Golgi-independent routes support protein disulfide isomerase externalization in vascular smooth muscle cells

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dc.contributorSistema FMUSP-HC: Faculdade de Medicina da Universidade de São Paulo (FMUSP) e Hospital das Clínicas da FMUSP
dc.contributor.authorARAUJO, Thais L. S.
dc.contributor.authorFERNANDES, Carolina G.
dc.contributor.authorLAURINDO, Francisco R. M.
dc.date.accessioned2017-08-17T19:22:17Z
dc.date.available2017-08-17T19:22:17Z
dc.date.issued2017
dc.description.abstractExtracellular pools of intracellular molecular chaperones are increasingly evident. The peri/epicellular(pec) pool of the endoplasmic reticulum redox chaperone protein disulfide isomerase-A1(PDI) is involved in thrombosis and vascular remodeling, while PDI externalization routes remain elusive. In endothelial cells, vesicular-type PDI secretion involves classical and unconventional pathways, while in platelets PDI exocytosis involves actin cytoskeleton. However, little is known about pecPDI in vascular smooth muscle cells(VSMC). Here, we showed that VSMC display a robust cell-surface(cs) PDI pool, which binds to cs independently of electrostatic forces. However, contrarily to other cells, soluble secreted PDI pool was undetectable in VSMC. Calcium ionophore A23187 and TNF alpha enhanced VSMC csPDI. Furthermore, VSMC PDI externalization occurred via Golgi-bypass unconventional route, which was independent of cytoskeleton or lysosomes. Secreted PDI was absent in ex vivo wild-type mice aortas but markedly enhanced in PDI-overexpressing mice. Such characterization of VSMC pecPDI reinforces cell-type and context specific routes of PDI externalization.
dc.description.indexMEDLINE
dc.description.sponsorshipFundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [12/02372-0, 15/06210-2]
dc.description.sponsorshipCentro de Pesquisa, Inovacao e Difusao FAPESP (CEPID ""Processos Redox em Biomedicina"") [13/07937-8]
dc.description.sponsorshipCAPES [PNPD20131600]
dc.description.sponsorshipFundacao Zerbini
dc.identifier.citationREDOX BIOLOGY, v.12, p.1004-1010, 2017
dc.identifier.doi10.1016/j.redox.2017.04.034
dc.identifier.issn2213-2317
dc.identifier.urihttps://observatorio.fm.usp.br/handle/OPI/21542
dc.language.isoeng
dc.publisherELSEVIER SCIENCE BV
dc.relation.ispartofRedox Biology
dc.rightsopenAccess
dc.rights.holderCopyright ELSEVIER SCIENCE BV
dc.subjectProtein disulfide isomerase
dc.subjectVascular smooth muscle cell
dc.subjectUnconventional protein traffic
dc.subjectEndoplasmic reticulum
dc.subjectCell-surface chaperones
dc.subject.otherthiol isomerases
dc.subject.otheractivated platelets
dc.subject.otherthrombus formation
dc.subject.othersecretion
dc.subject.otherexpression
dc.subject.othermigration
dc.subject.othersurface
dc.subject.otherendothelium
dc.subject.otherinhibitors
dc.subject.otherentry
dc.subject.wosBiochemistry & Molecular Biology
dc.titleGolgi-independent routes support protein disulfide isomerase externalization in vascular smooth muscle cells
dc.typearticle
dc.type.categoryoriginal article
dc.type.versionpublishedVersion
dspace.entity.typePublication
hcfmusp.citation.scopus16
hcfmusp.contributor.author-fmusphcTHAIS LARISSA ARAUJO DE OLIVEIRA SILVA
hcfmusp.contributor.author-fmusphcCAROLINA GONCALVES FERNANDES
hcfmusp.contributor.author-fmusphcFRANCISCO RAFAEL MARTINS LAURINDO
hcfmusp.description.beginpage1004
hcfmusp.description.endpage1010
hcfmusp.description.volume12
hcfmusp.origemWOS
hcfmusp.origem.pubmed28501017
hcfmusp.origem.scopus2-s2.0-85019057615
hcfmusp.origem.wosWOS:000403328700099
hcfmusp.publisher.cityAMSTERDAM
hcfmusp.publisher.countryNETHERLANDS
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