PKCδ regulates force signaling during VEGF/CXCL4 induced dissociation of endothelial tubes.
Identifieur interne : 003164 ( PubMed/Corpus ); précédent : 003163; suivant : 003165PKCδ regulates force signaling during VEGF/CXCL4 induced dissociation of endothelial tubes.
Auteurs : Joshua Jamison ; James H-C Wang ; Alan WellsSource :
- PloS one [ 1932-6203 ] ; 2014.
English descriptors
- KwdEn :
- Cell Movement (drug effects), Cell Movement (physiology), Cells, Cultured, Endothelial Cells (drug effects), Endothelial Cells (metabolism), Endothelium, Vascular (drug effects), Endothelium, Vascular (metabolism), Humans, Indoles (pharmacology), Neovascularization, Physiologic (drug effects), Neovascularization, Physiologic (physiology), Platelet Factor 4 (pharmacology), Protein Kinase C-delta (metabolism), Pyrroles (pharmacology), Vascular Endothelial Growth Factor A (pharmacology), Wound Healing (drug effects), Wound Healing (physiology).
- MESH :
- chemical , metabolism : Protein Kinase C-delta.
- chemical , pharmacology : Indoles, Platelet Factor 4, Pyrroles, Vascular Endothelial Growth Factor A.
- drug effects : Cell Movement, Endothelial Cells, Endothelium, Vascular, Neovascularization, Physiologic, Wound Healing.
- metabolism : Endothelial Cells, Endothelium, Vascular.
- physiology : Cell Movement, Neovascularization, Physiologic, Wound Healing.
- Cells, Cultured, Humans.
Abstract
Wound healing requires the vasculature to re-establish itself from the severed ends; endothelial cells within capillaries must detach from neighboring cells before they can migrate into the nascent wound bed to initiate angiogenesis. The dissociation of these endothelial capillaries is driven partially by platelets' release of growth factors and cytokines, particularly the chemokine CXCL4/platelet factor-4 (PF4) that increases cell-cell de-adherence. As this retraction is partly mediated by increased transcellular contractility, the protein kinase c-δ/myosin light chain-2 (PKCδ/MLC-2) signaling axis becomes a candidate mechanism to drive endothelial dissociation. We hypothesize that PKCδ activation induces contractility through MLC-2 to promote dissociation of endothelial cords after exposure to platelet-released CXCL4 and VEGF. To investigate this mechanism of contractility, endothelial cells were allowed to form cords following CXCL4 addition to perpetuate cord dissociation. In this study, CXCL4-induced dissociation was reduced by a VEGFR inhibitor (sunitinib malate) and/or PKCδ inhibition. During combined CXCL4+VEGF treatment, increased contractility mediated by MLC-2 that is dependent on PKCδ regulation. As cellular force is transmitted to focal adhesions, zyxin, a focal adhesion protein that is mechano-responsive, was upregulated after PKCδ inhibition. This study suggests that growth factor regulation of PKCδ may be involved in CXCL4-mediated dissociation of endothelial cords.
DOI: 10.1371/journal.pone.0093968
PubMed: 24699667
Links to Exploration step
pubmed:24699667Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">PKCδ regulates force signaling during VEGF/CXCL4 induced dissociation of endothelial tubes.</title><author><name sortKey="Jamison, Joshua" sort="Jamison, Joshua" uniqKey="Jamison J" first="Joshua" last="Jamison">Joshua Jamison</name><affiliation><nlm:affiliation>Department of Pathology, McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, James H C" sort="Wang, James H C" uniqKey="Wang J" first="James H-C" last="Wang">James H-C Wang</name><affiliation><nlm:affiliation>Department of Orthopedic Surgery, McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Wells, Alan" sort="Wells, Alan" uniqKey="Wells A" first="Alan" last="Wells">Alan Wells</name><affiliation><nlm:affiliation>Department of Pathology, McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States of America.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:24699667</idno><idno type="pmid">24699667</idno><idno type="doi">10.1371/journal.pone.0093968</idno><idno type="wicri:Area/PubMed/Corpus">003164</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003164</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">PKCδ regulates force signaling during VEGF/CXCL4 induced dissociation of endothelial tubes.</title><author><name sortKey="Jamison, Joshua" sort="Jamison, Joshua" uniqKey="Jamison J" first="Joshua" last="Jamison">Joshua Jamison</name><affiliation><nlm:affiliation>Department of Pathology, McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, James H C" sort="Wang, James H C" uniqKey="Wang J" first="James H-C" last="Wang">James H-C Wang</name><affiliation><nlm:affiliation>Department of Orthopedic Surgery, McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Wells, Alan" sort="Wells, Alan" uniqKey="Wells A" first="Alan" last="Wells">Alan Wells</name><affiliation><nlm:affiliation>Department of Pathology, McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States of America.</nlm:affiliation></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Movement (drug effects)</term><term>Cell Movement (physiology)</term><term>Cells, Cultured</term><term>Endothelial Cells (drug effects)</term><term>Endothelial Cells (metabolism)</term><term>Endothelium, Vascular (drug effects)</term><term>Endothelium, Vascular (metabolism)</term><term>Humans</term><term>Indoles (pharmacology)</term><term>Neovascularization, Physiologic (drug effects)</term><term>Neovascularization, Physiologic (physiology)</term><term>Platelet Factor 4 (pharmacology)</term><term>Protein Kinase C-delta (metabolism)</term><term>Pyrroles (pharmacology)</term><term>Vascular Endothelial Growth Factor A (pharmacology)</term><term>Wound Healing (drug effects)</term><term>Wound Healing (physiology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Protein Kinase C-delta</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Indoles</term><term>Platelet Factor 4</term><term>Pyrroles</term><term>Vascular Endothelial Growth Factor A</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Movement</term><term>Endothelial Cells</term><term>Endothelium, Vascular</term><term>Neovascularization, Physiologic</term><term>Wound Healing</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endothelial Cells</term><term>Endothelium, Vascular</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Cell Movement</term><term>Neovascularization, Physiologic</term><term>Wound Healing</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cells, Cultured</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Wound healing requires the vasculature to re-establish itself from the severed ends; endothelial cells within capillaries must detach from neighboring cells before