RapamycinFungusV1, Main, Exploration, bibRecord, 000065

Protein kinase D1 regulates metabolic switch in pancreatic cancer via modulation of mTORC1.

Identifieur interne : 000065 ( Main/Exploration ); précédent : 000064; suivant : 000066

Protein kinase D1 regulates metabolic switch in pancreatic cancer via modulation of mTORC1.

Auteurs : Sonam Kumari [États-Unis] ; Sheema Khan [États-Unis] ; Radhika Sekhri [États-Unis] ; Hassan Mandil [États-Unis] ; Stephen Behrman [États-Unis] ; Murali M. Yallapu [États-Unis] ; Subhash C. Chauhan [États-Unis] ; Meena Jaggi [États-Unis]

Source :

British journal of cancer [ 1532-1827 ] ; 2020.

RBID : pubmed:31819177

Descripteurs français

English descriptors

KwdEn :
- Carcinogenesis (genetics), Carcinoma in Situ (metabolism), Carcinoma in Situ (pathology), Carcinoma, Pancreatic Ductal (metabolism), Carcinoma, Pancreatic Ductal (pathology), Cell Line, Tumor (MeSH), Cell Movement (genetics), Cell Proliferation (genetics), Drug Resistance, Neoplasm (genetics), Gene Knockdown Techniques (MeSH), Glucose (metabolism), Humans (MeSH), Immunohistochemistry (MeSH), Mechanistic Target of Rapamycin Complex 1 (metabolism), Pancreatic Neoplasms (metabolism), Pancreatic Neoplasms (pathology), Pancreatitis, Chronic (metabolism), Pancreatitis, Chronic (pathology), Protein Kinase C (genetics), Protein Kinase C (metabolism), Signal Transduction (genetics), Transfection (MeSH).
MESH :
- chemical , genetics : Protein Kinase C.
- chemical , metabolism : Glucose, Mechanistic Target of Rapamycin Complex 1, Protein Kinase C.
- genetics : Carcinogenesis, Cell Movement, Cell Proliferation, Drug Resistance, Neoplasm, Signal Transduction.
- metabolism : Carcinoma in Situ, Carcinoma, Pancreatic Ductal, Pancreatic Neoplasms, Pancreatitis, Chronic.
- pathology : Carcinoma in Situ, Carcinoma, Pancreatic Ductal, Pancreatic Neoplasms, Pancreatitis, Chronic.
- Cell Line, Tumor, Gene Knockdown Techniques, Humans, Immunohistochemistry, Transfection.

Abstract

BACKGROUND

Protein kinase D1 (PKD1) is a serine-threonine kinase that regulates various functions within the cell. Herein, we report the significance of PKD1 expression in glucose metabolism resulting in pancreatic cancer (PanCa) progression and chemo-resistance.

METHODS

PKD1 expression in PanCa was investigated by using immunohistochemistry. Functional and metabolic assays were utilised to analyse the effect of PKD1 expression/knockdown on associated cellular/molecular changes.

RESULTS

PKD1 expression was detected in human pancreatic intraepithelial neoplasia lesions (MCS = 12.9; P < 0.0001) and pancreatic ductal adenocarcinoma samples (MCS = 15, P < 0.0001) as compared with faint or no expression in normal pancreatic tissues (MCS = 1.54; P < 0.0001). Our results determine that PKD1 enhances glucose metabolism in PanCa cells, by triggering enhanced tumorigenesis and chemo-resistance. We demonstrate that mTORC1 activation by PKD1 regulates metabolic alterations in PanCa cells. siRNA knockdown of Raptor or treatment with rapamycin inhibited PKD1-accelerated lactate production as well as glucose consumption in cells, which confirms the association of mTORC1 with PKD1-induced metabolic alterations.

CONCLUSION

This study suggests a novel role of PKD1 as a key modulator of the glucose metabolism in PanCa cells accelerating tumorigenesis and chemo-resistance. The remodelling of PKD1-dysregulated glucose metabolism can be achieved by regulation of mTORC1 for development of novel therapeutic strategies.

DOI: 10.1038/s41416-019-0629-9
PubMed: 31819177
PubMed Central: PMC6964700

Affiliations:

