Clathrin-dependent endocytosis of claudin-2 by DFYSP peptide causes lysosomal damage in lung adenocarcinoma A549 cells.
Identifieur interne : 000243 ( PubMed/Corpus ); précédent : 000242; suivant : 000244Clathrin-dependent endocytosis of claudin-2 by DFYSP peptide causes lysosomal damage in lung adenocarcinoma A549 cells.
Auteurs : Akira Ikari ; Saeko Taga ; Ryo Watanabe ; Tomonari Sato ; Shun Shimobaba ; Hiroyuki Sonoki ; Satoshi Endo ; Toshiyuki Matsunaga ; Hideki Sakai ; Masahiko Yamaguchi ; Yasuhiro Yamazaki ; Junko SugataniSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2015.
English descriptors
- KwdEn :
- Apoptosis (drug effects), Cell Line, Tumor, Clathrin (metabolism), Claudin-2 (metabolism), Dose-Response Relationship, Drug, Endocytosis (drug effects), Humans, Lung Neoplasms (metabolism), Lung Neoplasms (pathology), Lysosomes (drug effects), Lysosomes (metabolism), Lysosomes (pathology), Peptides (administration & dosage).
- MESH :
- chemical , administration & dosage : Peptides.
- chemical , metabolism : Clathrin, Claudin-2.
- drug effects : Apoptosis, Endocytosis, Lysosomes.
- metabolism : Lung Neoplasms, Lysosomes.
- pathology : Lung Neoplasms, Lysosomes.
- Cell Line, Tumor, Dose-Response Relationship, Drug, Humans.
Abstract
Claudins are tight junctional proteins and comprise a family of over 20 members. Abnormal expression of claudins is reported to be involved in tumor progression. Claudin-2 is highly expressed in lung adenocarcinoma tissues and increases cell proliferation, whereas it is not expressed in normal tissues. Claudin-2-targeting molecules such as peptides and small molecules may be novel anti-cancer drugs. The short peptide with the sequence DFYSP, which mimics the second extracellular loop of claudin-2, decreased claudin-2 content in the cytoplasmic fraction of A549 cells. In contrast, it did not affect the content in the nuclear fraction. The decrease in claudin-2 content was inhibited by chloroquine (CQ), a lysosomal inhibitor, but not by MG-132, a proteasome inhibitor. In the presence of DFYSP peptide and CQ, claudin-2 was co-localized with LAMP-1, a lysosomal marker. The DFYSP peptide-induced decrease in claudin-2 content was inhibited by monodancylcadaverine (MDC), an inhibitor of clathrin-dependent endocytosis. DFYSP peptide increased lysosome content and cathepsin B release, and induced cellular injury, which were inhibited by MDC. Cellular injury induced by DFYSP peptide was inhibited by necrostatin-1, an inhibitor of necrotic cell death, but not by Z-VAD-FMK, an inhibitor of apoptotic cell death. Our data indicate that DFYSP peptide increases the accumulation of the peptide and claudin-2 into the lysosome, resulting in lysosomal damage. Claudin-2 may be a new target for lung cancer therapy.
DOI: 10.1016/j.bbamem.2015.07.003
PubMed: 26163137
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pubmed:26163137Le document en format XML
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Electronic address: ikari@gifu-pu.ac.jp.</nlm:affiliation></affiliation></author><author><name sortKey="Taga, Saeko" sort="Taga, Saeko" uniqKey="Taga S" first="Saeko" last="Taga">Saeko Taga</name><affiliation><nlm:affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Watanabe, Ryo" sort="Watanabe, Ryo" uniqKey="Watanabe R" first="Ryo" last="Watanabe">Ryo Watanabe</name><affiliation><nlm:affiliation>Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Sato, Tomonari" sort="Sato, Tomonari" uniqKey="Sato T" first="Tomonari" last="Sato">Tomonari Sato</name><affiliation><nlm:affiliation>Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Shimobaba, Shun" sort="Shimobaba, Shun" uniqKey="Shimobaba S" first="Shun" last="Shimobaba">Shun Shimobaba</name><affiliation><nlm:affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Sonoki, Hiroyuki" sort="Sonoki, Hiroyuki" uniqKey="Sonoki H" first="Hiroyuki" last="Sonoki">Hiroyuki Sonoki</name><affiliation><nlm:affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Endo, Satoshi" sort="Endo, Satoshi" uniqKey="Endo S" first="Satoshi" last="Endo">Satoshi Endo</name><affiliation><nlm:affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Matsunaga, Toshiyuki" sort="Matsunaga, Toshiyuki" uniqKey="Matsunaga T" first="Toshiyuki" last="Matsunaga">Toshiyuki Matsunaga</name><affiliation><nlm:affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Sakai, Hideki" sort="Sakai, Hideki" uniqKey="Sakai H" first="Hideki" last="Sakai">Hideki Sakai</name><affiliation><nlm:affiliation>Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Yamaguchi, Masahiko" sort="Yamaguchi, Masahiko" uniqKey="Yamaguchi M" first="Masahiko" last="Yamaguchi">Masahiko Yamaguchi</name><affiliation><nlm:affiliation>School of Pharmaceutical Sciences, University of Shizuoka, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Yamazaki, Yasuhiro" sort="Yamazaki, Yasuhiro" uniqKey="Yamazaki Y" first="Yasuhiro" last="Yamazaki">Yasuhiro Yamazaki</name><affiliation><nlm:affiliation>School of Pharmaceutical Sciences, University of Shizuoka, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Sugatani, Junko" sort="Sugatani, Junko" uniqKey="Sugatani J" first="Junko" last="Sugatani">Junko Sugatani</name><affiliation><nlm:affiliation>School of Pharmaceutical Sciences, University of Shizuoka, Japan.