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Title page for ETD etd-06172008-105010


Type of Document Dissertation
Author Reading, Benjamin Jacob,
URN etd-06172008-105010
Title Immunobiochemical and Molecular Characterizations of Vitellogenesis in White Perch, Morone americana
Degree PhD
Graduate Program Zoology
Advisory Committee
Advisor Name Title
Craig V. Sullivan Committee Chair
Coby Schal Committee Member
John R. Godwin Committee Member
Russell J. Borski Committee Member
Keywords
  • teleost fish
  • vitellogenin receptor
  • vitellogenin
  • oocyte
  • oogenesis
  • egg yolk
  • white perch
  • gametogenesis
Date of Defense 2008-06-16
Availability unrestricted
Abstract
Three complete complementary DNAs encoding different forms of the yolk precursor protein, vitellogenin (Vtg), were cloned from a white perch (Morone americana) liver cDNA library. The two longest cDNAs encoded Vtgs with a complete suite of yolk protein domains and, based on comparisons with Vtg sequences from other species, they were categorized as VtgAa and VtgAb using nomenclature for multiple teleost Vtgs. The shorter cDNA encoded a Vtg that lacked a phosvitin (Pv) domain, had a shortened C-terminus, and was categorized as VtgC. Multiple distinct Vtg receptors (Vtgrs) with disparate affinities for binding the different types of complete Vtg ligands (Vtgs Aa and Ab) were discovered in the ovary of white perch. Ligand blots of ovarian membranes separated by non-denaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) using digoxigenin-labeled purified VtgAa and VtgAb resolved one large (200+kDa) receptor that binds primarily to VtgAa and two smaller receptors (116kDa and 110.5kDa) that bind primarily to VtgAb. Furthermore, in this species, the Pv-less Vtg (VtgC) does not bind to ovarian membranes in either ligand blotting or competitive binding assays. These findings provide the first evidence for a system of multiple Vtgrs involved in the specific uptake of dual complete type Vtgs and the lack of a receptor-mediated system for uptake of VtgC, thus providing for a new model of yolk protein deposition into teleost oocytes.
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