they can migrate into the nascent wound bed to initiate angiogenesis. The dissociation of these endothelial capillaries is driven partially by platelets' release of growth factors and cytokines, particularly the chemokine CXCL4/platelet factor-4 (PF4) that increases cell-cell de-adherence. As this retraction is partly mediated by increased transcellular contractility, the protein kinase c-δ/myosin light chain-2 (PKCδ/MLC-2) signaling axis becomes a candidate mechanism to drive endothelial dissociation. We hypothesize that PKCδ activation induces contractility through MLC-2 to promote dissociation of endothelial cords after exposure to platelet-released CXCL4 and VEGF. To investigate this mechanism of contractility, endothelial cells were allowed to form cords following CXCL4 addition to perpetuate cord dissociation. In this study, CXCL4-induced dissociation was reduced by a VEGFR inhibitor (sunitinib malate) and/or PKCδ inhibition. During combined CXCL4+VEGF treatment, increased contractility mediated by MLC-2 that is dependent on PKCδ regulation. As cellular force is transmitted to focal adhesions, zyxin, a focal adhesion protein that is mechano-responsive, was upregulated after PKCδ inhibition. This study suggests that growth factor regulation of PKCδ may be involved in CXCL4-mediated dissociation of endothelial cords.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24699667</PMID><DateCreated><Year>2014</Year><Month>04</Month><Day>04</Day></DateCreated><DateCompleted><Year>2015</Year><Month>01</Month><Day>29</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</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>PKCδ regulates force signaling during VEGF/CXCL4 induced dissociation of endothelial tubes.</ArticleTitle><Pagination><MedlinePgn>e93968</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0093968</ELocationID><Abstract><AbstractText>Wound healing requires the vasculature to re-establish itself from the severed ends; endothelial cells within capillaries must detach from neighboring cells before they can migrate into the nascent wound bed to initiate angiogenesis. The dissociation of these endothelial capillaries is driven partially by platelets' release of growth factors and cytokines, particularly the chemokine CXCL4/platelet factor-4 (PF4) that increases cell-cell de-adherence. As this retraction is partly mediated by increased transcellular contractility, the protein kinase c-δ/myosin light chain-2 (PKCδ/MLC-2) signaling axis becomes a candidate mechanism to drive endothelial dissociation. We hypothesize that PKCδ activation induces contractility through MLC-2 to promote dissociation of endothelial cords after exposure to platelet-released CXCL4 and VEGF. To investigate this mechanism of contractility, endothelial cells were allowed to form cords following CXCL4 addition to perpetuate cord dissociation. In this study, CXCL4-induced dissociation was reduced by a VEGFR inhibitor (sunitinib malate) and/or PKCδ inhibition. During combined CXCL4+VEGF treatment, increased contractility mediated by MLC-2 that is dependent on PKCδ regulation. As cellular force is transmitted to focal adhesions, zyxin, a focal adhesion protein that is mechano-responsive, was upregulated after PKCδ inhibition. This study suggests that growth factor regulation of PKCδ may be involved in CXCL4-mediated dissociation of endothelial cords.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jamison</LastName><ForeName>Joshua</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Pathology, McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>James H-C</ForeName><Initials>JH</Initials><AffiliationInfo><Affiliation>Department of Orthopedic Surgery, McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wells</LastName><ForeName>Alan</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Pathology, McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States of America.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AR061395</GrantID><Acronym>AR</Acronym><Agency>NIAMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM063569</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM069668</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32 HL094295</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>04</Month><Day>03</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="D007211">Indoles</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011758">Pyrroles</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D042461">Vascular Endothelial Growth Factor A</NameOfSubstance></Chemical><Chemical><RegistryNumber>37270-94-3</RegistryNumber><NameOfSubstance UI="D010978">Platelet Factor 4</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.13</RegistryNumber><NameOfSubstance UI="D051745">Protein Kinase C-delta</NameOfSubstance></Chemical><Chemical><RegistryNumber>V99T50803M</RegistryNumber><NameOfSubstance UI="C473478">sunitinib</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Circulation. 1999 Nov 2;100(18):1909-16</RefSource><PMID Version="1">10545436</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>PLoS One. 2013;8(10):e77434</RefSource><PMID Version="1">24155954</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Dev Cell. 2001 Dec;1(6):743-7</RefSource><PMID Version="1">11740936</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biochem. 2002 Dec;132(6):831-9</RefSource><PMID Version="1">12473183</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Microsc Res Tech. 2003 Jan 1;60(1):107-14</RefSource><PMID Version="1">12500267</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Am J Physiol Cell Physiol. 2004 Jan;286(1):C105-11</RefSource><PMID 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MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007211" MajorTopicYN="N">Indoles</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018919" MajorTopicYN="N">Neovascularization, Physiologic</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010978" MajorTopicYN="N">Platelet Factor 4</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051745" MajorTopicYN="N">Protein Kinase C-delta</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011758" MajorTopicYN="N">Pyrroles</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D042461" MajorTopicYN="N">Vascular Endothelial Growth Factor A</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014945" MajorTopicYN="N">Wound Healing</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC3974837</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>12</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>03</Month><Day>12</Day></PubMedPubDate><PubMedPubDate 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