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26163137</idno><idno type="pmid">26163137</idno><idno type="doi">10.1016/j.bbamem.2015.07.003</idno><idno type="wicri:Area/PubMed/Corpus">000243</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000243</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Clathrin-dependent endocytosis of claudin-2 by DFYSP peptide causes lysosomal damage in lung adenocarcinoma A549 cells.</title><author><name sortKey="Ikari, Akira" sort="Ikari, Akira" uniqKey="Ikari A" first="Akira" last="Ikari">Akira Ikari</name><affiliation><nlm:affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan. Electronic address: ikari@gifu-pu.ac.jp.</nlm:affiliation></affiliation></author><author><name sortKey="Taga, Saeko" sort="Taga, Saeko" uniqKey="Taga S" first="Saeko" last="Taga">Saeko Taga</name><affiliation><nlm:affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Watanabe, Ryo" sort="Watanabe, Ryo" uniqKey="Watanabe R" first="Ryo" last="Watanabe">Ryo Watanabe</name><affiliation><nlm:affiliation>Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Sato, Tomonari" sort="Sato, Tomonari" uniqKey="Sato T" first="Tomonari" last="Sato">Tomonari Sato</name><affiliation><nlm:affiliation>Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Shimobaba, Shun" sort="Shimobaba, Shun" uniqKey="Shimobaba S" first="Shun" last="Shimobaba">Shun Shimobaba</name><affiliation><nlm:affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Sonoki, Hiroyuki" sort="Sonoki, Hiroyuki" uniqKey="Sonoki H" first="Hiroyuki" last="Sonoki">Hiroyuki Sonoki</name><affiliation><nlm:affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Endo, Satoshi" sort="Endo, Satoshi" uniqKey="Endo S" first="Satoshi" last="Endo">Satoshi Endo</name><affiliation><nlm:affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Matsunaga, Toshiyuki" sort="Matsunaga, Toshiyuki" uniqKey="Matsunaga T" first="Toshiyuki" last="Matsunaga">Toshiyuki Matsunaga</name><affiliation><nlm:affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Sakai, Hideki" sort="Sakai, Hideki" uniqKey="Sakai H" first="Hideki" last="Sakai">Hideki Sakai</name><affiliation><nlm:affiliation>Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Yamaguchi, Masahiko" sort="Yamaguchi, Masahiko" uniqKey="Yamaguchi M" first="Masahiko" last="Yamaguchi">Masahiko Yamaguchi</name><affiliation><nlm:affiliation>School of Pharmaceutical Sciences, University of Shizuoka, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Yamazaki, Yasuhiro" sort="Yamazaki, Yasuhiro" uniqKey="Yamazaki Y" first="Yasuhiro" last="Yamazaki">Yasuhiro Yamazaki</name><affiliation><nlm:affiliation>School of Pharmaceutical Sciences, University of Shizuoka, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Sugatani, Junko" sort="Sugatani, Junko" uniqKey="Sugatani J" first="Junko" last="Sugatani">Junko Sugatani</name><affiliation><nlm:affiliation>School of Pharmaceutical Sciences, University of Shizuoka, Japan.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Apoptosis (drug effects)</term><term>Cell Line, Tumor</term><term>Clathrin (metabolism)</term><term>Claudin-2 (metabolism)</term><term>Dose-Response Relationship, Drug</term><term>Endocytosis (drug effects)</term><term>Humans</term><term>Lung Neoplasms (metabolism)</term><term>Lung Neoplasms (pathology)</term><term>Lysosomes (drug effects)</term><term>Lysosomes (metabolism)</term><term>Lysosomes (pathology)</term><term>Peptides (administration & dosage)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="administration & dosage" xml:lang="en"><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Clathrin</term><term>Claudin-2</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Apoptosis</term><term>Endocytosis</term><term>Lysosomes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Lung Neoplasms</term><term>Lysosomes</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Lung Neoplasms</term><term>Lysosomes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line, Tumor</term><term>Dose-Response Relationship, Drug</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Claudins are tight junctional proteins and comprise a family of over 20 members. Abnormal expression of claudins is reported to be involved in tumor progression. Claudin-2 is highly expressed in lung adenocarcinoma tissues and increases cell proliferation, whereas it is not expressed in normal tissues. Claudin-2-targeting molecules such as peptides and small molecules may be novel anti-cancer drugs. The short peptide with the sequence DFYSP, which mimics the second extracellular loop of claudin-2, decreased claudin-2 content in the cytoplasmic fraction of A549 cells. In contrast, it did not affect the content in the nuclear fraction. The decrease in claudin-2 content was inhibited by chloroquine (CQ), a lysosomal inhibitor, but not by MG-132, a proteasome inhibitor. In the presence of DFYSP peptide and CQ, claudin-2 was co-localized with LAMP-1, a lysosomal marker. The DFYSP peptide-induced decrease in claudin-2 content was inhibited by monodancylcadaverine (MDC), an inhibitor of clathrin-dependent endocytosis. DFYSP peptide increased lysosome content and cathepsin B release, and induced cellular injury, which were inhibited by MDC. Cellular injury induced by DFYSP peptide was inhibited by necrostatin-1, an inhibitor of necrotic cell death, but not by Z-VAD-FMK, an inhibitor of apoptotic cell death. Our data indicate that DFYSP peptide increases the accumulation of the peptide and claudin-2 into the lysosome, resulting in lysosomal damage. Claudin-2 may be a new target for lung cancer therapy.