{"id":{"repo_id":"texas-state","oai_identifier":"oai:digital.library.txst.edu:10877/23576"},"canonical_url":"https://search.dev.ndltd.org/etd/texas-state/oai:digital.library.txst.edu:10877/23576","repository":{"repo_id":"texas-state","name":"Texas State University","base_url":"https://digital.library.txst.edu/server/oai/request"},"display":{"title":"Localization of Cytoskeletal Elements in Teleost Retinal Pigment Epithelium","abstract":"The G.3.5 antigen (Mr = 100,000) has been localized in brain, cerebellum, skeletal, cardiac, and smooth muscle tissues using the G.3.5 mAb, and has been described as an IFAP on the basis of its co-localization and co-isolation with desmin. Through biochemical analysis, the G.3.5 antigen was found to contain a peptide sequence that is 80% homologous to the actin binding region of human sarcomeric a-actinin. Recent Studies have suggested that the G.3.5 antigen may be a novel isoform of a-actinin, and may function to cross-link [Fs to MFs. In this study, I have used epifluorescence labeling techniques on cryosectioned bluegill RPE that have either been PFA fixed or hexane prepared. Using confocal microscopy, the G.3.5 antigen appears to co-localize with IFs, but not the MFs of CMBs in frozen RPE sections. These results do not support a role for the G.3.5 antigen in cross-linking CMB MEFs to IFs in bluegill RPE. In similar preparations, labeling patterns of cytoplasmic α-actinin and the G.3.5 antigen were observed to be different, thus suggesting that the G.3.5 antigen is distinct from cytoplasmic α-actinin.","abstract_html":"The G.3.5 antigen (Mr = 100,000) has been localized in brain, cerebellum, skeletal, cardiac, and smooth muscle tissues using the G.3.5 mAb, and has been described as an IFAP on the basis of its co-localization and co-isolation with desmin. Through biochemical analysis, the G.3.5 antigen was found to contain a peptide sequence that is 80% homologous to the actin binding region of human sarcomeric a-actinin. Recent Studies have suggested that the G.3.5 antigen may be a novel isoform of a-actinin, and may function to cross-link [Fs to MFs. In this study, I have used epifluorescence labeling techniques on cryosectioned bluegill RPE that have either been PFA fixed or hexane prepared. Using confocal microscopy, the G.3.5 antigen appears to co-localize with IFs, but not the MFs of CMBs in frozen RPE sections. These results do not support a role for the G.3.5 antigen in cross-linking CMB MEFs to IFs in bluegill RPE. In similar preparations, labeling patterns of cytoplasmic α-actinin and the G.3.5 antigen were observed to be different, thus suggesting that the G.3.5 antigen is distinct from cytoplasmic α-actinin.","abstract_has_math":false,"creators":["Zamora, David O."],"institution":"Southwest Texas State University","degree_name":"Master of Science","degree_level":"Masters","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":[],"advisors":["Gardia, Dana M."],"committee_chairs":[],"committee_members":["Koke, Joseph R.","McLean, Robert J. C."],"year":1997,"date_issued":"1997-08","date_published":"1997-08","updated_at":"2026-07-27T21:22:51Z","subjects":["cytoskeletal proteins","epithelial cells","Osteichthyes"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/10877/23576","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Gardia, Dana M."]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Koke, Joseph R.","McLean, Robert J. 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Through biochemical analysis, the G.3.5 antigen was found to contain a peptide sequence that is 80% homologous to the actin binding region of human sarcomeric a-actinin. Recent Studies have suggested that the G.3.5 antigen may be a novel isoform of a-actinin, and may function to cross-link [Fs to MFs. In this study, I have used epifluorescence labeling techniques on cryosectioned bluegill RPE that have either been PFA fixed or hexane prepared. Using confocal microscopy, the G.3.5 antigen appears to co-localize with IFs, but not the MFs of CMBs in frozen RPE sections. These results do not support a role for the G.3.5 antigen in cross-linking CMB MEFs to IFs in bluegill RPE. In similar preparations, labeling patterns of cytoplasmic α-actinin and the G.3.5 antigen were observed to be different, thus suggesting that the G.3.5 antigen is distinct from cytoplasmic α-actinin."]},{"key":"dc:format","label":"Dc Format","values":["Text"]},{"key":"dc:format.medium","label":"Dc Format Medium","values":["1 file (.pdf)"]},{"key":"dc:title","label":"Title","values":["Localization of Cytoskeletal Elements in Teleost Retinal Pigment Epithelium"]}]}],"canonical_facts":{"dc:contributor.advisor":["Gardia, Dana M."],"dc:contributor.committeemember":["Koke, Joseph R.","McLean, Robert J. C."],"dc:creator":["Zamora, David O."],"dc:date.accessioned":["2025-12-18T18:13:45Z"],"dc:date.issued":["1997-08"],"dc:description.abstract":["The G.3.5 antigen (Mr = 100,000) has been localized in brain, cerebellum, skeletal, cardiac, and smooth muscle tissues using the G.3.5 mAb, and has been described as an IFAP on the basis of its co-localization and co-isolation with desmin. Through biochemical analysis, the G.3.5 antigen was found to contain a peptide sequence that is 80% homologous to the actin binding region of human sarcomeric a-actinin. Recent Studies have suggested that the G.3.5 antigen may be a novel isoform of a-actinin, and may function to cross-link [Fs to MFs. In this study, I have used epifluorescence labeling techniques on cryosectioned bluegill RPE that have either been PFA fixed or hexane prepared. Using confocal microscopy, the G.3.5 antigen appears to co-localize with IFs, but not the MFs of CMBs in frozen RPE sections. These results do not support a role for the G.3.5 antigen in cross-linking CMB MEFs to IFs in bluegill RPE. In similar preparations, labeling patterns of cytoplasmic α-actinin and the G.3.5 antigen were observed to be different, thus suggesting that the G.3.5 antigen is distinct from cytoplasmic α-actinin."],"dc:format":["Text"],"dc:format.medium":["1 file (.pdf)"],"dc:identifier.uri":["https://hdl.handle.net/10877/23576"],"dc:language.iso":["en"],"dc:subject":["cytoskeletal proteins","epithelial cells","Osteichthyes"],"dc:title":["Localization of Cytoskeletal Elements in Teleost Retinal Pigment Epithelium"],"dc:type":["Thesis"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Masters"],"thesis:degree_name":["Master of Science"],"thesis:institution_name":["Southwest Texas State University"]},"updated_at":"2026-07-27T21:22:51Z"}