Skip to main content

Physiological and molecular basis of fish oocyte hydration

  • Chapter
The Fish Oocyte

As in other lower vertebrates, teleost oocytes growing within the ovary pass through a series of developmental stages that eventually culminate in the production of a mature female gamete or egg. During most of its time they are temporarily arrested in meiotic prophase I, and energy expenditures are concentrated on the synthesis and uptake of various substances (e.g. vitellogenin (Vg) ) required by the developing oocyte and subsequent embryo development. After oocyte growth, meosis resumes as the large nucleus or germinal vesicle breaks down (GVBD), half the chromosomes are eliminated into a small polar body by unequal cytokinesis, and the remainder becomes aligned in second meiotic metaphase at the animal pole. During this process, termed “meiotic maturation”, or “oocyte maturation”, ovulation generally occurs. Shortly after second meiotic metaphase is achieved, the oocyte becomes “activable” or capable of being fertilized, and hence becomes an egg.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 129.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 299.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Abrami, L., Simon, M., Rousselet, G., Berthonaud, V., Buhler, J.M., Ripoche, P. Sequence and functional expression of an amphibian water channel, FA-CHIP: a new member of the MIP family. Biochim. Biophys. Acta. 1192:147–51 (1994).

    PubMed  CAS  Google Scholar 

  • Agre, P., Preston, G.M., Smith, B.L., Jung, J.S., Raina, S., Moon, C., Guggino, W.B., Nielsen, S. Aquaporin CHIP: the archetypal molecular water channel. Am. J. Physiol. 265:F463–476 (1993).

    PubMed  CAS  Google Scholar 

  • Agre, P., King, S.L., Yasui, M., Guggino, W.B., Ottersen, O.P., Fujiyoshi, Y., Engel, A., Nielsen, S. Aquaporin water channels–from atomic structure to clinical medicine. J. Physiol. 542:3–16 (2002).

    PubMed  CAS  Google Scholar 

  • Ahlstrom, E.H., Moser, H.G. Characters useful in identification of pelagic marine fish eggs. Rep. California Coop. Oceanic Fish. Inv. 21:121–131 (1980).

    Google Scholar 

  • Aoki, M., Kaneko, T., Katoh, F., Hasegawa, S., Tsutsui, N., Aida, K. Intestinal water absorption through aquaporin 1 expressed in the apical membrane of mucosal epithelial cells in seawater-adapted Japanese eel. J. Exp. Biol. 206:3495–3505 (2003).

    PubMed  Google Scholar 

  • Babiker, M.M., Ibrahim, H. Studies on the biology of reproduction in the ciclid Tilapia nilotica (L.): effects of steroid and trophic hormones on ovulation and ovarian hydration. J. Fish Biol. 15:21–30 (1979).

    CAS  Google Scholar 

  • Balon, E.K. Early ontogeny of Labeotropheus Ahl, 1927 (Mbuna, Cichlidae, Lake Malawi) with a discussion on advanced protective styles in fish reproduction and development. Environ. Biol. Fish. 2:147–176 (1977).

    Google Scholar 

  • Blank, M.E., Ehmke, H. Aquaporin-1 and HCO3-Cltransporter-mediated transport of CO2across the human erythrocyte membrane. J. Physiol. 550:419–429 (2003).

    PubMed  CAS  Google Scholar 

  • Bolamba, D., Patiño, R., Yoshizaki, G., Thomas, P. Changes in homologous and heterologous gap junction contacts during maturation-inducing hormone-dependent meiotic resumption in ovarian follicles of Atlantic croaker. Gen. Comp. Endocrinol. 131:291–295 (2003).

    PubMed  CAS  Google Scholar 

  • Borgnia, M., Nielsen, S., Engel, A., Agre, P. Cellular and molecular biology of the aquaporin water channels. Annu. Rev. Biochem. 68:425–458 (1999).

    PubMed  CAS  Google Scholar 

  • Brooks, H.L., Regan, J.W., Yool, A.J. Inhibition of aquaporin-1 water permeability by tetraethylamonium: involvement of the E pore region. Mol. Pharmacol. 57:1021–1026 (2000).

    PubMed  CAS  Google Scholar 

  • Bulling, A., Berg, F.D., Berg, U., Duffy, D.M., Stouffer, R.L., Ojeda, S.R., Gratzl, M., Mayerhofer, A. Identification of an ovarian voltage-activated Na+-channel type: hints to involvement in luteolysis. Mol. Cell. Endocrinol. 14:1064–1974 (2000).

    CAS  Google Scholar 

  • Byrne, B.M., Gruber, M., Ab, C. The evolution of egg yolk proteins. Prog. Biophys. Mol. Biol. 53:33–69 (1989).

    PubMed  CAS  Google Scholar 

  • Carnevali, O., Mosconi, G., Roncarati, A., Belvedere, P., Romano, M., Limatola, E. Changes in the electrophoretic pattern of yolk proteins during vitellogenesis in the gilthead sea bream, Sparus aurata L. Comp. Biochem. Physiol. 103B:955–962 (1992).

    CAS  Google Scholar 

  • Carnevali, O., Mosconi, G., Roncarati, A., Belvedere, P., Limatola, E., Polzonetti-Magni, A.M. Yolk protein changes during oocyte growth in European sea bass Dicentrarchus labrax L. J. Appl. Ichthyol. 9:175–184 (1993).

    CAS  Google Scholar 

  • Carnevali, O., Carletta, R., Cambi, A., Vita, A., Bromage, N. Yolk formation and degradation during oocyte maturation in seabream Sparus aurata. Involvement of two lysosomal proteinases. Biol. Reprod. 60:140–146 (1999a).

    Google Scholar 

  • Carnevali, O., Centonze, F., Brooks, S., Marota, I., Sumpter, J.P. Molecular cloning and expression of ovarian cathepsin D in sea bream Sparus aurata. Biol. Reprod. 61:785–791 (1999b).

    PubMed  CAS  Google Scholar 

  • Carnevali, O., Mosconi, G., Cardinali, M., Meiri, I., Polzonetti-Magni, A. Molecular components related to egg viability in the gilthead seabream, Sparus aurata. Mol. Reprod. Dev. 58:330–335 (2001a).

    Google Scholar 

  • Carnevali, O., Mosconi, G., Cambi, A., Ridolfi, S., Zanuy, S., Polzonetti-Magni, A.M. Changes of lysosomal enzyme activities in sea bass (Dicentrarchus labrax) eggs and developing embryos. Aquaculture 202:249–256 (2001b).