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26163137</PMID><DateCompleted><Year>2015</Year><Month>12</Month><Day>17</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1848</Volume><Issue>10 Pt A</Issue><PubDate><Year>2015</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim. Biophys. Acta</ISOAbbreviation></Journal><ArticleTitle>Clathrin-dependent endocytosis of claudin-2 by DFYSP peptide causes lysosomal damage in lung adenocarcinoma A549 cells.</ArticleTitle><Pagination><MedlinePgn>2326-36</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbamem.2015.07.003</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0005-2736(15)00225-4</ELocationID><Abstract><AbstractText>Claudins are tight junctional proteins and comprise a family of over 20 members. Abnormal expression of claudins is reported to be involved in tumor progression. Claudin-2 is highly expressed in lung adenocarcinoma tissues and increases cell proliferation, whereas it is not expressed in normal tissues. Claudin-2-targeting molecules such as peptides and small molecules may be novel anti-cancer drugs. The short peptide with the sequence DFYSP, which mimics the second extracellular loop of claudin-2, decreased claudin-2 content in the cytoplasmic fraction of A549 cells. In contrast, it did not affect the content in the nuclear fraction. The decrease in claudin-2 content was inhibited by chloroquine (CQ), a lysosomal inhibitor, but not by MG-132, a proteasome inhibitor. In the presence of DFYSP peptide and CQ, claudin-2 was co-localized with LAMP-1, a lysosomal marker. The DFYSP peptide-induced decrease in claudin-2 content was inhibited by monodancylcadaverine (MDC), an inhibitor of clathrin-dependent endocytosis. DFYSP peptide increased lysosome content and cathepsin B release, and induced cellular injury, which were inhibited by MDC. Cellular injury induced by DFYSP peptide was inhibited by necrostatin-1, an inhibitor of necrotic cell death, but not by Z-VAD-FMK, an inhibitor of apoptotic cell death. Our data indicate that DFYSP peptide increases the accumulation of the peptide and claudin-2 into the lysosome, resulting in lysosomal damage. Claudin-2 may be a new target for lung cancer therapy.</AbstractText><CopyrightInformation>Copyright © 2015 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ikari</LastName><ForeName>Akira</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan. Electronic address: ikari@gifu-pu.ac.jp.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Taga</LastName><ForeName>Saeko</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Watanabe</LastName><ForeName>Ryo</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sato</LastName><ForeName>Tomonari</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shimobaba</LastName><ForeName>Shun</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sonoki</LastName><ForeName>Hiroyuki</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Endo</LastName><ForeName>Satoshi</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matsunaga</LastName><ForeName>Toshiyuki</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>The Laboratory of Biochemistry, Department of Biopharmaceutical Sciences, Gifu Pharmaceutical University, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sakai</LastName><ForeName>Hideki</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yamaguchi</LastName><ForeName>Masahiko</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>School of Pharmaceutical Sciences, University of Shizuoka, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yamazaki</LastName><ForeName>Yasuhiro</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>School of Pharmaceutical Sciences, University of Shizuoka, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sugatani</LastName><ForeName>Junko</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>School of Pharmaceutical Sciences, University of Shizuoka, Japan.</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></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>07</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002966">Clathrin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D062446">Claudin-2</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D017209" MajorTopicYN="N">Apoptosis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002966" MajorTopicYN="N">Clathrin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D062446" MajorTopicYN="N">Claudin-2</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004705" MajorTopicYN="N">Endocytosis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008175" MajorTopicYN="N">Lung Neoplasms</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008247" MajorTopicYN="N">Lysosomes</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000008" MajorTopicYN="Y">administration & dosage</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Adenocarcinoma</Keyword><Keyword MajorTopicYN="N">Claudin-2</Keyword><Keyword MajorTopicYN="N">Lung</Keyword><Keyword MajorTopicYN="N">Lysosomal damage</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>03</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>07</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>07</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>7</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>7</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>12</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26163137</ArticleId><ArticleId 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