Niemann-Pick disease type C2 protein induces autophagy and inhibits growth in FM3A breast cancer cells.
Identifieur interne : 000C58 ( Main/Exploration ); précédent : 000C57; suivant : 000C59Niemann-Pick disease type C2 protein induces autophagy and inhibits growth in FM3A breast cancer cells.
Auteurs : Tatsuo Adachi [Japon] ; Yasuhiko Matsumoto ; Yoshinori Inagaki ; Kazuhisa SekimizuSource :
- Drug discoveries & therapeutics [ 1881-7831 ] ; 2015.
Descripteurs français
- KwdFr :
- AMP-Activated Protein Kinases (métabolisme), Animaux (MeSH), Autophagie (effets des médicaments et des substances chimiques), Femelle (MeSH), Hémolymphe (physiologie), Lignée cellulaire tumorale (MeSH), Prolifération cellulaire (effets des médicaments et des substances chimiques), Protéines du transport vésiculaire (pharmacologie), Souris (MeSH), Tumeurs du sein (anatomopathologie), Tumeurs du sein (traitement médicamenteux).
- MESH :
- anatomopathologie : Tumeurs du sein.
- effets des médicaments et des substances chimiques : Autophagie, Prolifération cellulaire.
- métabolisme : AMP-Activated Protein Kinases.
- pharmacologie : Protéines du transport vésiculaire.
- physiologie : Hémolymphe.
- traitement médicamenteux : Tumeurs du sein.
- Animaux, Femelle, Lignée cellulaire tumorale, Souris.
English descriptors
- KwdEn :
- AMP-Activated Protein Kinases (metabolism), Animals (MeSH), Autophagy (drug effects), Breast Neoplasms (drug therapy), Breast Neoplasms (pathology), Cell Line, Tumor (MeSH), Cell Proliferation (drug effects), Female (MeSH), Hemolymph (physiology), Mice (MeSH), Vesicular Transport Proteins (pharmacology).
- MESH :
- chemical , metabolism : AMP-Activated Protein Kinases.
- drug effects : Autophagy, Cell Proliferation.
- drug therapy : Breast Neoplasms.
- pathology : Breast Neoplasms.
- chemical , pharmacology : Vesicular Transport Proteins.
- physiology : Hemolymph.
- Animals, Cell Line, Tumor, Female, Mice.
Abstract
Some peptides that are highly conserved between insects and mammals have anti-tumor action. Screening for inhibitors of cell growth from animal fluids may provide useful clues to anti-tumor drugs. Inducers of autophagy also have anti-tumor activity. The current authors recently studied a protein found in silkworm hemolymph, Niemann-Pick disease type C2 (NPC2). This protein, which is highly conserved among eukaryotes, was found to have anti-proliferative action on a silkworm cell line. The current study found that the silkworm NPC2 protein also inhibits the growth of FM3A murine breast cancer cells. In FM3A cells, silkworm NPC2 increased phosphorylation of AMP-activated protein kinase and decreased phosphorylation of Akt and mammalian target of rapamycin, which are regulators of autophagy. This study also found that NPC2 increased the amount of microtubule-associated protein light chain 3 (LC3)-II, an autophagosome marker, in FM3A cells. Silkworm NPC2 also induced an increase in the number of LC3-dots, a marker of pre-autophagic endosomes, in FM3A cells. When silkworm NPC2 was used to inhibit FM3A cell growth, that inhibition was attenuated by chloroquine, which inhibits autophagic activity by preventing lysosomal acidification. Murine NPC2 also inhibited growth and induced autophagy in FM3A cells. These findings suggest that NPC2 is involved in the induction and/or maintenance of autophagy and may help to elucidate the mechanisms underlying other neurodegenerative disorders such as Niemann-Pick disease.
