Browsing by Author "Mamuris, Z."
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- Expression of the myosin light chains 1 and 2 in the developing fast muscle of gilthead sea bream (Sparus aurata)Publication . Moutou, Katerina A.; Silva, Nadia; Mamuris, Z.; Power, DeborahMyosin, the major component of striated muscle, is a complex molecule of heavy and light chains, which undergo continuous replacement to meet developmental and environmental demands. A range of myosin isoforms are expressed in early developmental stages and are of special interest as they offer information about muscle formation and function early in life. In addition, they can act as markers for the study of prenatal events with an effect on postnatal growth performance. In this study, the spatial and temporal expression of embryonic myosin light chains 1 (MLC1) and 2 (MLC2) was studied in sea bream larvae post-hatch by in situ hybridization using riboprobes.
- Molecular cloning and sequence of gilthead sea bream (Sparus aurata) alpha-skeletal actin: tissue and developmental expressionPublication . Moutou, K. A.; Socorro, Sílvia; Power, Deborah; Mamuris, Z.; Canario, Adelino V. M.In the present study, the Sparus aurata -skeletal actin was cloned from a mixed larvae complementary DNA library. The clone isolated was 1523 bp long with an open reading frame of 1134 bp coding for a 377-amino acid protein. The deduced amino acid sequence of sea bream -actin is identical to Fugu -actin-1. The expression of -actin was initiated at the onset of segmentation. In adult fish, -actin is expressed predominantly in white and red muscle.
- Molecular cloning and sequence of Sparus aurata skeletal myosin light chains expressed in white muscle: developmental expression and thyroid regulationPublication . Moutou, K. A.; Canario, Adelino V. M.; Mamuris, Z.; Power, DeborahTwo full-length cDNA clones encoding the skeletal myosin light chain 2 (MLC2; 1452 bp) and myosin light chain 3 (MLC3; 972 bp) were isolated from a cDNA library prepared from gilthead sea bream Sparus aurata larvae. The MLC2 cDNA encoded a predicted protein of 170 residues that was 79 % identical to rabbit MLC2 over the entire length and 87 % identical within the Ca2+- binding region. The deduced amino acid sequence of MLC3 was 153 residues in length and was 91 % and 69% identical to the zebrafish and rabbit MLC3, respectively. Northern blot analysis revealed that in adults both transcripts were expressed in fast white muscle only. MLC2 appeared earlier in development: MLC2 transcripts were detectable from the beginning of segmentation, whereas MLC3 transcripts did not appear until 27 h post-fertilisation. At this developmental stage, a second MLC2 transcript of 0.89 kilobase-pairs was present. MLCs exhibited a different age-related pattern of response to varied thyroidal states, which were experimentally induced by the administration of 1 mgg-1 body mass of thyroxine (T4) or triiodothyronine (T3), or 5 ng g-1 body mass of the hypothyroidal compound thiourea; MLC3 expression was not significantly affected, whereas levels of MLC2 transcripts were significantly elevated in the white muscle only of juvenile sea bream after administration of T4. Although the mechanism of thyroidal regulation of MLC expression remains unknown, the present results suggest that different regulatory mechanisms exist for different MLCs.