    CAS  Google Scholar 

  • Cerdà, J., Petrino, T.R., Wallace, R.A. Functional heterologous gap junctions in Fundulus ovarian follicles maintain meiotic arrest and permit hydration during oocyte maturation. Dev. Biol. 160:228–235 (1993).

    PubMed  Google Scholar 

  • Cerdà, J., Selman, K., Wallace, R.A. Observations on oocyte maturation and hydration in vitro in the black sea bass, Centropristis striata (Serranidae). Aquat. Living Res. 9:325–335 (1996).

    Google Scholar 

  • Chang, X., Patiño, R., Yoshizaki, G., Thomas, P., Lee, V.H. Hormonal regulation and cellular distribution of connexin 32.2 and connexin 32.7 RNAs in the ovary of Atlantic croaker. Gen. Comp. Endocrinol. 120:146–156 (2000).

    Google Scholar 

  • Chen, Y.-N., Hsieh, S.-L., Kuo, C.M. Changes in oocyte and blood plasma osmotic components of ayu, Plecoglossus altivelis Temminck and Schlegel during oocyte maturation. Aquacult. Res. 34:859–867 (2003).

    Google Scholar 

  • Cho, W.L., Tsao, S.M., Hays, A.R., Walter, R., Chen, J.S., Snigirevskaya, E.S., Raikhel, A.S. Mosquito cathepsin B-like protease involved in embryonic degradation of vitellin is produced as a latent extraovarian precursor. J. Biol. Chem. 274:13311–13321 (1999).

    PubMed  CAS  Google Scholar 

  • Choi, C.Y., Takashima, F. Molecular cloning and hormonal control in the ovary of connexin 31.5 mRNA and correlation with the appearance of oocyte maturational competence in red seabream. J. Exp. Biol. 203:3299–3306 (2000).

    PubMed  CAS  Google Scholar 

  • Chrispeels, M.J., Morillon, R., Maurel, C., Gerbeau, P., Kjellbom, P., Johansson, I. Aquaporins of plants: structure, function, regulation, and role in plant water relations. In: Hohmann, S., Nielsen, S. Agre, P. (eds.), Aquaporins. Current Topics in Membranes, Vol. 51. Academic Press, San Diego, CA, pp. 277–334 (2001).

    Google Scholar 

  • Chuda, H., Matsuyama, M., Hara, Y., Yada, T., Matsuura, S. Relationship between post-ovulation time and fertilization rate of eggs in artificial insemination of tiger puffer, Takifugu rubripes. Nippon Suisan Gakkaishi 64:993–998 (1998).

    CAS  Google Scholar 

  • Cionna, C., Verdecchia, V., Di Rosa, C., Cardinalli, M., Carnevali, O. Expression of cathepsins B, D and L genes and their enzymatic activities during oocyte maturation in Danio rerio. Proc. 5th Int. Symp. Fish Endocrinol, p. 89 (2004).

    Google Scholar 

  • Clemens, H.P., Grant, F.B. Gonadal hydration of carp (Cyprinus carpio) and goldfish (Carassius auratus) after injections of pituitary extracts. Zoologica 49:193–210 (1964).

    CAS  Google Scholar 

  • Craik, J.C.A. Levels of phosphoprotein in the eggs and ovaries of some fish species. Comp. Biochem. Physiol. 72B:507–512 (1982).

    CAS  Google Scholar 

  • Craik, J.C.A., Harvey, S.M. Biochemical changes occurring during final maturation of eggs of some marine and freshwater teleosts. J. Fish. Biol. 24:599–610 (1984).

    CAS  Google Scholar 

  • Craik, J.C.A., Harvey, S.M. Phosphorus metabolism and water uptake during final maturation of ovaries of teleosts with pelagic and demersal eggs. Mar. Biol. 90:285–289 (1986).

    CAS  Google Scholar 

  • Craik, J.C.A., Harvey, S.M. The causes of buoyancy in eggs of marine teleosts. J. Mar. Biol. Ass. UK 67:169–182 (1987).

    Google Scholar 

  • Cutler, C.P., Cramb, G. Branchial expression of an aquaporin 3 (AQP3) homologue is downregulated in the European eel, Anguilla anguilla following seawater acclimation. J. Exp. Biol. 205:2643–2651 (2002).

    PubMed  CAS  Google Scholar 

  • Deen, P.M.T., van Balkom, B.W.M., Kamsteeg, E.-J. Routing of the aquaporin-2 water channel in health and disease. Eur. J. Cell Biol. 79:523–530 (2000).

    PubMed  CAS  Google Scholar 

  • Eldridge, M.B., Joseph, J.D., Taberski, K.M., Seaborn, G. Lipid and fatty acid composition of the endogeneous energy sources of striped bass (Morone saxatilis) eggs. Lipids 18:510–513 (1983).

    PubMed  CAS  Google Scholar 

  • Fabra, M., Cerdà, J. Ovarian cysteine proteinases in the teleost Fundulus heteroclitus: molecular cloning and gene expression during vitellogenesis and oocyte maturation. Mol. Reprod. Dev. 67:282–294 (2004).

    PubMed  CAS  Google Scholar 

  • Fabra, M., Raldúa, D., Power, D.A., Deen, P.M.T., Cerdà, J. Marine fish egg hydration is aquaporinmediated. Science 307:545 (2005).

    PubMed  CAS  Google Scholar 

  • Fabra, M., Raldúa, D., Bozzo, M.G., Deen, P.M.T., Lubzens, E., Cerdà, J. Yolk proteolysis and aquaporin-1o play essential roles to regulate fish oocyte hydration during meiosis resumption. Dev. Biol. 295:250–262 (2006).

    PubMed  CAS  Google Scholar 

  • Fagotto, F. Yolk degradation in tick eggs: I. Occurrence of a cathepsin L-like acid proteinase in yolk spheres. Arch. Insect Biochem. Physiol. 14:217–235 (1990a).

    PubMed  CAS  Google Scholar 

  • Fagotto, F. Yolk degradation in tick eggs: II. Evidence that cathepsin L-like proteinase is stored as a latent, acid-activatable proenzyme. Arch. Insect Biochem. Physiol. 14:237–252 (1990b).

    PubMed  CAS  Google Scholar 

  • Fagotto, F., Maxfield, F.R. Yolk platelets in Xenopus oocytes maintain an acidic internal pH which may be essential for sodium accumulation. J. Cell Biol. 125:1047–1056 (1994a).