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Le document en format XML

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<series><title level="j">British journal of cancer</title>
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<term>Carcinoma in Situ (metabolism)</term>
<term>Carcinoma in Situ (pathology)</term>
<term>Carcinoma, Pancreatic Ductal (metabolism)</term>
<term>Carcinoma, Pancreatic Ductal (pathology)</term>
<term>Cell Line, Tumor (MeSH)</term>
<term>Cell Movement (genetics)</term>
<term>Cell Proliferation (genetics)</term>
<term>Drug Resistance, Neoplasm (genetics)</term>
<term>Gene Knockdown Techniques (MeSH)</term>
<term>Glucose (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Immunohistochemistry (MeSH)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term>
<term>Pancreatic Neoplasms (metabolism)</term>
<term>Pancreatic Neoplasms (pathology)</term>
<term>Pancreatitis, Chronic (metabolism)</term>
<term>Pancreatitis, Chronic (pathology)</term>
<term>Protein Kinase C (genetics)</term>
<term>Protein Kinase C (metabolism)</term>
<term>Signal Transduction (genetics)</term>
<term>Transfection (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Carcinogenèse (génétique)</term>
<term>Carcinome du canal pancréatique (anatomopathologie)</term>
<term>Carcinome du canal pancréatique (métabolisme)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Glucose (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Immunohistochimie (MeSH)</term>
<term>Lignée cellulaire tumorale (MeSH)</term>
<term>Mouvement cellulaire (génétique)</term>
<term>Pancréatite chronique (anatomopathologie)</term>
<term>Pancréatite chronique (métabolisme)</term>
<term>Prolifération cellulaire (génétique)</term>
<term>Protéine kinase C (génétique)</term>
<term>Protéine kinase C (métabolisme)</term>
<term>Résistance aux médicaments antinéoplasiques (génétique)</term>
<term>Techniques de knock-down de gènes (MeSH)</term>
<term>Transduction du signal (génétique)</term>
<term>Transfection (MeSH)</term>
<term>Tumeurs du pancréas (anatomopathologie)</term>
<term>Tumeurs du pancréas (métabolisme)</term>
<term>Épithélioma in situ (anatomopathologie)</term>
<term>Épithélioma in situ (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Protein Kinase C</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glucose</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Protein Kinase C</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Carcinome du canal pancréatique</term>
<term>Pancréatite chronique</term>
<term>Tumeurs du pancréas</term>
<term>Épithélioma in situ</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Carcinogenesis</term>
<term>Cell Movement</term>
<term>Cell Proliferation</term>
<term>Drug Resistance, Neoplasm</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Carcinogenèse</term>
<term>Mouvement cellulaire</term>
<term>Prolifération cellulaire</term>
<term>Protéine kinase C</term>
<term>Résistance aux médicaments antinéoplasiques</term>
<term>Transduction du signal</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Carcinoma in Situ</term>
<term>Carcinoma, Pancreatic Ductal</term>
<term>Pancreatic Neoplasms</term>
<term>Pancreatitis, Chronic</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carcinome du canal pancréatique</term>
<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Glucose</term>
<term>Pancréatite chronique</term>
<term>Protéine kinase C</term>
<term>Tumeurs du pancréas</term>
<term>Épithélioma in situ</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Carcinoma in Situ</term>
<term>Carcinoma, Pancreatic Ductal</term>
<term>Pancreatic Neoplasms</term>
<term>Pancreatitis, Chronic</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Cell Line, Tumor</term>
<term>Gene Knockdown Techniques</term>
<term>Humans</term>
<term>Immunohistochemistry</term>
<term>Transfection</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Humains</term>
<term>Immunohistochimie</term>
<term>Lignée cellulaire tumorale</term>
<term>Techniques de knock-down de gènes</term>
<term>Transfection</term>
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<front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b>
</p>
<p>Protein kinase D1 (PKD1) is a serine-threonine kinase that regulates various functions within the cell. Herein, we report the significance of PKD1 expression in glucose metabolism resulting in pancreatic cancer (PanCa) progression and chemo-resistance.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>METHODS</b>
</p>
<p>PKD1 expression in PanCa was investigated by using immunohistochemistry. Functional and metabolic assays were utilised to analyse the effect of PKD1 expression/knockdown on associated cellular/molecular changes.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>RESULTS</b>
</p>
<p>PKD1 expression was detected in human pancreatic intraepithelial neoplasia lesions (MCS = 12.9; P < 0.0001) and pancreatic ductal adenocarcinoma samples (MCS = 15, P < 0.0001) as compared with faint or no expression in normal pancreatic tissues (MCS = 1.54; P < 0.0001). Our results determine that PKD1 enhances glucose metabolism in PanCa cells, by triggering enhanced tumorigenesis and chemo-resistance. We demonstrate that mTORC1 activation by PKD1 regulates metabolic alterations in PanCa cells. siRNA knockdown of Raptor or treatment with rapamycin inhibited PKD1-accelerated lactate production as well as glucose consumption in cells, which confirms the association of mTORC1 with PKD1-induced metabolic alterations.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>CONCLUSION</b>
</p>
<p>This study suggests a novel role of PKD1 as a key modulator of the glucose metabolism in PanCa cells accelerating tumorigenesis and chemo-resistance. The remodelling of PKD1-dysregulated glucose metabolism can be achieved by regulation of mTORC1 for development of novel therapeutic strategies.</p>
</div>
</front>
</TEI>
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<DateCompleted><Year>2020</Year>
<Month>07</Month>
<Day>21</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>07</Month>
<Day>21</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1532-1827</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>122</Volume>
<Issue>1</Issue>
<PubDate><Year>2020</Year>
<Month>01</Month>
</PubDate>
</JournalIssue>
<Title>British journal of cancer</Title>
<ISOAbbreviation>Br J Cancer</ISOAbbreviation>
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<ArticleTitle>Protein kinase D1 regulates metabolic switch in pancreatic cancer via modulation of mTORC1.</ArticleTitle>
