp>Corresponding author <email xlink:href="mailto:boris.turk@ijs.si">boris.turk@ijs.si</email></corresp></author-notes><pub-date pub-type="epub"><day>01</day><month>06</month><year>2007</year><string-date>June 2007</string-date></pub-date><volume>388</volume><issue>6</issue><fpage>555</fpage><lpage>560</lpage><copyright-statement>©2007 by Walter de Gruyter Berlin New York</copyright-statement><copyright-year>2007</copyright-year><related-article related-article-type="pdf" xlink:href="bc.2007.064.pdf"></related-article><abstract><title>Abstract</title><p>Apoptosis is the major mechanism by which eukaryotic organisms eliminate potentially dangerous, superfluous and damaged cells. Initially, nuclei and mitochondria were found to be the key organelles involved in the process. However, recent data suggest that lysosomes and the endoplasmic reticulum also play important roles in the process. A number of different stimuli were found to directly or indirectly target the lysosomal membrane, thereby inducing lysosomal permeabilization and the release of cysteine cathepsins and the aspartic protease cathepsin D into the cytosol. Once in the cytosol, cathepsins can trigger cell death by different mechanisms. Here we discuss the different signaling pathways used by lysosomal proteases to trigger apoptosis and their potential role in physiological processes.</p></abstract><kwd-group><title>Keywords</title><kwd>BH3-only protein</kwd><x>, </x><kwd>Bid</kwd><x>, </x><kwd>caspases</kwd><x>, </x><kwd>cathepsins</kwd><x>, </x><kwd>extrinsic pathway</kwd><x>, </x><kwd>intrinsic pathway</kwd><x>, </x><kwd>lysosomes</kwd></kwd-group><counts><fig-count count="2"></fig-count><table-count count="0"></table-count><ref-count count="60"></ref-count></counts></article-meta></front></article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Lysosomal cysteine cathepsins: signaling pathways in apoptosis</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Lysosomal cysteine cathepsins: signaling pathways in apoptosis</title></titleInfo><name type="personal"><namePart type="given">Veronika</namePart><namePart type="family">Stoka</namePart><affiliation>Department of Biochemistry and Molecular Biology, J. Stefan Institute, SI-1000 Ljubljana, Slovenia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Vito</namePart><namePart type="family">Turk</namePart><affiliation>Department of Biochemistry and Molecular Biology, J. Stefan Institute, SI-1000 Ljubljana, Slovenia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Boris</namePart><namePart type="family">Turk</namePart><affiliation>Department of Biochemistry and Molecular Biology, J. 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Here we discuss the different signaling pathways used by lysosomal proteases to trigger apoptosis and their potential role in physiological processes.</abstract><subject><genre>Keywords</genre><topic>BH3-only protein</topic><topic>Bid</topic><topic>caspases</topic><topic>cathepsins</topic><topic>extrinsic pathway</topic><topic>intrinsic pathway</topic><topic>lysosomes</topic></subject><relatedItem type="host"><titleInfo><title>Biological Chemistry</title></titleInfo><titleInfo type="abbreviated"><title>Biological Chemistry</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>Walter de Gruyter</publisher><dateIssued encoding="w3cdtf">2007-06-01</dateIssued><dateCreated encoding="w3cdtf">2007-06-01</dateCreated><copyrightDate encoding="w3cdtf">2007</copyrightDate></originInfo><identifier type="ISSN">14374315</identifier><identifier type="eISSN">14316730</identifier><identifier type="PublisherID">bchm</identifier><part><date>2007</date><detail type="volume"><caption>vol.</caption><number>388</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>555</start><end>560</end></extent></part></relatedItem><identifier type="istex">ED3A6E841955D5FB1A5382706A9B2709BCA394F1</identifier><identifier type="ark">ark:/67375/QT4-7NX8ZR0J-3</identifier><identifier type="DOI">10.1515/BC.2007.064</identifier><identifier type="ArticleID">bc.2007.064</identifier><identifier type="pdf">bc.2007.064.pdf</identifier><accessCondition type="use and reproduction" contentType="copyright">©2007 by Walter de Gruyter Berlin New York, 2007</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-B4QPMMZB-D">degruyter-journals</recordContentSource><recordOrigin>Converted from (version 1.2.5) to MODS version 3.6.</recordOrigin><recordCreationDate encoding="w3cdtf">2020-02-05</recordCreationDate></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/QT4-7NX8ZR0J-3/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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