    PubMed  CAS  Google Scholar 

  • Fagotto, F., Maxfield, F.R. Changes in yolk platelet pH during Xenopus laevis development correlate with yolk utilization. A quantitative confocal microscopy study. J. Cell Sci. 107:3325–3337 (1994b).

    PubMed  CAS  Google Scholar 

  • Finn, R.N., Rønnestad, I., Fyhn, H.J. Respiration, nitrogen and energy metabolism of developing yolk-sac larvae of Atlantic halibut (Hippoglossus hippoglossus L.). Comp. Biochem. Physiol. 111A:647–671 (1995).

    Google Scholar 

  • Finn, R.N., Ostby, G.C., Norberg, B., Fyhn, H.J. In vivo oocyte hydration in Atlantic halibut (Hippoglossus hipoglossus): proteolytic liberation of free amino acids, and ion transport, are driving forces for osmotic water influx. J. Exp. Biol. 205:211–224 (2002a).

    PubMed  CAS  Google Scholar 

  • Finn, R.N., Wamboldt, M., Fyhn, H.J. Differential processing of yolk proteins during hydration in marine fishes (Labridae) that spawn benthic and pelagic eggs. Mar. Ecol. Prog. Ser. 237:217–226 (2002b).

    CAS  Google Scholar 

  • Flegler, C. Electron microscopic studies on the development of the chorion of the viviparous teleost Dermogenys pusillus (Hemirhamphidae). Cell Tissue Res. 179:255–270 (1977).

    PubMed  CAS  Google Scholar 

  • Fugelli, K., Thoroed, S.M. Taurine and volume regulation in fish cells. In: Pasantes-Morales, H., Martin, D.L., Shain, W., del Río, R.M. (eds.), Taurine: Functional Neurochemistry, Physiology and Cardiology. Wiley-Liss, New York, pp. 481–488 (1990).

    Google Scholar 

  • Fujiyoshi, Y., Mitsuoka, K., de Groot, B.L., Philippsen, A., Grubmüller, H., Agre, P., Engel, A. Structure and function of water channels. Curr. Opin. Struct. Biol. 12:509–515 (2002).

    PubMed  CAS  Google Scholar 

  • Fulton, T.W. The comparative fecundity of sea fishes. Fish. Board Scotland Ann. Rep. 9:243–268 (1891).

    Google Scholar 

  • Fulton, T.W. On the growth and maturation of the ovarian eggs of teleostean fishes. Fish. Board Scotland Ann. Rep. 16:88–134 (1898).

    Google Scholar 

  • Fyhn, H.J., Serigstad, B. Free amino acids as energy substrate in developing eggs and larvae of the cod Gadus morhua. Mar. Biol. 96:335–341 (1987).

    CAS  Google Scholar 

  • Fyhn, H.J. First feeding of marine fish larvae: are free amino acids the source of energy? Aquaculture 80:111–120 (1989).

    Google Scholar 

  • Fyhn, H.J., Finn, R.N., Reith, M., Norberg, B. Yolk protein hydrolysis and oocyte free amino acids as key features in the adaptative evolution of teleost fishes to seawater. Sarsia 84:451–456 (1999).

    Google Scholar 

  • Geck, P., Heinz, E. The Na-K-2Cl cotransport system. J. Membr. Biol. 91:97–105 (1986).

    PubMed  CAS  Google Scholar 

  • Gerhartz, B., Kolb, H. J., Wittmann, J. Proteolytic activity in the yolk sac membrane of quail eggs. Comp. Biochem. Physiol. 123A:1–8 (1999).

    CAS  Google Scholar 

  • Greeley, M.S., Calder, D.R., Wallace, R.A. Changes in teleost yolk proteins during oocyte maturation: correlation of yolk proteolysis with oocyte hydration. Comp. Biochem. Physiol. 84B:1–9 (1986).

    CAS  Google Scholar 

  • Greeley, M.S., Hols, H., Wallace, R.A. Changes in size, hydration and low molecular weight osmotic effectors during meiotic maturation of Fundulus oocytes in vivo. Comp. Biochem. Physiol. 100A:639–647 (1991).

    Google Scholar 

  • Harries, W.E.C., Akhavan, D., Miercke, L.J.W., Khademi, S., Stroud, R.M. The channel architechture of aquaporin 0 at a 2.2-Å resolution. Proc. Natl. Acad. Sci. USA 101:14045–14050 (2004).

    Google Scholar 

  • Hasegawa, T., Tanii, H., Suzuki, M., Tanaka, S. Regulation of water absorption in the frog skins by two vasotocin-dependent water-channel aquaporins, AQP-h2 and AQP-h3. Endocrinology 144:4087–4096 (2003).

    PubMed  CAS  Google Scholar 

  • Hasilik, A. The early an late processing of lysosomal enzymes: proteolysis and compartmentation. Experientia 48:130–151 (1992).

    PubMed  CAS  Google Scholar 

  • Hiramatsu, N., Ichikawa, N., Fukada, H., Fujita, T., Sullivan, C.V., Hara, A. Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids. J. Exp. Zool. 292:11–25 (2002a).

    PubMed  CAS  Google Scholar 

  • Hiramatsu, N., Hara, A., Hiramatsu, K., Fukada, H., Weber, G.M., Denslow, N.D., Sullivan, C.V. Vitellogenin-derived yolk proteins of white perch, Morone americana: purification, characterization, and vitellogenin-receptor binding. Biol. Reprod. 67:655–667 (2002b).

    PubMed  CAS  Google Scholar 

  • Hirata, T., Kaneko, T., Ono, T., Nakazato, T., Furukawa, N., Hasegawa, S., Wakabayashi, S., Shigekawa, M., Chang, M.-H., Romero, M.F., Hirose, S. Mechanism of acid adaptation of a fish living in a pH 3.5 lake. Am. J. Physiol. Regul. Integr. Comp. Physiol. 284:R1199–R1212 (2003).

    Google Scholar 

  • Hirose, K., Hirano, T., Ishida, R. Effects of salmon gonadotropin on ovulation in thye ayu, Plecoglossus altivelis, with special reference to water balance. Comp. Biochem. Physiol. 47A:283–289 (1974).

    Google Scholar 

  • Hirose, K., Ishida, R. Effects of cortisol and human chorionic gonadotropin (hCG) on ovulation in ayu, Plecoglossus altivelis (Temminck and Schlegel) with special respect to waterf and ion balance. J. Fish Biol. 6:557–564 (1974).