<Pagination><MedlinePgn>121-131</MedlinePgn>
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<ELocationID EIdType="doi" ValidYN="Y">10.1038/s41416-019-0629-9</ELocationID>
<Abstract><AbstractText Label="BACKGROUND">Protein kinase D1 (PKD1) is a serine-threonine kinase that regulates various functions within the cell. Herein, we report the significance of PKD1 expression in glucose metabolism resulting in pancreatic cancer (PanCa) progression and chemo-resistance.</AbstractText>
<AbstractText Label="METHODS">PKD1 expression in PanCa was investigated by using immunohistochemistry. Functional and metabolic assays were utilised to analyse the effect of PKD1 expression/knockdown on associated cellular/molecular changes.</AbstractText>
<AbstractText Label="RESULTS">PKD1 expression was detected in human pancreatic intraepithelial neoplasia lesions (MCS = 12.9; P < 0.0001) and pancreatic ductal adenocarcinoma samples (MCS = 15, P < 0.0001) as compared with faint or no expression in normal pancreatic tissues (MCS = 1.54; P < 0.0001). Our results determine that PKD1 enhances glucose metabolism in PanCa cells, by triggering enhanced tumorigenesis and chemo-resistance. We demonstrate that mTORC1 activation by PKD1 regulates metabolic alterations in PanCa cells. siRNA knockdown of Raptor or treatment with rapamycin inhibited PKD1-accelerated lactate production as well as glucose consumption in cells, which confirms the association of mTORC1 with PKD1-induced metabolic alterations.</AbstractText>
<AbstractText Label="CONCLUSION">This study suggests a novel role of PKD1 as a key modulator of the glucose metabolism in PanCa cells accelerating tumorigenesis and chemo-resistance. The remodelling of PKD1-dysregulated glucose metabolism can be achieved by regulation of mTORC1 for development of novel therapeutic strategies.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kumari</LastName>
<ForeName>Sonam</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences and Center for Cancer Research, University of Tennessee Health Science Center, Memphis, TN, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Khan</LastName>
<ForeName>Sheema</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences and Center for Cancer Research, University of Tennessee Health Science Center, Memphis, TN, USA. sheema.khan@utrgv.edu.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Immunology and Microbiology, University of Texas Rio Grande Valley, McAllen, TX, USA. sheema.khan@utrgv.edu.</Affiliation>
</AffiliationInfo>
</Author>
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<ForeName>Radhika</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>Department of Pathology, University of Tennessee Health Science Center, Memphis, TN, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Mandil</LastName>
<ForeName>Hassan</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences and Center for Cancer Research, University of Tennessee Health Science Center, Memphis, TN, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Behrman</LastName>
<ForeName>Stephen</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Surgery, University of Tennessee Health Science Center, Memphis, TN, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yallapu</LastName>
<ForeName>Murali M</ForeName>
<Initials>MM</Initials>
<AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences and Center for Cancer Research, University of Tennessee Health Science Center, Memphis, TN, USA.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Immunology and Microbiology, University of Texas Rio Grande Valley, McAllen, TX, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chauhan</LastName>
<ForeName>Subhash C</ForeName>
<Initials>SC</Initials>
<AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences and Center for Cancer Research, University of Tennessee Health Science Center, Memphis, TN, USA.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Immunology and Microbiology, University of Texas Rio Grande Valley, McAllen, TX, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jaggi</LastName>
<ForeName>Meena</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences and Center for Cancer Research, University of Tennessee Health Science Center, Memphis, TN, USA. Meena.Jaggi@utrgv.edu.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Immunology and Microbiology, University of Texas Rio Grande Valley, McAllen, TX, USA. Meena.Jaggi@utrgv.edu.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R01 CA204552</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 CA210192</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 CA206069</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
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<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2019</Year>
<Month>12</Month>
<Day>10</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Br J Cancer</MedlineTA>
<NlmUniqueID>0370635</NlmUniqueID>
<ISSNLinking>0007-0920</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>EC 2.7.10.-</RegistryNumber>
<NameOfSubstance UI="C089212">protein kinase D</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D000076222">Mechanistic Target of Rapamycin Complex 1</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.13</RegistryNumber>
<NameOfSubstance UI="D011493">Protein Kinase C</NameOfSubstance>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D063646" MajorTopicYN="N">Carcinogenesis</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002278" MajorTopicYN="N">Carcinoma in Situ</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002465" MajorTopicYN="N">Cell Movement</DescriptorName>
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</MeshHeading>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
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<MeshHeading><DescriptorName UI="D014162" MajorTopicYN="N">Transfection</DescriptorName>
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<affiliations><list><country><li>États-Unis</li>
</country>
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<li>Texas</li>
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	Serveur d'exploration sur la rapamycine et les champignons
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Serveur d'exploration sur la rapamycine et les champignons

Protein kinase D1 regulates metabolic switch in pancreatic cancer via modulation of mTORC1.

Protein kinase D1 regulates metabolic switch in pancreatic cancer via modulation of mTORC1.

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