Characterization of proteins and tissue remodeling components in porcine aqueous humor

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dc.contributor.authorChandran, Jayanth Sankriten
dc.contributor.committeechairVan Cott, Kevin E.en
dc.contributor.committeememberGoldstein, Aaron S.en
dc.contributor.committeememberForsten-Williams, Kimberlyen
dc.contributor.departmentChemical Engineeringen
dc.date.accessioned2014-03-14T20:44:32Zen
dc.date.adate2000-09-08en
dc.date.available2014-03-14T20:44:32Zen
dc.date.issued2000-08-22en
dc.date.rdate2001-09-08en
dc.date.sdate2000-08-31en
dc.description.abstractConnective tissue remodeling is an important area of study in biomedical engineering with respect to cancer and wound healing. Tissue remodeling components may be involved in the pathogenesis of open-angle glaucoma. Risk factors for open angle glaucoma include increased intraocular pressure (IOP), male gender, and advanced age. In a 1963 study, the hormone relaxin decreased IOP in the human eye through a mechanism that may involve the up-regulation of tissue remodeling matrix metalloproteinases (MMPs). The effects of age and gender on MMP and protein activity in porcine aqueous humor were determined in this study to identify correlations existing between MMP activity and glaucoma risk factors. Gelatin zymography identified MMPs at 66 kD and approximately 105 kD. The concentration of the 66 kD band compared to human MMP-2 standard was 0.22 ± 0.06 ng/ml for the adult female (AF) samples and 0.28 ± 0.04 ng/ml for the juvenile samples. This difference in concentration was statistically significant (p < 0.05). The concentration of the protease migrating to 66 kD was statistically independent of gender. Casein zymograms identified two non-MMP proteinases at 51 kD and 80 kD. The average total protein concentration for all aqueous humor samples was 2.54 ± 0.89 mg/ml. The mean IgG, transferrin, and albumin concentrations for all aqueous humor samples was 11.4 ± 4.2 mg/ml, 17.11 ± 6.8 mg/ml, and 78.0 ± 26.3 mg/ml respectively. Results from these experiments establish baseline levels of MMP and protein activity, allowing for identification of potential changes caused by relaxin in tissue culture studies.en
dc.description.degreeMaster of Scienceen
dc.identifier.otheretd-08312000-16210046en
dc.identifier.sourceurlhttp://scholar.lib.vt.edu/theses/available/etd-08312000-16210046/en
dc.identifier.urihttp://hdl.handle.net/10919/34859en
dc.publisherVirginia Techen
dc.relation.haspartthesis_final.pdfen
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectmatrix metalloproteinaseen
dc.subjectrelaxinen
dc.subjectglaucomaen
dc.subjectaqueous humoren
dc.titleCharacterization of proteins and tissue remodeling components in porcine aqueous humoren
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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