IPF fibroblasts are desensitized to type I collagen matrix-induced cell death by suppressing low autophagy via aberrant Akt/mTOR kinases.
Identifieur interne : 000247 ( Ncbi/Merge ); précédent : 000246; suivant : 000248IPF fibroblasts are desensitized to type I collagen matrix-induced cell death by suppressing low autophagy via aberrant Akt/mTOR kinases.
Auteurs : Richard Seonghun Nho [États-Unis] ; Polla Hergert [États-Unis]Source :
- PloS one [ 1932-6203 ] ; 2014.
Descripteurs français
- KwdFr :
- Activation enzymatique, Adénine (analogues et dérivés), Adénine (pharmacologie), Autophagie (), Chloroquine (pharmacologie), Collagène de type I (), Collagène de type I (métabolisme), Fibroblastes (métabolisme), Fibrose pulmonaire idiopathique (métabolisme), Humains, Lignée cellulaire, Multimérisation de protéines, Phagosomes (métabolisme), Prolifération cellulaire, Protéines proto-oncogènes c-akt (métabolisme), Survie cellulaire, Sérine-thréonine kinases TOR (métabolisme).
- MESH :
- analogues et dérivés : Adénine.
- métabolisme : Collagène de type I, Fibroblastes, Fibrose pulmonaire idiopathique, Phagosomes, Protéines proto-oncogènes c-akt, Sérine-thréonine kinases TOR.
- pharmacologie : Adénine, Chloroquine.
- Activation enzymatique, Autophagie, Collagène de type I, Humains, Lignée cellulaire, Multimérisation de protéines, Prolifération cellulaire, Survie cellulaire.
English descriptors
- KwdEn :
- Adenine (analogs & derivatives), Adenine (pharmacology), Autophagy (drug effects), Cell Line, Cell Proliferation, Cell Survival, Chloroquine (pharmacology), Collagen Type I (chemistry), Collagen Type I (metabolism), Enzyme Activation, Fibroblasts (metabolism), Humans, Idiopathic Pulmonary Fibrosis (metabolism), Phagosomes (metabolism), Protein Multimerization, Proto-Oncogene Proteins c-akt (metabolism), TOR Serine-Threonine Kinases (metabolism).
- MESH :
- chemical , analogs & derivatives : Adenine.
- chemical , chemistry : Collagen Type I.
- chemical , metabolism : Collagen Type I, Proto-Oncogene Proteins c-akt, TOR Serine-Threonine Kinases.
- chemical , pharmacology : Adenine, Chloroquine.
- drug effects : Autophagy.
- metabolism : Fibroblasts, Idiopathic Pulmonary Fibrosis, Phagosomes.
- Cell Line, Cell Proliferation, Cell Survival, Enzyme Activation, Humans, Protein Multimerization.
Abstract
Idiopathic pulmonary fibrosis (IPF) is a chronic, lethal interstitial lung disease in which the aberrant PTEN/Akt axis plays a major role in conferring a survival phenotype in response to the cell death inducing properties of type I collagen matrix. The underlying mechanism by which IPF fibroblasts become desensitized to polymerized collagen, thereby eluding collagen matrix-induced cell death has not been fully elucidated. We hypothesized that the pathologically altered PTEN/Akt axis suppresses autophagy via high mTOR kinase activity, which subsequently desensitizes IPF fibroblasts to collagen matrix induced cell death. We found that the autophagosome marker LC3-2 expression is suppressed, while mTOR activity remains high when IPF fibroblasts are cultured on collagen. However, LC3-2 expression increased in response to IPF fibroblast attachment to collagen in the presence of rapamycin. In addition, PTEN over-expression or Akt inhibition suppressed mTOR activity, thereby increasing LC3-2 expression in IPF fibroblasts. Furthermore, the treatment of IPF fibroblasts over-expressing PTEN or dominant negative Akt with autophagy inhibitors increased IPF fibroblast cell death. Enhanced p-mTOR expression along with low LC3-2 expression was also found in myofibroblasts within the fibroblastic foci from IPF patients. Our data show that the aberrant PTEN/Akt/mTOR axis desensitizes IPF fibroblasts from polymerized collagen driven stress by suppressing autophagic activity, which produces a viable IPF fibroblast phenotype on collagen. This suggests that the aberrantly regulated autophagic pathway may play an important role in maintaining a pathological IPF fibroblast phenotype in response to collagen rich environment.