DOI: 10.5582/ddt.2015.01014
PubMed: 25843701
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Inagaki</name></author><author><name sortKey="Sekimizu, Kazuhisa" sort="Sekimizu, Kazuhisa" uniqKey="Sekimizu K" first="Kazuhisa" last="Sekimizu">Kazuhisa Sekimizu</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:25843701</idno><idno type="pmid">25843701</idno><idno type="doi">10.5582/ddt.2015.01014</idno><idno type="wicri:Area/Main/Corpus">000C81</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C81</idno><idno type="wicri:Area/Main/Curation">000C81</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C81</idno><idno type="wicri:Area/Main/Exploration">000C81</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Niemann-Pick disease type C2 protein induces autophagy and inhibits growth in FM3A breast cancer cells.</title><author><name sortKey="Adachi, Tatsuo" sort="Adachi, Tatsuo" uniqKey="Adachi T" first="Tatsuo" last="Adachi">Tatsuo Adachi</name><affiliation wicri:level="4"><nlm:affiliation>Laboratory of Microbiology, Graduate School of Pharmaceutical Sciences, The University of Tokyo.</nlm:affiliation><country>Japon</country><placeName><settlement type="city">Tokyo</settlement><region type="province">Région de Kantō</region></placeName><orgName type="university">Université de Tokyo</orgName></affiliation></author><author><name sortKey="Matsumoto, Yasuhiko" sort="Matsumoto, Yasuhiko" uniqKey="Matsumoto Y" first="Yasuhiko" last="Matsumoto">Yasuhiko Matsumoto</name></author><author><name sortKey="Inagaki, Yoshinori" sort="Inagaki, Yoshinori" uniqKey="Inagaki Y" first="Yoshinori" last="Inagaki">Yoshinori Inagaki</name></author><author><name sortKey="Sekimizu, Kazuhisa" sort="Sekimizu, Kazuhisa" uniqKey="Sekimizu K" first="Kazuhisa" last="Sekimizu">Kazuhisa Sekimizu</name></author></analytic><series><title level="j">Drug discoveries & therapeutics</title><idno type="ISSN">1881-7831</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>AMP-Activated Protein Kinases (metabolism)</term><term>Animals (MeSH)</term><term>Autophagy (drug effects)</term><term>Breast Neoplasms (drug therapy)</term><term>Breast Neoplasms (pathology)</term><term>Cell Line, Tumor (MeSH)</term><term>Cell Proliferation (drug effects)</term><term>Female (MeSH)</term><term>Hemolymph (physiology)</term><term>Mice (MeSH)</term><term>Vesicular Transport Proteins (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>AMP-Activated Protein Kinases (métabolisme)</term><term>Animaux (MeSH)</term><term>Autophagie (effets des médicaments et des substances chimiques)</term><term>Femelle (MeSH)</term><term>Hémolymphe (physiologie)</term><term>Lignée cellulaire tumorale (MeSH)</term><term>Prolifération cellulaire (effets des médicaments et des substances chimiques)</term><term>Protéines du transport vésiculaire (pharmacologie)</term><term>Souris (MeSH)</term><term>Tumeurs du sein (anatomopathologie)</term><term>Tumeurs du sein (traitement médicamenteux)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>AMP-Activated Protein Kinases</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Tumeurs du sein</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Autophagy</term><term>Cell Proliferation</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Breast Neoplasms</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Autophagie</term><term>Prolifération cellulaire</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>AMP-Activated Protein Kinases</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Breast Neoplasms</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Protéines du transport vésiculaire</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Vesicular Transport Proteins</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Hémolymphe</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Hemolymph</term></keywords><keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Tumeurs du sein</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line, Tumor</term><term>Female</term><term>Mice</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Femelle</term><term>Lignée cellulaire tumorale</term><term>Souris</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Some peptides that are highly conserved between insects and mammals have anti-tumor action. Screening for inhibitors of cell growth from animal fluids may provide useful clues to anti-tumor drugs. Inducers of autophagy also have anti-tumor activity. The current authors recently studied a protein found in silkworm hemolymph, Niemann-Pick disease type C2 (NPC2). This protein, which is highly conserved among eukaryotes, was found to have anti-proliferative action on a silkworm cell line. The current study found that the silkworm NPC2 protein also inhibits the growth of FM3A murine breast cancer cells. In FM3A cells, silkworm NPC2 increased phosphorylation of AMP-activated protein kinase and decreased phosphorylation of Akt and mammalian target of rapamycin, which are regulators of autophagy. This study also found that NPC2 increased the amount of microtubule-associated protein light chain 3 (LC3)-II, an autophagosome marker, in FM3A cells. Silkworm NPC2 also induced an increase in the number of LC3-dots, a marker of pre-autophagic endosomes, in FM3A cells. When silkworm NPC2 was used to inhibit FM3A cell growth, that inhibition was attenuated by chloroquine, which inhibits autophagic activity by preventing lysosomal acidification. Murine NPC2 also inhibited growth and induced autophagy in FM3A cells. These findings suggest that NPC2 is involved in the induction and/or maintenance of autophagy and may help to elucidate the mechanisms underlying other neurodegenerative disorders such as Niemann-Pick disease.