Peptides Derived from Two Separate Domains of the Matrix Protein Thrombospondin-1 Have Anti-Angiogenlc Activity

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dc.contributor.authorTolsma, Sara S.en
dc.contributor.authorVolpert, Olga V.en
dc.contributor.authorGood, Deborah J.en
dc.contributor.authorFrazier, William A.en
dc.contributor.authorPolverini, Peter J.en
dc.contributor.authorBouck, Noelen
dc.contributor.departmentHuman Nutrition, Foods, and Exerciseen
dc.date.accessioned2017-02-08T13:16:10Zen
dc.date.available2017-02-08T13:16:10Zen
dc.date.issued1993-07-01en
dc.description.abstractThrombospondin-1 (TSP1) is a large modular matrix protein containing three identical disulfide-linked 180-kD chains that inhibits neovascularization in vivo (Good et al., 1990). To determine which of the structural motifs present in the 180-kD TSP1 polypeptide mediate the anti-angiogenic activity, a series of protease-generated fragments were tested using several in vitro and in vivo assays that reflect angiogenic activity. The majority of the anti-angiogenic activity of TSP1 resides in the central 70-kD stalk region which alone could block neovascularization induced by bFGF in the rat cornea in vivo and inhibit both migration in a modified Boyden chamber and [~H]thymidine incorporation stimulated by bFGF in cultured capillary endothelial cells. Although TSP1 has been shown to bind active TGF/31, this cytokine could not account for the inhibitory effects of the stalk region of TSP1 on cultured endothelial cells.en
dc.description.versionPublished versionen
dc.format.extent497 - 511 (15) page(s)en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1083/jcb.122.2.497en
dc.identifier.issn0021-9525en
dc.identifier.issue2en
dc.identifier.urihttp://hdl.handle.net/10919/74964en
dc.identifier.volume122en
dc.language.isoenen
dc.publisherRockefeller University Pressen
dc.relation.urihttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:A1993LM58400019&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=930d57c9ac61a043676db62af60056c1en
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectCell Biologyen
dc.subjectGROWTH-FACTOR-BETAen
dc.subjectENDOTHELIAL-CELLS INVITROen
dc.subjectCIRCUMSPOROZOITE PROTEINen
dc.subjectCHORIOALLANTOIC MEMBRANEen
dc.subjectPLATELET THROMBOSPONDINen
dc.subjectADHESIVE GLYCOPROTEINen
dc.subjectBINDING DOMAINen
dc.subjectMESSENGER-RNAen
dc.subjectTGF-BETAen
dc.subjectINHIBITIONen
dc.titlePeptides Derived from Two Separate Domains of the Matrix Protein Thrombospondin-1 Have Anti-Angiogenlc Activityen
dc.title.serialJournal of Cell Biologyen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciencesen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/CALS T&R Facultyen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/Human Nutrition, Foods, & Exerciseen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen

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