Characterization of Insulin-like Growth Factor Binding Protein-3 (IGFBP-3) interaction with the Bovine Aortic Endothelial (BAE) cell surface: Examination of the Role of Heparan Sulfate Proteoglycans (HSPG)

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dc.contributor.authorParghi, Niraven
dc.contributor.committeechairForsten-Williams, Kimberlyen
dc.contributor.committeememberConger, William L.en
dc.contributor.committeememberAkers, Robert Michaelen
dc.contributor.departmentChemical Engineeringen
dc.date.accessioned2014-03-14T20:52:14Zen
dc.date.adate1998-08-24en
dc.date.available2014-03-14T20:52:14Zen
dc.date.issued1998-07-15en
dc.date.rdate1998-08-24en
dc.date.sdate1998-07-15en
dc.description.abstractInsulin-like growth factor binding proteins (IGFBPs) are known to be important modulators of the insulin-like growth factor (IGF-I). However, their precise role is as yet unclear. Further, recent studies have indicated that IGFBP-3 has a receptor mediated growth inhibitory response of its own. In the present study, we quantified the binding characteristics of IGFBP-3 to bovine aortic endothelial (BAE) cells. Binding studies at 4 <sup>o</sup>C were conducted and a specific binding curve for IGFBP-3 was obtained. IGFBP-3 was found to bind with an equilibrium dissociation constant (K<sub>D</sub>) value of 3.1 x 10<sup>-10</sup> M. The role of heparan sulfate proteoglycans (HSPG) in the IGFBP-3 binding mechanism was also examined. It was seen that inactivation of the cell surface HSPGs with 75 mM sodium chlorate did not affect IGFBP-3 binding. Further, there have been reports of inhibition of IGFBP-3 binding by heparin in the media. Hence, the most probable interaction of HSPG with IGFBP-3 occurs in the extracellular region, with soluble HSPGs acting as receptors for IGFBP-3 and decreasing the net cell associated ligand receptor interaction. This is likely, since IGFBP-3 is known to possess a heparin binding domain. Simultaneous introduction of IGF-I and IGFBP-3 into the extracellular media decreased IGFBP-3 binding to the cell surface, which might imply that IGF-I and IGFBP-3 regulate each other's action.en
dc.description.degreeMaster of Scienceen
dc.identifier.otheretd-72398-15376en
dc.identifier.sourceurlhttp://scholar.lib.vt.edu/theses/available/etd-72398-15376/en
dc.identifier.urihttp://hdl.handle.net/10919/36928en
dc.publisherVirginia Techen
dc.relation.haspartthesisfinA.PDFen
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectKDen
dc.subjectHSPGen
dc.subjectIGFBP-3en
dc.subjectbindingen
dc.subjectBAEen
dc.titleCharacterization of Insulin-like Growth Factor Binding Protein-3 (IGFBP-3) interaction with the Bovine Aortic Endothelial (BAE) cell surface: Examination of the Role of Heparan Sulfate Proteoglycans (HSPG)en
dc.typeThesisen
thesis.degree.disciplineChemical Engineeringen
thesis.degree.grantorVirginia Polytechnic Institute and State Universityen
thesis.degree.levelmastersen
thesis.degree.nameMaster of Scienceen

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