Identification of Regulatory Elements in a Conserved Upstream Region of the Gene Encoding Interphotoreceptor Retinoid-Binding Protein (IRBP)

Hdl Handle:
http://hdl.handle.net/10675.2/550457
Title:
Identification of Regulatory Elements in a Conserved Upstream Region of the Gene Encoding Interphotoreceptor Retinoid-Binding Protein (IRBP)
Authors:
Lu, Haiyan
Abstract:
(First Paragraph) IRBP is a large, single-subunit extracellular glycolipoprotein found in the interphotoreceptor matrix between the photoreceptor cells and retinal pigment epithelium cell layer (Fig. 1.). The protein is synthesized and secreted by the photoreceptor rods and cones, as well as pinealocytes, of all vertebrates. The molecular weight of human IRBP (1230 residues) is 133,400 daltons. This protein consists of four homologous segments of approximately 300 residues each. Each segment contains highly conserved hydrophobic domains among species. Ligands identified as bound to IRBP include retinoid isomers and fatty acids, and IRBP can also bind cholesterol, a-tocopherol and retinoic acid. The ability of IRBP to bind various retinoid isomers, fatty acids and many other hydrophobic ligands suggests multiple functions in the retina .
Affiliation:
Department of Ophthalmology
Issue Date:
Jun-1999
URI:
http://hdl.handle.net/10675.2/550457
Additional Links:
http://ezproxy.augusta.edu/login?url=http://search.proquest.com/docview/304463562?accountid=12365
Type:
Dissertation
Appears in Collections:
Department of Ophthalmology: Faculty Research and Presentations; Theses and Dissertations

Full metadata record

DC FieldValue Language
dc.contributor.authorLu, Haiyanen
dc.date.accessioned2015-04-22T02:33:47Zen
dc.date.available2015-04-22T02:33:47Zen
dc.date.issued1999-06en
dc.identifier.urihttp://hdl.handle.net/10675.2/550457-
dc.description.abstract(First Paragraph) IRBP is a large, single-subunit extracellular glycolipoprotein found in the interphotoreceptor matrix between the photoreceptor cells and retinal pigment epithelium cell layer (Fig. 1.). The protein is synthesized and secreted by the photoreceptor rods and cones, as well as pinealocytes, of all vertebrates. The molecular weight of human IRBP (1230 residues) is 133,400 daltons. This protein consists of four homologous segments of approximately 300 residues each. Each segment contains highly conserved hydrophobic domains among species. Ligands identified as bound to IRBP include retinoid isomers and fatty acids, and IRBP can also bind cholesterol, a-tocopherol and retinoic acid. The ability of IRBP to bind various retinoid isomers, fatty acids and many other hydrophobic ligands suggests multiple functions in the retina .en
dc.relation.urlhttp://ezproxy.augusta.edu/login?url=http://search.proquest.com/docview/304463562?accountid=12365en
dc.rightsCopyright protected. Unauthorized reproduction or use beyond the exceptions granted by the Fair Use clause of U.S. Copyright law may violate federal law.en
dc.subjectIRBPen
dc.subjectOligonucleotidesen
dc.subjectRetinaen
dc.titleIdentification of Regulatory Elements in a Conserved Upstream Region of the Gene Encoding Interphotoreceptor Retinoid-Binding Protein (IRBP)en
dc.typeDissertationen
dc.contributor.departmentDepartment of Ophthalmologyen
dc.description.advisorLiou, Gregory I.en
dc.description.committeeGreen, Keith; Bollag, Roni J.; Galileo, Deni S.; Stoming, Terrence A.en
dc.description.degreeDoctor of Philosophy (Ph.D.)en
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