@article{davis_hiramatsu_hiramatsu_reading_matsubara_hara_sullivan_pierce_hirano_grau_2007, title={Induction of three vitellogenins by 17beta-estradiol with concurrent inhibition of the growth hormone-insulin-like growth factor 1 axis in a euryhaline teleost, the tilapia (Oreochromis mossambicus)}, volume={77}, ISSN={["1529-7268"]}, DOI={10.1095/biolreprod.107.060947}, abstractNote={Abstract The objective of the present study was to utilize the male Mozambique tilapia (Oreochromis mossambicus) as a model for examining the molecular mechanisms that mediate the physiological transition between somatic and gonadal growth in female teleost fish, and in vertebrates in general. Partial cDNAs that encode multiple forms of vitellogenin (Vtg), which is the major precursor of yolk proteins, were cloned from estrogen-treated males and utilized to develop real-time quantitative RT-PCR assays, which were supplemented by an assay for Vtg immunoreactivity in the plasma. Alignment analyses of the amino acid sequences deduced from the vtg cDNAs revealed three distinct tilapia Vtgs, which were categorized as Aa-, Ab-, and C-type Vtgs. A single injection of male tilapias with 17beta-estradiol (E2) at 5 μg/g body weight significantly increased the plasma E2 and hepatic levels of all three vtg transcripts within 1 day. Plasma E2 levels declined after 3 days, whereas the plasma Vtg immunoreactivity and hepatic levels of the three vtg transcripts continued to increase. Hepatic expression of the estrogen receptor (esr) 1 gene, but not the esr2 gene, also increased markedly 1 day after E2 injection and remained elevated for 5 days. While plasma growth hormone (Gh) levels were unaffected, hepatic expression of transcripts that encoded the Gh receptor and insulin-like growth factor 1 (Igf1) was suppressed by E2, as were the plasma Igf1 levels. These results clearly suggest a distinct negative interplay between the growth and reproductive axes at the molecular level of key hepatic regulatory pathways involved in the control of energy utilization by gonadal and somatic growth processes.}, number={4}, journal={BIOLOGY OF REPRODUCTION}, author={Davis, Lori K. and Hiramatsu, Naoshi and Hiramatsu, Kaori and Reading, Benjamin J. and Matsubara, Takahiro and Hara, Akihiko and Sullivan, Craig V. and Pierce, Andrew L. and Hirano, Tetsuya and Grau, Gordon}, year={2007}, month={Oct}, pages={614–625} }
 @article{sawaguchi_koya_yoshizaki_ohkubo_andoh_hiramatsu_sullivan_hara_matsubara_2005, title={Multiple vitellogenins (Vgs) in mosquitofish (Gambusia affinis): Identification and characterization of three functional Vg genes and their circulating and yolk protein products}, volume={72}, ISSN={["1529-7268"]}, DOI={10.1095/biolreprod.104.037895}, abstractNote={Abstract The objectives of this study were to characterize multiple forms of vitellogenin (Vg) in mosquitofish (Gambusia affinis) and to discover the fate of each Vg during its processing into product yolk proteins. Two Vg preparations, with apparent masses of 600 kDa (600 Vg) and 400 kDa (400 Vg), were isolated from the plasma of fish treated with estradiol-17β (E2) by various chromatographic procedures. Immunological analyses verified the presence of two different Vg proteins (600 VgA and 600 VgB) in the 600 Vg preparation and of a single protein in the 400 Vg preparation. Three major yolk proteins (Yps) with apparent masses of 560, 400, and 28 kDa were observed in extracts of ovarian follicles from vitellogenic females. Immunological analyses demonstrated that the 400 Vg underwent no change in native mass after being incorporated into oocytes. The 600 Vgs gave rise to a 28 kDa β′-component and a native 560 kDa Yp, which was heterodimeric in structure, consisting of two types of complexes between phosvitin (Pv) and lipovitellin (Lv) heavy- and light-chains. Full-length cDNAs encoding the 600 VgA, 600 VgB, and 400 Vg were isolated from a liver cDNA library of E2 treated fish. Similar to the zebrafish vg3 gene, the 400 Vg cDNA lacked a Pv domain and was classified as an incomplete or phosvitinless (C-type) Vg. The deduced primary structures of 600 VgA and 600 VgB were complete, and these were categorized as type A and type B Vgs, respectively, according to our recent classification scheme. This is the first report on the characterization of three functional Vg genes and their circulating and yolk protein products in any vertebrate species.}, number={4}, journal={BIOLOGY OF REPRODUCTION}, author={Sawaguchi, S and Koya, Y and Yoshizaki, N and Ohkubo, N and Andoh, T and Hiramatsu, N and Sullivan, CV and Hara, A and Matsubara, T}, year={2005}, month={Apr}, pages={1045–1060} }
