Inhibition of lysosome degradation on autophagosome formation and responses to GMI, an immunomodulatory protein from Ganoderma microsporum.
Identifieur interne : 000359 ( PubMed/Corpus ); précédent : 000358; suivant : 000360Inhibition of lysosome degradation on autophagosome formation and responses to GMI, an immunomodulatory protein from Ganoderma microsporum.
Auteurs : I-Lun Hsin ; Gwo-Tarng Sheu ; Ming-Shiou Jan ; Hai-Lun Sun ; Tzu-Chin Wu ; Ling-Yen Chiu ; Ko-Huang Lue ; Jiunn-Liang KoSource :
- British journal of pharmacology [ 1476-5381 ] ; 2012.
English descriptors
- KwdEn :
- Autophagy (drug effects), Cell Line, Tumor, Chloroquine (pharmacology), Fungal Proteins (pharmacology), Ganoderma, Gene Silencing, Humans, Immunologic Factors (pharmacology), Lysosomes (drug effects), Macrolides (pharmacology), Phagosomes (drug effects), Proto-Oncogene Proteins c-akt (metabolism), TOR Serine-Threonine Kinases (metabolism), Vacuolar Proton-Translocating ATPases (genetics).
- MESH :
- chemical , genetics : Vacuolar Proton-Translocating ATPases.
- chemical , metabolism : Proto-Oncogene Proteins c-akt, TOR Serine-Threonine Kinases.
- chemical , pharmacology : Chloroquine, Fungal Proteins, Immunologic Factors, Macrolides.
- drug effects : Autophagy, Lysosomes, Phagosomes.
- Cell Line, Tumor, Ganoderma, Gene Silencing, Humans.
Abstract
Autophagic cell death is considered a self-destructive process that results from large amounts of autophagic flux. In our previous study, GMI, a recombinant fungal immunomodulatory protein cloned from Ganoderma microsporum, induced autophagic cell death in lung cancer cells. The aim of this study was to examine the role of autophagosome accumulation in GMI-mediated cell death.
DOI: 10.1111/j.1476-5381.2012.02073.x
PubMed: 22708544
Links to Exploration step
pubmed:22708544Le document en format XML
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last="Wu">Tzu-Chin Wu</name></author><author><name sortKey="Chiu, Ling Yen" sort="Chiu, Ling Yen" uniqKey="Chiu L" first="Ling-Yen" last="Chiu">Ling-Yen Chiu</name></author><author><name sortKey="Lue, Ko Huang" sort="Lue, Ko Huang" uniqKey="Lue K" first="Ko-Huang" last="Lue">Ko-Huang Lue</name></author><author><name sortKey="Ko, Jiunn Liang" sort="Ko, Jiunn Liang" uniqKey="Ko J" first="Jiunn-Liang" last="Ko">Jiunn-Liang Ko</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22708544</idno><idno type="pmid">22708544</idno><idno type="doi">10.1111/j.1476-5381.2012.02073.x</idno><idno type="wicri:Area/PubMed/Corpus">000359</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000359</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Inhibition of lysosome degradation on autophagosome formation and responses to GMI, an immunomodulatory protein from Ganoderma microsporum.</title><author><name sortKey="Hsin, I Lun" sort="Hsin, I Lun" uniqKey="Hsin I" first="I-Lun" last="Hsin">I-Lun Hsin</name><affiliation><nlm:affiliation>Institute of Medical and Molecular Toxicology, Chung Shan Medical University, Taichung, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Sheu, Gwo Tarng" sort="Sheu, Gwo Tarng" uniqKey="Sheu G" first="Gwo-Tarng" last="Sheu">Gwo-Tarng Sheu</name></author><author><name sortKey="Jan, Ming Shiou" sort="Jan, Ming Shiou" uniqKey="Jan M" first="Ming-Shiou" last="Jan">Ming-Shiou Jan</name></author><author><name sortKey="Sun, Hai Lun" sort="Sun, Hai Lun" uniqKey="Sun H" first="Hai-Lun" last="Sun">Hai-Lun Sun</name></author><author><name sortKey="Wu, Tzu Chin" sort="Wu, Tzu Chin" uniqKey="Wu T" first="Tzu-Chin" last="Wu">Tzu-Chin Wu</name></author><author><name sortKey="Chiu, Ling Yen" sort="Chiu, Ling Yen" uniqKey="Chiu L" first="Ling-Yen" last="Chiu">Ling-Yen Chiu</name></author><author><name sortKey="Lue, Ko Huang" sort="Lue, Ko Huang" uniqKey="Lue K" first="Ko-Huang" last="Lue">Ko-Huang Lue</name></author><author><name sortKey="Ko, Jiunn Liang" sort="Ko, Jiunn Liang" uniqKey="Ko J" first="Jiunn-Liang" last="Ko">Jiunn-Liang Ko</name></author></analytic><series><title level="j">British journal of pharmacology</title><idno type="eISSN">1476-5381</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Autophagy (drug effects)</term><term>Cell Line, Tumor</term><term>Chloroquine (pharmacology)</term><term>Fungal Proteins (pharmacology)</term><term>Ganoderma</term><term>Gene Silencing</term><term>Humans</term><term>Immunologic Factors (pharmacology)</term><term>Lysosomes (drug effects)</term><term>Macrolides (pharmacology)</term><term>Phagosomes (drug effects)</term><term>Proto-Oncogene Proteins c-akt (metabolism)</term><term>TOR Serine-Threonine Kinases (metabolism)</term><term>Vacuolar Proton-Translocating ATPases (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Vacuolar Proton-Translocating ATPases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Proto-Oncogene Proteins c-akt</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Chloroquine</term><term>Fungal Proteins</term><term>Immunologic Factors</term><term>Macrolides</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Autophagy</term><term>Lysosomes</term><term>Phagosomes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line, Tumor</term><term>Ganoderma</term><term>Gene Silencing</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Autophagic cell death is considered a self-destructive process that results from large amounts of autophagic flux. In our previous study, GMI, a recombinant fungal immunomodulatory protein cloned from Ganoderma microsporum, induced autophagic cell death in lung cancer cells. The aim of this study was to examine the role of autophagosome accumulation in GMI-mediated cell death.