DOI: 10.1371/journal.pone.0094616
PubMed: 24728102
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(metabolism)</term><term>Humans</term><term>Idiopathic Pulmonary Fibrosis (metabolism)</term><term>Phagosomes (metabolism)</term><term>Protein Multimerization</term><term>Proto-Oncogene Proteins c-akt (metabolism)</term><term>TOR Serine-Threonine Kinases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique</term><term>Adénine (analogues et dérivés)</term><term>Adénine (pharmacologie)</term><term>Autophagie ()</term><term>Chloroquine (pharmacologie)</term><term>Collagène de type I ()</term><term>Collagène de type I (métabolisme)</term><term>Fibroblastes (métabolisme)</term><term>Fibrose pulmonaire idiopathique (métabolisme)</term><term>Humains</term><term>Lignée cellulaire</term><term>Multimérisation de protéines</term><term>Phagosomes (métabolisme)</term><term>Prolifération cellulaire</term><term>Protéines proto-oncogènes c-akt (métabolisme)</term><term>Survie cellulaire</term><term>Sérine-thréonine kinases TOR (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Adenine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Collagen Type I</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Collagen Type I</term><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>Adenine</term><term>Chloroquine</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Adénine</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Autophagy</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fibroblasts</term><term>Idiopathic Pulmonary Fibrosis</term><term>Phagosomes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Collagène de type I</term><term>Fibroblastes</term><term>Fibrose pulmonaire idiopathique</term><term>Phagosomes</term><term>Protéines proto-oncogènes c-akt</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Adénine</term><term>Chloroquine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Cell Proliferation</term><term>Cell Survival</term><term>Enzyme Activation</term><term>Humans</term><term>Protein Multimerization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term><term>Autophagie</term><term>Collagène de type I</term><term>Humains</term><term>Lignée cellulaire</term><term>Multimérisation de protéines</term><term>Prolifération cellulaire</term><term>Survie cellulaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Idiopathic pulmonary fibrosis (IPF) is a chronic, lethal interstitial lung disease in which the aberrant PTEN/Akt axis plays a major role in conferring a survival phenotype in response to the cell death inducing properties of type I collagen matrix. The underlying mechanism by which IPF fibroblasts become desensitized to polymerized collagen, thereby eluding collagen matrix-induced cell death has not been fully elucidated. We hypothesized that the pathologically altered PTEN/Akt axis suppresses autophagy via high mTOR kinase activity, which subsequently desensitizes IPF fibroblasts to collagen matrix induced cell death. We found that the autophagosome marker LC3-2 expression is suppressed, while mTOR activity remains high when IPF fibroblasts are cultured on collagen. However, LC3-2 expression increased in response to IPF fibroblast attachment to collagen in the presence of rapamycin. In addition, PTEN over-expression or Akt inhibition suppressed mTOR activity, thereby increasing LC3-2 expression in IPF fibroblasts. Furthermore, the treatment of IPF fibroblasts over-expressing PTEN or dominant negative Akt with autophagy inhibitors increased IPF fibroblast cell death. Enhanced p-mTOR expression along with low LC3-2 expression was also found in myofibroblasts within the fibroblastic foci from IPF patients. Our data show that the aberrant PTEN/Akt/mTOR axis desensitizes IPF fibroblasts from polymerized collagen driven stress by suppressing autophagic activity, which produces a viable IPF fibroblast phenotype on collagen. This suggests that the aberrantly regulated autophagic pathway may play an important role in maintaining a pathological IPF fibroblast phenotype in response to collagen rich environment. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24728102</PMID><DateCompleted><Year>2015</Year><Month>05</Month><Day>29</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>4</Issue><PubDate><Year>2014</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>IPF fibroblasts are desensitized to type I collagen matrix-induced cell death by suppressing low autophagy via aberrant Akt/mTOR kinases.</ArticleTitle><Pagination><MedlinePgn>e94616</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0094616</ELocationID><Abstract><AbstractText>Idiopathic pulmonary fibrosis (IPF) is a chronic, lethal interstitial lung disease in which the aberrant PTEN/Akt axis plays a major role in conferring a survival phenotype in response to the cell death inducing properties of type I collagen matrix. The underlying mechanism by which IPF fibroblasts become desensitized to polymerized collagen, thereby eluding collagen matrix-induced cell death has not been fully elucidated. We hypothesized that the pathologically altered PTEN/Akt axis suppresses autophagy via high mTOR kinase activity, which subsequently desensitizes IPF fibroblasts to collagen matrix induced cell death. We found that the autophagosome marker LC3-2 expression is suppressed, while mTOR activity remains high when IPF fibroblasts are cultured on collagen. However, LC3-2 expression increased in response to IPF fibroblast attachment to collagen in the presence of rapamycin. In addition, PTEN over-expression or Akt inhibition suppressed mTOR activity, thereby increasing LC3-2 expression in IPF fibroblasts. Furthermore, the treatment of IPF fibroblasts over-expressing PTEN or dominant negative Akt with autophagy inhibitors increased IPF fibroblast cell death. Enhanced p-mTOR expression along with low LC3-2 expression was also found in myofibroblasts within the fibroblastic foci from IPF patients. Our data show that the aberrant PTEN/Akt/mTOR axis desensitizes IPF fibroblasts from polymerized collagen driven stress by suppressing autophagic activity, which produces a viable IPF fibroblast phenotype on collagen. This suggests that the aberrantly regulated autophagic pathway may play an important role in maintaining a pathological IPF fibroblast phenotype in response to collagen rich environment. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nho</LastName><ForeName>Richard Seonghun</ForeName><Initials>RS</Initials><AffiliationInfo><Affiliation>Department of Medicine, University of Minnesota, Minneapolis, Minnesota, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hergert</LastName><ForeName>Polla</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Medicine, University of Minnesota, Minneapolis, Minnesota, United States of America.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 HL114662</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL114662-01A</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><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>2014</Year><Month>04</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024042">Collagen Type I</NameOfSubstance></Chemical><Chemical><RegistryNumber>5142-23-4</RegistryNumber><NameOfSubstance 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