    CAS  Google Scholar 

  • Hirose, K. Endocrine control of ovulation in medaka (Oryzias latipes) and ayu (Plecoglossus altivelis). J. Fish. Res. Board Can. 33:989–994 (1976).

    CAS  Google Scholar 

  • Hoffman, E.K. Role of separate K+and Clchannels and of Na/Cl cotransport in volume regulation in Ehrlich cells. Fed. Proc. 44:2513–2519 (1985).

    Google Scholar 

  • Hølleland, T., Fyhn, H.J. Osmotic properties of eggs of the herring Clupea harengus. Mar. Biol. 91:377–383 (1986).

    Google Scholar 

  • Holm, L.M., Klaerke, D.A., Zeuthen, T. Aquaporin 6 is permeable to glycerol and urea. Eur. J. Physiol. 448:181–186 (2004).

    CAS  Google Scholar 

  • Iwamatsu, T., Ohta, T., Oshima, E., Noriyoshi, S. Oogenesis in the medaka Oryzias latipes –stages of oocyte development. Zool. Sci. 5:353–373 (1988).

    Google Scholar 

  • Iwamatsu, T., Takahashi, S.Y., Oh-ishi, T., Yokochi, T., Maeda, H. Changes in electrophoretic patterns of oocyte proteins during oocyte maturation in Oryzias latipes. Dev. Growth Differ. 34:173–179 (1992).

    Google Scholar 

  • Jahn, T.P., Møller, A.L.B., Zeuthen, T., Holm, L.M., Klaerke, D.A., Mohsin, B., Kühlbrandt, W., Schjoerring, J.K. Aquaporin homologues in plants and mammals transport ammonia. FEBS Lett. 574:31–36 (2004).

    PubMed  CAS  Google Scholar 

  • Kamsteeg, E.J., Heijnen, I., van Os, C.H., Deen, P.M.T. The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers. J. Cell Biol. 151:919–930 (2000).

    PubMed  CAS  Google Scholar 

  • Kestemont, P., Cooremans, J., Abi-Ayad, A., Mélard, C. Cathepsin L in eggs and larvae of perch Perca fluviatilis: variations with developmental stage and spawning period. Fish Physiol. Biochem. 21:59–64 (1999).

    CAS  Google Scholar 

  • King, P.A., Goldstein, L. Organic osmolytes and cell volume regulation in fish. Mol. Physiol. 4:53–66 (1983).

    CAS  Google Scholar 

  • Kjesbu, O.S., Kryvi, H. Oogenesis in cod, Gadus morhua L., studied by light and electron microscopy. J. Fish Biol. 34:735–746 (1989).

    Google Scholar 

  • Kjesbu, O.S., Kryvi, H. A histological examination of oocyte final maturation in cod (Gadus morhua). In: Walther, B.T., Fyhn, H.J. (eds.), Physiological and Biochemical Aspects of Fish Development. University of Bergen, Oslo, pp. 86–92 (1993).

    Google Scholar 

  • Kjørsvik, E., Mangor-Jensen, A., Holmefjord, I. Egg quality in fishes. Adv. Mar. Biol. 26:71–113 (1990).

    Google Scholar 

  • Kwon, J.Y., Prat, F., Randall, C., Tyler, C. Molecular characterization of putative yolk processing enzymes and their expression during oogenesis and embryogenesis in rainbow trout (Oncorhynchus mykiss). Biol. Reprod. 65:1701–1709 (2001).

    PubMed  CAS  Google Scholar 

  • LaFleur, G.J., Jr., Thomas, P. Evidence for a role of Na+, K+-ATPase in the hydration of atlantic croaker and spotted seatrout oocytes during final maturation. J. Exp. Biol. 258:126–136 (1991).

    CAS  Google Scholar 

  • LaFleur, G.J., Jr., Byrne, B.M., Kanungo, J., Nelson, L.D., Greenberg, R.M., Wallace, R.A. Fundulus heteroclitus vitelllogenin: the deduced primary structure of a piscine precursor to noncrystalline, liquid-phase yolk protein. J. Mol. Evol. 41:505–521 (1995a).

    Google Scholar 

  • LaFleur, G.J., Jr., Byrne, B.M., Haux, C., Greenberg, M.A., Wallace, R.A. Liver-derived cDNAs: vitellogenin and vitelline envelope proteins precursors (choriogenins). Proc. 5th Int. Symp. Reprod. Physiol. Fish (1995b).

    Google Scholar 

  • LaFleur, G.J., Jr., Raldúa, D., Fabra, M., Carnevali, O., Denslow, N., Wallace, R.A., Cerdà, J. Derivation of major yolk proteins from parental vitellogenins and alternative processing during oocyte maturation in Fundulus heteroclitus. Biol. Reprod.73:815–824 (2005).

    Google Scholar 

  • Lang, F., Busch, G.L., Volkl, H. The diversity of volume regulatory mechanisms. Cell Physiol. Biochem. 8:1–45 (1998).

    PubMed  CAS  Google Scholar 

  • Lange, R.H. Lipoprotein crystals in the yolk platelet of a teleost, Pelvicachromis pulcher (Cichlidae). Cell Tissue Res. 209:511–513 (1980).

    PubMed  CAS  Google Scholar 

  • Lignot, J.H., Cutler, C.P. Hazon, N., Cramb, G. Immunolocalization of aquaporin-3 in the gill and the gastrointestinal tract of the European eel Anguilla anguilla (L.). J. Exp. Biol. 205:2653–2663 (2002).

    Google Scholar 

  • Ling, G.N. The physical state of potassium ion in the living cell. Scanning Microsc. 4:737–750 (1990).

    PubMed  CAS  Google Scholar 

  • Liu, Z., Shen, J., Carbrey, J.M., Mukhopadhyay, R., Agre, P., Rosen, B. Arsenite transport by mammalian aquaglyceroporins AQP7 and AQP9. Proc. Natl. Acad. Sci. USA 99:6053–6058 (2002).

    PubMed  CAS  Google Scholar 

  • Long, J.A. The Rise of Fishes. 500 Millions Years of Evolution. The John Hopkins University Press, Baltimore (1996).

    Google Scholar 

  • Ma, T., Yang, B., Verkman, A.S. cDNA cloning of a functional water channel from toad urinary bladder epithelium. Am. J. Physiol. 271:C1699–1704 (1996).

