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dc.identifier.urihttp://hdl.handle.net/1951/59591
dc.identifier.urihttp://hdl.handle.net/11401/71017
dc.description.sponsorshipThis work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree.en_US
dc.formatMonograph
dc.format.mediumElectronic Resourceen_US
dc.language.isoen_US
dc.publisherThe Graduate School, Stony Brook University: Stony Brook, NY.
dc.typeThesis
dcterms.abstractMembrane type 1 matrix metalloproteinase (MT1-MMP) plays a major role in cancer invasion and metastasis. The mechanism by which MT1-MMP is trafficked to the plasma membrane where it functions to proteolytically activate its substrate proteins is not fully understood. The gene of heat shock protein (Hsp90alpha) was identified as being upregulated in HT1080 cells treated with concanavalin A (conA), a lectin that promotes proMMP-2 activation and cell migration in HT1080 cells compared to untreated HT1080 cells. To determine the mechanism underlying MT1-MMP substrate degradation and cell migration, biological and biochemical approaches were carried out. Zymography was preformed to examine the affect of the presence of both Hsp90alpha; and MT1-MMP, on the gelatinase activity of matrix metalloproteinase (MMP-2). The zympograph showed that when both Hsp90alpha and MT1-MMP were both present, there was an increase in the active form of MMP-2, a protein that is proteolytically activated by MT1-MMP at the plasma membrane. shRNA knockdown studies of Hsp90alpha were also done to further establish a role for Hsp90alpha in effecting the ability of MT1-MMP to activate its target proteins at the plasma membrane. Together these studies indicate that Hsp90alpha plays a role in the ability of MT1-MMP to activate substrate proteins at the plasma membrane.
dcterms.available2013-05-22T17:34:14Z
dcterms.available2015-04-24T14:45:35Z
dcterms.contributorDean, Neta.en_US
dcterms.contributorCao, Jianen_US
dcterms.creatorBuck, Theresa
dcterms.dateAccepted2013-05-22T17:34:14Z
dcterms.dateAccepted2015-04-24T14:45:35Z
dcterms.dateSubmitted2013-05-22T17:34:14Z
dcterms.dateSubmitted2015-04-24T14:45:35Z
dcterms.descriptionDepartment of Biochemistry and Cell Biologyen_US
dcterms.extent31 pg.en_US
dcterms.formatApplication/PDFen_US
dcterms.formatMonograph
dcterms.identifierhttp://hdl.handle.net/1951/59591
dcterms.identifierBuck_grad.sunysb_0771M_10741en_US
dcterms.identifierhttp://hdl.handle.net/11401/71017
dcterms.issued2011-12-01
dcterms.languageen_US
dcterms.provenanceMade available in DSpace on 2013-05-22T17:34:14Z (GMT). No. of bitstreams: 1 Buck_grad.sunysb_0771M_10741.pdf: 2805726 bytes, checksum: 982477b4fbe480ea29839a6f6ebba890 (MD5) Previous issue date: 1en
dcterms.provenanceMade available in DSpace on 2015-04-24T14:45:35Z (GMT). No. of bitstreams: 3 Buck_grad.sunysb_0771M_10741.pdf.jpg: 1894 bytes, checksum: a6009c46e6ec8251b348085684cba80d (MD5) Buck_grad.sunysb_0771M_10741.pdf.txt: 68255 bytes, checksum: 1e22ecb87b2fe5a30cb44f707766904c (MD5) Buck_grad.sunysb_0771M_10741.pdf: 2805726 bytes, checksum: 982477b4fbe480ea29839a6f6ebba890 (MD5) Previous issue date: 1en
dcterms.publisherThe Graduate School, Stony Brook University: Stony Brook, NY.
dcterms.subjectBiology
dcterms.titleHeat shock protein, Hsp90 plays a role in MT1-MMP's ability to activate substrate proteins
dcterms.typeThesis


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