@prefix activity: .
@prefix address: .
@prefix agency: .
@prefix assay: .
@prefix assayCategory: .
@prefix assayTargetLink: .
@prefix biopax3: .
@prefix calbc: .
@prefix calbc-group: .
@prefix carrierLink: .
@prefix certainAgreement: .
@prefix chebi: .
@prefix chembl: .
@prefix chemicalCompound: .
@prefix chemicalCompoundRecord: .
@prefix clan: .
@prefix clinicalResult: .
@prefix clinicalStudy: .
@prefix clinicaltrials: .
@prefix company: .
@prefix confidenceScore: .
@prefix contact: .
@prefix country: .
@prefix cpath: .
@prefix curationLookup: .
@prefix dailymed: .
@prefix dailymed-drugs: .
@prefix dailymed-ingredient: .
@prefix dailymed-instance: .
@prefix databaseReference: .
@prefix dc: .
@prefix dc-term: .
@prefix diseaseontology: .
@prefix diseasome: .
@prefix diseasome-diseases: .
@prefix diseasome-gene: .
@prefix diseasome-instance: .
@prefix documentType: .
@prefix dosageForm: .
@prefix drug: .
@prefix drugbank: .
@prefix drugbank-proteinSequence: .
@prefix drugCategory: .
@prefix drugInteraction: .
@prefix drugTarget: .
@prefix eligibility: .
@prefix entrez-gene: .
@prefix entrez-goterm: .
@prefix entrezgene: .
@prefix enzymeLink: .
@prefix externalIdentifier: .
@prefix externalLink: .
@prefix factforge: .
@prefix family: .
@prefix foaf: .
@prefix formulation: .
@prefix freebase: .
@prefix gene-rif: .
@prefix geneontology: .
@prefix geneSequence: .
@prefix hapmap: .
@prefix indication: .
@prefix intervention: .
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@prefix lifeskim: .
@prefix linkedct: .
@prefix linkedct-condition: .
@prefix linkedct-intervention: .
@prefix literatureCitation: .
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@prefix mixture: .
@prefix molecularSpecies: .
@prefix molecule: .
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@prefix ontotext: .
@prefix organismSpecies: .
@prefix outcomeAnalysis: .
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@prefix overallOfficial: .
@prefix owl: .
@prefix owlim: .
@prefix packager: .
@prefix participantFlow: .
@prefix patent: .
@prefix pfam: .
@prefix phenotype: .
@prefix pointOfContact: .
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@prefix pubmed: .
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@prefix result: .
@prefix resultsBaseline: .
@prefix resultsMeasure: .
@prefix resultsOutcome: .
@prefix secondaryOutcome: .
@prefix sideEffect: .
@prefix sideEffectFrequency: .
@prefix sider: .
@prefix sider-drug: .
@prefix skos: .
@prefix skos-xl: .
@prefix snp: .
@prefix structureType: .
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@prefix substructure: .
@prefix symptom: .
@prefix synonym: .
@prefix targetLink: .
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@prefix taxonomyClass: .
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@prefix transporterLink: .
@prefix umls: .
@prefix umls-concept: .
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@prefix umls-semnetwork: .
@prefix uniprot: .
@prefix uniprot-protein: .
@prefix uniprot-unstable: .
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pubmed-article:2745554 a pubmed:Citation ;
lifeskim:mentions umls-concept:C0007634 , umls-concept:C0015350 , umls-concept:C0033684 , umls-concept:C0596290 , umls-concept:C1327616 , umls-concept:C0020507 , umls-concept:C0332281 , umls-concept:C1420342 , umls-concept:C1167622 , umls-concept:C0332261 , umls-concept:C1533691 , umls-concept:C0015272 ;
pubmed:issue "1" ;
pubmed:dateCreated "1989-8-21" ;
pubmed:abstractText "SPARC (Secreted Protein Acidic and Rich in Cysteine) is a Ca+2-binding glycoprotein that is differentially associated with morphogenesis, remodeling, cellular migration, and proliferation. We show here that exogenous SPARC, added to cells in culture, was associated with profound changes in cell shape, caused rapid, partial detachment of a confluent monolayer, and inhibited spreading of newly plated cells. Bovine aortic endothelial cells, exposed to 2-40 micrograms SPARC/ml per 2 x 10(6) cells, exhibited a rounded morphology in a dose-dependent manner but remained attached to plastic or collagen-coated surfaces. These round cells synthesized protein, uniformly excluded trypan blue, and grew in aggregates after replating in media without SPARC. SPARC caused rounding of bovine endothelial cells, fibroblasts, and smooth muscle cells; however, the cell lines F9, PYS-2, and 3T3 were not affected. The activity of native SPARC was inhibited by heat denaturation and prior incubation with anti-SPARC IgG. The effect of SPARC on endothelial cells appeared to be independent of the rounding phenomenon produced by the peptide GRGDSP. Immunofluorescence localization of SPARC on endothelial cells showed preferential distribution at the leading edges of membranous extensions. SPARC bound Ca+2 in both amino- and carboxyl-terminal (EF-hand) domains and required this cation for maintenance of native structure. Solid-phase binding assays indicated a preferential affinity of native SPARC for several proteins comprising the extracellular matrix, including types III and V collagen, and thrombospondin. This binding was saturable, Ca+2 dependent, and inhibited by anti-SPARC IgG. Endothelial cells also failed to spread on a substrate of native type III collagen complexed with SPARC. We propose that SPARC is an extracellular modulator of Ca+2 and cation-sensitive proteins or proteinases, which facilitates changes in cellular shape and disengagement of cells from the extracellular matrix." ;
pubmed:grant ;
pubmed:commentsCorrections , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , ;
pubmed:language "eng" ;
pubmed:journal ;
pubmed:citationSubset "IM" ;
pubmed:chemical , , , ;
pubmed:status "MEDLINE" ;
pubmed:month "Jul" ;
pubmed:issn "0021-9525" ;
pubmed:author pubmed-author:SageHH , , , pubmed-author:AngelloJJ , ;
pubmed:issnType "Print" ;
pubmed:volume "109" ;
pubmed:owner "NLM" ;
pubmed:authorsComplete "Y" ;
pubmed:pagination "341-56" ;
pubmed:dateRevised "2009-11-18" ;
pubmed:meshHeading pubmed-meshheading:2745554-Animals , pubmed-meshheading:2745554-Calcium , pubmed-meshheading:2745554-Collagen , pubmed-meshheading:2745554-Cattle , , , , , , , , , pubmed-meshheading:2745554-Osteonectin ;
pubmed:year "1989" ;
pubmed:articleTitle "SPARC, a secreted protein associated with cellular proliferation, inhibits cell spreading in vitro and exhibits Ca+2-dependent binding to the extracellular matrix." ;
pubmed:affiliation "Department of Biological Structure, University of Washington, Seattle 98195." ;
pubmed:publicationType "Journal Article" , "In Vitro" , "Research Support, U.S. Gov't, P.H.S." .