    PubMed  CAS  Google Scholar 

  • Maarstoel, M.J., Fyhn, H.J., Kjesbu, O.S., Solemdal, P. Free amino acid content as a potential criterion of egg quality in Atlantic cod (Gadus morhua). In: Walther, B.T., Fyhn, H.J. (eds.) Physiological and Biochemical Aspects of Fish Development. University of Bergen, Bergen, pp. 99–103 (1993).

    Google Scholar 

  • Mallya, S., Partin, J.S., Valdizan, M.C., Lennarz, W.J. Proteolysis of the major yolk glycoproteins is regulated by acidification of the yolk platelets in sea urchin embryos. J. Cell Biol. 117:1211–1221 (1992).

    PubMed  CAS  Google Scholar 

  • Mangor-Jensen, A., Waiwood, K.G., Peterson, R.H. Water balance in eggs of striped bass (Morone saxatilis). J. Fish Biol. 43:345–353 (1993).

    Google Scholar 

  • Manley, G.T., Binder D.K., Papadopoulos, M.C., Verkman, A.S. New insights into water transport and edema in the central nervous system from phenotype analysisn of aquaporin-4 null mice. Neuroscience 129:983–991 (2004).

    PubMed  CAS  Google Scholar 

  • Marshall, W.S. Gonadotropin stimulation of K+secretion and Na+absorption by brook trout (Salvelinus fontinalis) sperm duct epithelium. Gen. Comp. Endocrinol. 75:118–128 (1989).

    PubMed  CAS  Google Scholar 

  • Masuda, K., Iuchi, I., Iwamori, M., Nagai, Y., Yamagami, K. Presence of a substance crossreacting with cortical alveolar material in “yolk vesicles” of growing oocytes of Oryzias latipes. J. Exp. Zool. 238:261–265 (1986).

    CAS  Google Scholar 

  • Matsubara, T., Sawano, K. Proteolytic cleavage of vitellogenin and yolk proteins during vitellogenin uptake and oocyte maturation in barfin flounder (Verasper moseri). J. Exp. Zool. 272:34–45 (1995).

    CAS  Google Scholar 

  • Matsubara, T., Adachi, S., Ijiri, S., Yamauchi, K. Change of lipovitellin during in vitro oocyte maturation in Japanese flounder Paralichthys olivaceus. Fish. Sci. 61:478–481 (1995).

    Google Scholar 

  • Matsubara, T., and Koya, Y. Course of proteolytic cleavage in three classes of yolk proteins during oocyte maturation in barfin flounder Verasper moseri, a marine teleost spawning pelagic eggs. J. Exp. Zool. 278:189–200 (1997).

    CAS  Google Scholar 

  • Matsubara, T., Ohkubo, N., Andoh, T., Sullivan, C. V., Hara, A. Two forms of vitellogenin, yielding two distinct lipovitellins, play different roles during oocyte maturation and early development of barfin flounder, Verasper moseri, a marine teleost that spawns pelagic eggs. Dev. Biol. 213:18–32 (1999).

    PubMed  CAS  Google Scholar 

  • McPherson, R., Greeley, M.S., Jr., Wallace, R.A. The influence of yolk protein proteolysis on hydration in the oocytes of Fundulus heteroclitus. Develop. Growth Differ. 31:475–483 (1989).

    Google Scholar 

  • Mellinger, J. La flottabilité des oeufs des teléostéens. L’Anné Biologique 33:117–138 (1994).

    Google Scholar 

  • Milroy, T.H. The physical and chemical changes taking plaice in the ova of certain marine teleosteans during maturation. Fish Board Scot. 16th Ann. Rep. 16 Part 3:135–152 (1898).

    Google Scholar 

  • Morishita, Y., Sakube, Y., Sasaki, S., Ishibashi, K. Molecular mechanisms and drug development in aquaporin water channel diseases: aquaporin superfamily (superaquaporins): expansion of aquaporins restricted to multicellular organisms. J. Pharmacol. Sci. 96:276–279 (2004).

    PubMed  CAS  Google Scholar 

  • Murakami, M., Iuch, I., Yamagami, K. Yolk phosphoprotein metabolism during early development of the fish, Oryzias latipes. Develop Growth Differ. 32:619–627 (1990).

    CAS  Google Scholar 

  • Nardelli, D., von-het Ship, F.D., Gerber-Huber, S., Haefliger, J.A., Gruber, M., Ab, G., Wahli, W. Comparison of the organization and fine structure of a chicken and a Xenopus laevis vitellogenin gene. J. Biol. Chem. 262:15337–15385 (1987).

    Google Scholar 

  • Nelson, N., Harvey, W.R. Vacuolar and plasma membrane proton-adenosinetriphosphatases. Physiol. Rev. 79:361–385 (1999).

    PubMed  CAS  Google Scholar 

  • Nielsen, S., Smith, B.L., Christensen, E.I., Agre, P. Distribution of the aquaporin CHIP in secretory and resorptive epithelia and capillary endothelia. Proc. Natl. Acad. Sci. USA 90:7275–7279 (1993a).

    PubMed  CAS  Google Scholar 

  • Nielsen, S., Smith, B.L., Christensen, E.I., Knepper, M.A., Agre, P. CHIP28 water channels are localized in constitutively water-permeable segments of the nephron. J. Cell Biol. 120:371–383 (1993b).

    PubMed  CAS  Google Scholar 

  • Nissling, A., Westin, L. Egg buoyancy of Baltic cod (Gadus morhua) and its implications for cod stock fluctuations in the Baltic. Mar. Biol. 111:33–35 (1991).

    Google Scholar 

  • Nissling, A., Kryvi, H., Vallin, L. Variations in egg buoyancy of Baltic cod Gadus morhua and its implications for egg survival in prevailing conditions in the Baltic sea. Mar. Ecol. Prog. Ser. 110:67–74 (1994).

    Google Scholar 

  • Nissling, A., Müller, A., Hinrichsen, H.-H. Specific gravity and vertical distribution of sprat eggs in the Baltic sea. J. Fish Biol. 63:280–299 (2003).

    Google Scholar 

  • Nordin, J.H., Beaudoin, E.L., Liu, X. Identification of yolk granules in Blatella germanica eggs coincident with proteolytic processing of vitellin. Arch. Insect Biochem. Physiol. 18:177–192 (1991).

    CAS  Google Scholar 

  • Ohkubo, N., Matsubara, T. Sequential utilization of free amino acids, yolk proteins and lipids in developing eggs and yolk-sac larvae of barfin flounder Verasper moseri. Mar. Biol. 140:187–196 (2002).