 @article{donato_hiramatsu_arey_hiramatsu_kennedy_morton_hara_sullivan_2003, title={Atresia in temperate basses: cloning of hatching enzyme (choriolysin) homologues from atretic ovaries}, volume={28}, ISSN={["0920-1742"]}, DOI={10.1023/B:FISH.0000030573.04442.19}, number={1-4}, journal={FISH PHYSIOLOGY AND BIOCHEMISTRY}, author={Donato, DM and Hiramatsu, N and Arey, KM and Hiramatsu, K and Kennedy, AM and Morton, CL and Hara, A and Sullivan, CV}, year={2003}, pages={329–330} }
 @article{hiramatsu_hiramatsu_hara_matsubara_sullivan_2003, title={Multiple vitellogenins in white perch (Morone americana)}, volume={28}, ISSN={["1573-5168"]}, DOI={10.1023/B:FISH.0000030582.66324.6c}, number={1-4}, journal={FISH PHYSIOLOGY AND BIOCHEMISTRY}, author={Hiramatsu, K and Hiramatsu, N and Hara, A and Matsubara, T and Sullivan, CV}, year={2003}, pages={347–348} }
 @article{hiramatsu_hara_matsubara_hiramatsu_sullivan_2003, title={Oocyte growth in temperate basses: multiple forms of vitellogenin and their receptor}, volume={28}, ISSN={["0920-1742"]}, DOI={10.1023/B:FISH.0000030560.79921.10}, number={1-4}, journal={FISH PHYSIOLOGY AND BIOCHEMISTRY}, author={Hiramatsu, N and Hara, A and Matsubara, T and Hiramatsu, K and Sullivan, CV}, year={2003}, pages={301–303} }
 @article{hiramatsu_matsubara_hara_donato_hiramatsu_denslow_sullivan_2002, title={Identification, purification and classification of multiple forms of vitellogenin from white perch (Morone americana)}, volume={26}, ISSN={["1573-5168"]}, DOI={10.1023/B:FISH.0000009266.58556.9a}, number={4}, journal={FISH PHYSIOLOGY AND BIOCHEMISTRY}, author={Hiramatsu, N and Matsubara, T and Hara, A and Donato, DM and Hiramatsu, K and Denslow, ND and Sullivan, CV}, year={2002}, pages={355–370} }
 @article{hiramatsu_hara_hiramatsu_fukada_weber_denslow_sullivan_2002, title={Vitellogenin-derived yolk proteins of white perch, Morone americana: Purification, characterization, and vitellogenin-receptor binding}, volume={67}, ISSN={["1529-7268"]}, DOI={10.1095/biolreprod67.2.655}, abstractNote={Abstract The objectives of this study were to 1) purify and characterize vitellogenin-derived yolk proteins of white perch (Morone americana), 2) develop a nonisotopic receptor binding assay for vitellogenin, and 3) identify the yolk protein domains of vitellogenin recognized by the ovarian vitellogenin receptor. Four yolk proteins derived from vitellogenin (YP1, YP2 monomer [YP2m] and dimer [YP2d], and YP3) were isolated from ovaries of vitellogenic perch by selective precipitation, ion exchange chromatography, and gel filtration. The apparent molecular masses of purified YP1, YP2m, and YP2d after gel filtration were 310 kDa, 17 kDa, and 27 kDa, respectively. YP3 appeared in SDS-PAGE as a ∼20-kDa band plus some diffuse smaller bands that could be visualized by staining for phosphoprotein with Coomassie Brilliant Blue complexed with aluminum nitrate. Immunological and biochemical characteristics of YP1, YP2s, and YP3 identified them as white perch lipovitellin, β′-components, and phosvitin, respectively. A novel receptor-binding assay for vitellogenin was developed based on digoxigenin (DIG)-labeled vitellogenin tracer binding to ovarian membrane proteins immobilized in 96-well plates. Lipovitellin from white perch and vitellogenin from perch and other teleosts effectively displaced specifically bound DIG-vitellogenin in the assay, but phosvitin and the β′-component could not, demonstrating for the first time that the lipovitellin domain of teleost vitellogenin mediates its binding to the oocyte receptor. Lipovitellin was less effective than vitellogenin in this regard, suggesting that the remaining yolk protein domains of vitellogenin may interact with its lipovitellin domain to facilitate binding of vitellogenin to its receptor.}, number={2}, journal={BIOLOGY OF REPRODUCTION}, author={Hiramatsu, N and Hara, A and Hiramatsu, K and Fukada, H and Weber, GM and Denslow, ND and Sullivan, CV}, year={2002}, month={Aug}, pages={655–667} }