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22708544</PMID><DateCompleted><Year>2013</Year><Month>03</Month><Day>25</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1476-5381</ISSN><JournalIssue CitedMedium="Internet"><Volume>167</Volume><Issue>6</Issue><PubDate><Year>2012</Year><Month>Nov</Month></PubDate></JournalIssue><Title>British journal of pharmacology</Title><ISOAbbreviation>Br. J. Pharmacol.</ISOAbbreviation></Journal><ArticleTitle>Inhibition of lysosome degradation on autophagosome formation and responses to GMI, an immunomodulatory protein from Ganoderma microsporum.</ArticleTitle><Pagination><MedlinePgn>1287-300</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1476-5381.2012.02073.x</ELocationID><Abstract><AbstractText Label="BACKGROUND AND PURPOSE" NlmCategory="OBJECTIVE">Autophagic cell death is considered a self-destructive process that results from large amounts of autophagic flux. In our previous study, GMI, a recombinant fungal immunomodulatory protein cloned from Ganoderma microsporum, induced autophagic cell death in lung cancer cells. The aim of this study was to examine the role of autophagosome accumulation in GMI-mediated cell death.</AbstractText><AbstractText Label="EXPERIMENTAL APPROACH" NlmCategory="METHODS">Western blot analysis, flow cytometry and confocal microscopy were used to evaluate the effects of different treatments, including silencing of ATP6V0A1 by use of short hairpin RNAi, on GMI-mediated cell death, lung cancer cell viability and autophagosome accumulation in vitro.</AbstractText><AbstractText Label="KEY RESULTS" NlmCategory="RESULTS">Lysosome inhibitors bafilomycin-A1 and chloroquine increased GMI-mediated autophagic cell death. GMI and bafilomycin-A1 co-treatment induced the accumulation of large amounts of autophagosomes, but did not significantly induce apoptosis. GMI elicited autophagy through the PKB (Akt)/mammalian target of rapamycin signalling pathway. Silencing of ATP6V0A1, one subunit of vesicular H(+)-ATPases (V-ATPases) that mediates lysosome acidification, spontaneously induced autophagosome accumulation, but did not affect lysosome acidity. GMI-mediated autophagosome accumulation and cytotoxicity was increased in shATP6V0A1 lung cancer cells. Furthermore, ATP6V0A1 silencing decreased autophagosome and lysosome fusion in GMI-treated CaLu-1/GFP-LC3 lung cancer cells.</AbstractText><AbstractText Label="CONCLUSION AND IMPLICATIONS" NlmCategory="CONCLUSIONS">We demonstrated that autophagosome accumulation induces autophagic cell death in a GMI treatment model, and ATP6V0A1 plays an important role in mediating autophagosome-lysosome fusion. Our findings provide new insights into the mechanisms involved in the induction of autophagic cell death.</AbstractText><CopyrightInformation>© 2012 The Authors. British Journal of Pharmacology © 2012 The British Pharmacological Society.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hsin</LastName><ForeName>I-Lun</ForeName><Initials>IL</Initials><AffiliationInfo><Affiliation>Institute of Medical and Molecular Toxicology, Chung Shan Medical University, Taichung, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sheu</LastName><ForeName>Gwo-Tarng</ForeName><Initials>GT</Initials></Author><Author ValidYN="Y"><LastName>Jan</LastName><ForeName>Ming-Shiou</ForeName><Initials>MS</Initials></Author><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Hai-Lun</ForeName><Initials>HL</Initials></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Tzu-Chin</ForeName><Initials>TC</Initials></Author><Author ValidYN="Y"><LastName>Chiu</LastName><ForeName>Ling-Yen</ForeName><Initials>LY</Initials></Author><Author ValidYN="Y"><LastName>Lue</LastName><ForeName>Ko-Huang</ForeName><Initials>KH</Initials></Author><Author ValidYN="Y"><LastName>Ko</LastName><ForeName>Jiunn-Liang</ForeName><Initials>JL</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Br J Pharmacol</MedlineTA><NlmUniqueID>7502536</NlmUniqueID><ISSNLinking>0007-1188</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007155">Immunologic Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018942">Macrolides</NameOfSubstance></Chemical><Chemical><RegistryNumber>886U3H6UFF</RegistryNumber><NameOfSubstance UI="D002738">Chloroquine</NameOfSubstance></Chemical><Chemical><RegistryNumber>88899-55-2</RegistryNumber><NameOfSubstance UI="C040929">bafilomycin A1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.1</RegistryNumber><NameOfSubstance UI="C546842">MTOR protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.1</RegistryNumber><NameOfSubstance UI="D058570">TOR Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D051057">Proto-Oncogene Proteins c-akt</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="C529316">ATP6V0A1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D025262">Vacuolar Proton-Translocating 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