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25843701</PMID><DateCompleted><Year>2016</Year><Month>03</Month><Day>07</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1881-7831</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>4</Issue><PubDate><Year>2015</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Drug discoveries & therapeutics</Title><ISOAbbreviation>Drug Discov Ther</ISOAbbreviation></Journal><ArticleTitle>Niemann-Pick disease type C2 protein induces autophagy and inhibits growth in FM3A breast cancer cells.</ArticleTitle><Pagination><MedlinePgn>282-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.5582/ddt.2015.01014</ELocationID><Abstract><AbstractText>Some peptides that are highly conserved between insects and mammals have anti-tumor action. Screening for inhibitors of cell growth from animal fluids may provide useful clues to anti-tumor drugs. Inducers of autophagy also have anti-tumor activity. The current authors recently studied a protein found in silkworm hemolymph, Niemann-Pick disease type C2 (NPC2). This protein, which is highly conserved among eukaryotes, was found to have anti-proliferative action on a silkworm cell line. The current study found that the silkworm NPC2 protein also inhibits the growth of FM3A murine breast cancer cells. In FM3A cells, silkworm NPC2 increased phosphorylation of AMP-activated protein kinase and decreased phosphorylation of Akt and mammalian target of rapamycin, which are regulators of autophagy. This study also found that NPC2 increased the amount of microtubule-associated protein light chain 3 (LC3)-II, an autophagosome marker, in FM3A cells. Silkworm NPC2 also induced an increase in the number of LC3-dots, a marker of pre-autophagic endosomes, in FM3A cells. When silkworm NPC2 was used to inhibit FM3A cell growth, that inhibition was attenuated by chloroquine, which inhibits autophagic activity by preventing lysosomal acidification. Murine NPC2 also inhibited growth and induced autophagy in FM3A cells. These findings suggest that NPC2 is involved in the induction and/or maintenance of autophagy and may help to elucidate the mechanisms underlying other neurodegenerative disorders such as Niemann-Pick disease.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Adachi</LastName><ForeName>Tatsuo</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Laboratory of Microbiology, Graduate School of Pharmaceutical Sciences, The University of Tokyo.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matsumoto</LastName><ForeName>Yasuhiko</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Inagaki</LastName><ForeName>Yoshinori</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Sekimizu</LastName><ForeName>Kazuhisa</ForeName><Initials>K</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><ArticleDate DateType="Electronic"><Year>2015</Year><Month>04</Month><Day>06</Day></ArticleDate></Article><MedlineJournalInfo><Country>Japan</Country><MedlineTA>Drug Discov Ther</MedlineTA><NlmUniqueID>101493809</NlmUniqueID><ISSNLinking>1881-7831</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C497045">Npc2 protein, mouse</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D033921">Vesicular Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.31</RegistryNumber><NameOfSubstance UI="D055372">AMP-Activated Protein Kinases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D055372" MajorTopicYN="N">AMP-Activated Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="N">Autophagy</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001943" MajorTopicYN="N">Breast Neoplasms</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="Y">drug therapy</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D049109" MajorTopicYN="N">Cell Proliferation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006458" MajorTopicYN="N">Hemolymph</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D033921" MajorTopicYN="N">Vesicular Transport Proteins</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>4</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>4</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>3</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25843701</ArticleId><ArticleId IdType="doi">10.5582/ddt.2015.01014</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><noCountry><name sortKey="Inagaki, Yoshinori" sort="Inagaki, Yoshinori" uniqKey="Inagaki Y" first="Yoshinori" last="Inagaki">Yoshinori Inagaki</name><name sortKey="Matsumoto, Yasuhiko" sort="Matsumoto, Yasuhiko" uniqKey="Matsumoto Y" first="Yasuhiko" last="Matsumoto">Yasuhiko Matsumoto</name><name sortKey="Sekimizu, Kazuhisa" sort="Sekimizu, Kazuhisa" uniqKey="Sekimizu K" first="Kazuhisa" last="Sekimizu">Kazuhisa Sekimizu</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Adachi, Tatsuo" sort="Adachi, Tatsuo" uniqKey="Adachi T" first="Tatsuo" last="Adachi">Tatsuo Adachi</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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