Now showing items 1-3 of 3

    • Article

      Cortisol stimulates the size and number of mitochondrion-rich cells in the yolk-sac membrane of embryos and larvae of tilapia (Oreochromis mossambicus) in vitro and in vivo 

      FG Ayson, T Kaneko, S Hasegawa & T Hirano - Journal of Experimental Zoology, 1995 - John Wiley and Sons
      The effect of cortisol and thyroid hormones on the activity of mitochondrion-rich (MR) cells in the yolk-sac membrane of tilapia (Oreochromis mossambicus) embryos and larvae was investigated. MR cells were identified by the fluorescent mitochondrial stain DASPEI. Yolk-sac membranes from 4-day-old embryos in fresh water (FW) were incubated for 24 h in medium supplemented with cortisol, thyroxine (T4), or triiodothyronine (T3). Treatment with cortisol at 0.1 μ/ml and higher significantly increased the population of MR cells and the intensity of fluorescence compared with the control, whereas MR cell size was not affected. Treatments with T4 and T3 did not affect MR cell density, size, or intensity of fluorescence.

      Four-day-old embryos in FW were immersed for 10 days in FW supplemented with cortisol, T4, or T3. A significant increase in MR cell size was observed starting on day 3 after treatment with 100 μ/ml cortisol. Treatment with lower doses of cortisol produced increases in the cell size on later days. Density of MR cells was significantly increased only on day 9. Treatment with T4 produced inconsistent results. Treatment with T3 did not affect MR cell size or density at any time. None of the three hormones affected the intensity of fluorescence of MR cells. The stimulatory activity of cortisol on MR cells in the yolk-sac membrane suggests that cortisol, present in the yolk of tilapia embryos and larvae, may be involved in osmoregulation during the early life stages of fish.
    • Article

      Isolation, cDNA cloning, and growth promoting activity of rabbitfish (Siganus guttatus) growth hormone 

      FG Ayson, EGT de Jesus, Y Amemiya, S Moriyama, T Hirano & H Kawauchi - General and Comparative Endocrinology, 2000 - Elsevier
      We report the isolation, cDNA cloning, and growth promoting activity of rabbitfish (Siganus guttatus; Teleostei; Perciformes; Siganidae) growth hormone (GH). Rabbitfish GH was extracted from pituitary glands under alkaline conditions, fractionated by gel filtration chromatography on Sephadex G-100, and purified by high-performance liquid chromatography. The fractions containing GH were identified by immunoblotting with bonito GH antiserum. Under nonreducing conditions, the molecular weight of rabbitfish GH is about 19 kDa as estimated by SDS–PAGE. The purified hormone was potent in promoting growth in rabbitfish fry. Weekly intraperitoneal injections of the hormone significantly accelerated growth. This was evident 3 weeks after the start of the treatment, and its effect was still significant 2 weeks after the treatment was terminated. Rabbitfish GH cDNA was cloned to determine its nucleotide sequence. Excluding the poly (A) tail, rabbitfish GH cDNA is 860 base pairs (bp) long. It contained untranslated regions of 94 and 175 bp in the 5′ and 3′ ends, respectively. It has an open reading frame of 588 bp coding for a signal peptide of 18 amino acids and a mature protein of 178 amino acid residues. Rabbitfish GH has 4 cysteine residues. On the amino acid level, rabbitfish GH shows high identity (71–74%) with GHs of other perciforms, such as tuna, sea bass, yellow tail, bonito, and tilapia, and less (47–49%) identity with salmonid and carp GHs.
    • Article

      Milkfish (Chanos chanos) growth hormone cDNA cloning and mRNA expression in embryos and early larval stages. 

      EGT de Jesus, FG Ayson, Y Amemiya, S Moriyama, S Hyodo, T Hirano & H Kawauchi - Aquaculture, 2002 - Elsevier
      In an attempt to understand growth regulation in milkfish, the milkfish growth hormone (GH) and its cDNA were characterized and the expression of GH mRNA in embryos and larvae was examined by RT-PCR. The milkfish GH was purified from an alkaline extract of the pituitary by reverse-phase high-performance liquid chromatography and detected as an immuno-positive protein with anti-salmon GH serum. The complete sequence of milkfish pre-GH was determined by cDNA cloning and nucleotide sequencing. On the basis of the N-terminal amino acid analysis of the native protein, the pre-GH was found to consist of a signal peptide of 22 amino acids and a mature protein of 188 amino acids. Milkfish GH shows higher amino acid sequence identity with GHs of carps (91–94%) and salmonids (70%) than with GHs of more advanced teleosts (<60%) in good accordance with its taxonomic position in teleosts. It has five half Cys residues, four of which are at positions homologous with those of other known GHs and the extra Cys with those of carp GHs. The molecular weight of milkfish GH was estimated to be 22 kDa, which is comparable to the theoretical value. This suggests that milkfish GH is a simple protein, although it has two potential N-glycosylation sites. Semiquantitative RT-PCR showed that GH mRNA expression was relatively weak in embryos and newly hatched larvae but was already strong in 2-day old and older larvae.