    CAS  Google Scholar 

  • Okumura, H., Kayaba, T., Kazeto, Y., Hara, A., Adachi, S., Yamauchi, K. Changes in the electrophoretic patterns of lipovitellin during oocyte development in the Japanese eel Anguilla japonica. Fish Sci. 61:529–530 (1995).

    Google Scholar 

  • Oshiro, T., Hibiya, T. Water absorption of oocytes in the plaice Limanda yokohamae during meiotic maturation and its role in rupturing follicles. Bull. Jpn. Soc. Sci. Fish. 47:835–841 (1981a).

    Google Scholar 

  • Oshiro, T., Hibiya, T. Relationship of yolk globules fusion to oocyte water absorption in the plaice Limanda yokohamae during meiotic maturation. Bull. Jpn. Soc. Sci. Fish. 47:1123–1130 (1981b).

    Google Scholar 

  • Oshiro, T., Hibiya, T. In vitro yolk globule fusion in the oocytes of the plaice Limanda yokohamae. Bull. Jpn. Soc. Sci. Fish. 48:181–186 (1982).

    Google Scholar 

  • Patiño, R., Yoshizaki, G., Thomas, P., Kagawa, H. Gonadotropic control of ovarian follicle maturation: the two stage concept and its mechanisms. Comp. Biochem. Physiol. 129B:427–439 (2001).

    Google Scholar 

  • Pillay, C.S., Elliot, E., Dennison, C. Endolysosomal proteolysis and its regulation. Biochem. J. 363:417–429 (2002).

    PubMed  CAS  Google Scholar 

  • Podrabsky, J.E., Carpenter, J.F., Hand, S.C. Survival of water stress in annual fish embryos: dehydration avoidance and egg envelope amyloid fibers. Am. J. Physiol. Regul. Integr. Comp. Physiol. 280:R123–R131 (2001).

    PubMed  CAS  Google Scholar 

  • Postlethwait, J.H., Woods, I.G., Ngo-Hazelett, P., Yan Y.L., Kelly, P.D., Chu, F., Huang, H., Hill-Force, A., Talbot, W.S. Zebrafish comparative genomics and the origins of vertebrate chromosomes. Genome Res. 10:1890–1902 (2000).

    PubMed  CAS  Google Scholar 

  • Postlethwait, J., Amores, A., Cresko, W., Singer, A., Yan, Y.L. Subfunction partitioning, the teleost radiation and the annotation of the human genome. Trends Genet. 20:481–490 (2004).

    PubMed  CAS  Google Scholar 

  • Potts, W.T., Rudy, P.P. Water balance in the egg of the Atlantic salmon, Salmo salar. J. Exp. Biol. 50:223–237 (1969).

    PubMed  CAS  Google Scholar 

  • Preston, G.M., Carroll, T.P., Guggino, W.B., Agre, P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256:385–387 (1992).

    PubMed  CAS  Google Scholar 

  • Preston, G.M., Jung, J.S., Guggino, W.B., Agre, P. The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel. J. Biol. Chem. 268:17–20 (1993).

    PubMed  CAS  Google Scholar 

  • Preston, G.M. Cloning gene family members using the polymerase chain reaction with degenerate oligonucleotide primers. Meth. Mol. Biol. 69:97–113 (1997).

    CAS  Google Scholar 

  • Raldúa, D., Fabra, M., Bozzo, M.G., Weber, E., Cerdà, J. Cathepsin B-mediated yolk protein degradation during killifish oocyte maturation is blocked by a H+-ATPase inhibitor: effects on the hydration mechanism. Am. J. Physiol. Regul. Integr. Comp. Physiol. 290:R456–R466 (2006).

    PubMed  Google Scholar 

  • Reith, M., Munholland, J., Kelly, J., Finn, R.N., Fyhn, H.J. Lipovitellins derived from two forms of vitellogenin are differentially processed during oocyte maturation in haddock (Melanogrammus aeglefinus). J. Exp. Zool. 291:58–67 (2001).

    PubMed  CAS  Google Scholar 

  • Riis-Vestergaard, J. Energy density of marine pelagic eggs. J. Fish Biol. 60:1511–1528 (2002).

    Google Scholar 

  • Rogers, S., Wells, R., Rechsteiner, M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234:364–368 (1986).

    PubMed  CAS  Google Scholar 

  • Rønnestad, I., Fyhn, H.J., Gravningen, K. The importance of free amino acids to the energy metabolism of eggs and larvae of turbot (Scophthalmus maximus). Mar. Biol. 114:517–524 (1992).

    Google Scholar 

  • Rønnestad, I., Groot, E.P., Fyhn, H.J. Compartmental distribution of free amino acids and protein in developing yolk-sac larvae of Atlantic halibut (Hippoglossus hippoglossus). Mar. Biol. 116:349–354 (1993).

    Google Scholar 

  • Rønnestad, I., Fyhn, H.J. Metabolic aspects of free amino acids in developing marine fish eggs and larvae. Rev. Fish. Sci. 1:239–259 (1993).

    Google Scholar 

  • Russell, F.S. The eggs and planktonic stages of British marine fishes. Academic Press, London (1976).

    Google Scholar 

  • Santos, C.R.A., Estevao, M.D., Fuentes, J., Cardoso, J.C.R., Fabra, M., Passos, A.L., Detmers, F.J., Deen, P.M.T., Cerdà, J., Power, D.M. Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus): function and tissue distribution. J. Exp. Biol. 207:1217–1227 (2004).

    PubMed  CAS  Google Scholar 

  • Selman, K., Wallace, R.A. Oocyte growth in the sheepshead minnow: uptake of exogenous proteins by vitellogenic oocytes. Tissue Cell 14:555–571 (1982).

    PubMed  CAS  Google Scholar 

  • Selman, K., Wallace, R.A. Gametogenesis in Fundulus heteroclitus. Am. Zool. 26:173–192 (1986).

    Google Scholar 

  • Selman, K., Wallace, R.A., Barr. V. Oogenesis in Fundulus heteroclitus IV. Yolk-vesicle formation. J. Exp. Zool., 239:277–288 (1986).

    Google Scholar 

  • Selman, K., Wallace, R.A., Barr, V. Oogenesis in Fundulus heteroclitus V. The relationship of yolk vesicles and cortical alveoli. J. Exp. Zool. 246:42–56 (1988).

    CAS  Google Scholar 

  • Selman, K., Wallace, R.A. Cellular aspects of oocyte growth in teleosts. Zool. Sci. 6:211–231 (1989).

    Google Scholar 

  • Selman, K., Wallace, R.A., Sarka, A., Qi, X. Stages of oocyte development in the zebrafish, Brachydanio rerio. J. Morphol. 218:203–224 (1993).

    Google Scholar 

  • Selman, K., Wallace, R.A., Cerdà, J. Bafilomycin A1 inhibits proteolytic cleavage and hydration but not yolk crystal disassembly and meiosis during maturation of sea bass oocytes. J. Exp. Zool. 290:265–278 (2001).

    PubMed  CAS  Google Scholar 

  • Seoka, M., Yamada, S., Iwata, Y., Yanagisawa, T., Nakagawa, T., Kumai, H. Differences in the biochemical content of buoyant and non-buoyant eggs of the Japanese eel, Anguilla japonica. Aquaculture 216:355–362 (2003).

    Google Scholar 

  • Shi, L.B., Verkman, A.S. Selected cysteine point mutations confer mercurial sensitivity to the mercurial-insensitive water channel MIWC/AQP-4. Biochemistry 35:538–544 (1996).

    PubMed  CAS  Google Scholar 

  • Sire, M.F., Babin, P.J., Vernier, J.M. Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout. J. Exp. Zool. 269:69–83 (1994).

    CAS  Google Scholar 

  • Soin, S.G. Adaptative characteristics of the structure and development of fish eggs and embryos promoting their respiration. Vestnik Moskovskogo (Moscow University Herald) (ser. 6) 1:9–31 (1964).

    Google Scholar 

  • Solemdal, P. The effect of salinity on buoyancy, size and development of flounder eggs. Sarsia 29:431–442 (1967).

    Google Scholar 

  • Solemdal, P. Transfer of Baltic flatfish to a marine environment and the long term effects on reproduction. OIKOS Suppl. 15:268–276 (1973).

    Google Scholar 

  • Stahlberg, H., Heymann, B., Mitsuoka, K., Fujiyoshi, Y., Engel, A. The aquaporin superfamily: structure and function. In: Hohmann, S., Nielsen, S., Agre, P. (eds.), Current Topics in Cell Membranes, Vol. 51. Academic Press, San Diego, pp. 39–119 (2001).

    Google Scholar 

  • Stevens, R.E. Hormone-induced spawning of striped bass for reservoir stocking. Prog. Fish Cult. 28:431–442 (1966).

    Google Scholar 

  • Sui, H., Han, B.G., Lee, J.K., Walian, P., Jap, B.K. Structural basis of water-specific transport through the AQP1 water channel. Nature. 414:872–878 (2001).

    PubMed  CAS  Google Scholar 

  • Takata, K., Matsuzaki, T., Tajika, Y. Aquaporins: water channel proteins of the cell membrane. Prog. Histochem. Cytochem. 39:1–83 (2004).

    PubMed  CAS  Google Scholar 

  • Tanii, H., Hasegawa, T., Hirakawa, N., Suzuki, M., Tanaka, S. Molecular and cellular characterization of a water-channel protein, AQP-h3, specifically expressed in the frog ventral skin. J. Membr. Biol. 188:43–53 (2002).

    PubMed  CAS  Google Scholar 

  • Taylor, M.H. Lunar synchronization of fish reproduction. Trans. Am. Fish. Soc. 113:484–493 (1984).

    Google Scholar 

  • Telfer, W.H., Anderson, L.M. Functional transformations accompanying the initiation of a terminal growth phase in the cecropia moth oocyte. Dev. Biol. 17:512–535 (1968).

    PubMed  CAS  Google Scholar 

  • Tocher, D.R., Sargent, J.R. Analysis of lipids and fatty acids in ripe roes of some northwest European marine fish. Lipids 19:492–499 (1984).

    CAS  Google Scholar 

  • Thorsen, A., Fyhn, H.J. Osmotic effectors during preovulatory swelling of marine fish eggs. Proc. 4th Int. Symp. Reprod. Pysiol. Fish 91:312–314 (1991).

    Google Scholar 

  • Thorsen, A., Fyhn, H.J., Wallace, R.A. Free amino acids as osmotic effectors for oocyte hydration in marine fishes. In: Walther, B.T., Fyhn, H.J. (eds.), Physiological and Biochemical Aspects of Fish Development. University of Bergen, Bergen, pp. 94–98 (1993).

    Google Scholar 

  • Thorsen, A., Fyhn, H.J. Final oocyte maturation in vivo and in vitro in marine fishes with pelagic eggs; yolk protein hydrolysis and free amino acid content. J. Fish Biol. 48:1195–1209 (1996).

    CAS  Google Scholar 

  • Thorsen, A., Kjesbu, O.S., Fyhn, H.J., Solemdal, P. Physiological mechanisms of buoyancy in eggs from brackish water cod. J. Fish Biol. 48:457–477 (1996).

    CAS  Google Scholar 

  • Tsukaguchi, H., Weremowicz, S., Morton, C.C., Hediger, M.A. Functional and molecular characterization of the human neutral solute channel aquaporin-9. Am. J. Physiol. Renal Phsyiol. 277:F685–F696 (1999).

    CAS  Google Scholar 

  • Uehlein, N., Lovisolo, C., Siefritz, F., Kaldenhoff, R. The tobacco aquaporin NtAQP1 is a membrane CO2pore with physiological functions. Nature 425:734–737 (2003).

    PubMed  CAS  Google Scholar 

  • Ulrich, E. Etude des ultrastructures au cours de l’ovogenèse d’un poisson téléostéen, le danio, Brachydanio rerio (Hamilton-Buchanan). J. Microsc. 8:447–478 (1969).

    Google Scholar 

  • Verkman, A.S. Lessons on renal physiology from transgenic mice lacking aquaporin water channels. J. Am. Soc. Nephrol. 10:1126–1135 (1999).

    PubMed  CAS  Google Scholar 

  • Verkman, A.S. Physiological importance of aquaporins: lessons from knockout mice. Curr. Opin. Nephrol. Hypertens. 9:517–522 (2000).

    PubMed  CAS  Google Scholar 

  • Verkman, A.S. Role of aquaporin water channels in eye function. Exp. Eye Res. 76:137–143 (2003).

    PubMed  CAS  Google Scholar 

  • Virkki, L.V., Cooper, G.J., Boron, W.F. Cloning and functional expression of a MIP (AQP0) homolog from killifish (Fundulus heteroclitus) lens. Am. J. Physiol. 281:R1994–R2003 (2001).

    CAS  Google Scholar 

  • Virkki, L.V., Franke, C., Somieski, P., Boron, W.F. Cloning and functional characterization of a novel aquaporin from Xenopus laevis oocytes. J. Biol. Chem. 277:40610–40616 (2002).

    PubMed  CAS  Google Scholar 

  • Wallace, R.A., Selman, K. Oogenesis in Fundulus heteroclitus. I. Preliminary observations on oocyte maturation in vivo and in vitro. Dev. Biol. 62:354–369 (1978).

    Google Scholar 

  • Wallace, R.A., Selman, K. Physiological aspects of oogenesis in two species of sticklebacks, Gasterosteus aculeatus L. and Apeltes quadracus (Mitchill). J. Fish Biol. 14:551–564 (1979).

    Google Scholar 

  • Wallace, R.A. Selman, K. Cellular and dynamic aspects of oocyte growth in teleosts. Am. Zool. 21:325–343 (1981).

    Google Scholar 

  • Wallace, R.A. Vitellogenesis and oocyte growth in non-mammalian vertebrates. In: Browder, L.W. (ed.), Developmental Biology, Vol. 1. Plenum Press, New York, pp. 127–177 (1985).

    Google Scholar 

  • Wallace, R.A., Begovac, P.C. Phosvitins in Fundulus oocytes and eggs. Preliminary chromatographic and electrophoretic analyses together with biological considerations. J. Biol. Chem. 260:11268–11274 (1985).

    PubMed  CAS  Google Scholar 

  • Wallace, R.A, Selman, K. Major proteins changes during vitellogenesis and maturation of Fundulus oocytes. Dev. Biol. 110:492–498 (1985).

    Google Scholar 

  • Wallace, R.A., Greeley, M.S., Jr., McPherson, R. Analytical and experimental studies on the relationship between Na+, K+, and water-uptake during volume increases associated with Fundulus oocyte maturation in vitro. J. Comp. Physiol. 162B:241–248 (1992).

    Google Scholar 

  • Walz, T., Smith, B.L., Agre, P., Engel, A. The three-dimensional structure of human erythrocyte aquaporin CHIP. EMBO J. 13:2985–2993 (1994).

    PubMed  CAS  Google Scholar 

  • Watanabe, W.O., Kuo, C-M. Water and ion balance in hydrating oocytes of the grey mullet, Mugil cephalus (L.), during hormone-induced final maturation. J. Fish Biol. 28:425–437 (1986).

    Google Scholar 

  • Wilson, R.W., Wilson, J.M., Grosell, M. Intestinal bicarbonate secretion by marine teleost fish-why and how? Biochim. Biophys. Acta 1566:182–193 (2002).

    PubMed  CAS  Google Scholar 

  • Wright, P.A., Fyhn, H.J. Ontogeny of nitrogen metabolism and excretion. In: Wright, P.A., Anderson, P.M. (eds.), Nitrogen Excretion. Fish Physiology, Vol. 20. Academic Press, San Diego, pp. 141–201 (2001).

    Google Scholar 

  • Yamahama, Y., Uto, N., Tamotsu, S., Miyata, T., Yamamoto, Y., Watabe, S., Takahashi, S.Y. In vivo activation of pro-form Bombyx cysteine protease (BCP) in silkmoth eggs: localization of yolk proteins and BCP, and acidification of yolk granules. J. Insect Physiol. 49:131–140 (2003).

    PubMed  CAS  Google Scholar 

  • Yamamoto, K. Studies on the formation of fish eggs. XI. The formation of a continuous mass of yolk and the nature of the lipids contained in it in the oocyte of the flounder, Liopsetta obscura. J. Fac. Sci. Hokkaido Univ. 8:344–351 (1957).

    Google Scholar 

  • Yamamoto, K., Yamazaki, F. Rhythm of development in the oocyte of the goldfish, Caraussius auratus. Bull. Fac. Fish. Hokkaido Univ. 12:93–110 (1961).

    Google Scholar 

  • Yamamoto, K., Oota, I. Fine structure of yolk globules in the oocyte of the zebrafish, Brachydanio rerio. Annot. Zool. Jpn. 40:20–27 (1967).

    Google Scholar 

  • Yasui, M., Kwon, T.H., Knepper, M.A., Nielsen, S., Agre, P. Aquaporin-6: an intracellular vesicle water channel protein. Proc. Natl. Acad. Sci. USA 96:5808–5813 (1999a).

    PubMed  CAS  Google Scholar 

  • Yasui, M., Hazama, A., Kwon, T.H., Nielsen, S., Guggino, W.B., Agre, P. Rapid gating and anion permeability of an intracellular aquaporin. Nature 402:184–187 (1999b).

    PubMed  CAS  Google Scholar 

  • Yool, A.J., Brokl, O.H., Pannabecker, T.L., Dantzler, W.H., Stamer, W.D. Tetraethylamonium block of water flux in aquaporin-1 channels expressed in kidney thin limbs of Henle’s loop and a kidney-derived cell line. BMC Physiology. www.biomedcentral.com/1472–6793/2/4 (2002).

  • Yoshizaki, G., Patiño, R., Thomas, P., Bolamba, D., Chang, X. Effects of maturation-inducing hormone on heterologous gap junctional coupling in ovarian follicles of Atlantic croaker. Gen. Comp. Endocrinol. 124:359–366 (2001).

    PubMed  CAS  Google Scholar 

  • Yoshizaki, N., Moriyama, A., Yonezawa, S. Purification and properties of embryonic cysteine proteinase which participates in yolk-lysis of Xenopus laevis. Comp. Biochem. Physiol. 119B:571–576 (1998).

    Google Scholar 

  • Yoshizaki, N., Soga, M., Ito, Y., Mao, K.M., Sultana, F., Yonezawa, S. Two-step consumption of yolk granules during the development of quail embryos. Develop. Growth Differ. 46:229–238 (2004).

    Google Scholar 

  • Zhu, Y., Rice, C.D., Pang, Y., Pace, M., Thomas, P. Cloning, expression, and characterization of a membrane progestin receptor and evidence it is an intermediary in meiotic maturaton of fish oocytes. Proc. Natl. Acad. Sci. USA 100:2231–2236 (2003).

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2007 Springer

About this chapter

Cite this chapter

Cerdà, J., Fabra, M., Raldúa, D. (2007). Physiological and molecular basis of fish oocyte hydration. In: Babin, P.J., Cerdà, J., Lubzens, E. (eds) The Fish Oocyte. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-6235-3_12

Download citation

Publish with us

Policies and ethics