Expression Analysis of Cathepsin F during Embryogenesis and Early Developmental Stage in Olive Flounder (Paralichthys olivaceus)
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Cathepsins are members of the multigene family of lysosomal cysteine proteinases and have regulated function in several life processes. The potential role of cathepsin F cysteine gene was expected as protease in the yolk processing mechanism during early developmental stage, but expression analysis was unknown after fertilization. The alignment analysis showed that amino acid sequence of cathepsin F from olive flounder liver expressed sequence tag (EST) homologous to cathepsin F of other known cathepsin F sequences with 87-98% identity. In this study, we examined the gene expression analysis of cathepsin F in various tissues at variety age flounder. Tissue distribution of the cathepsin F mRNA has been shown to be ubiquitous and constitutive pattern regardless of age in each group, although derived from cDNA library using liver sample. The mRNA level of cathepsin F more increased as developmental proceed during embryogenesis and early developmental stage, especially increased in the blastula, hatching stage and 3 days post hatching (dph). As a result, it may suggest that the proteolysis of yolk proteins (YPs) has been implicated as a mechanism for nutrient supply during early larval stages in olive flounder.
Abstract
Cathepsins are members of the multigene family of lysosomal cysteine proteinases and have regulated function in several life processes. The potential role of cathepsin F cysteine gene was expected as protease in the yolk processing mechanism during early developmental stage, but expression analysis was unknown after fertilization. The alignment analysis showed that amino acid sequence of cathepsin F from olive flounder liver expressed sequence tag (EST) homologous to cathepsin F of other known cathepsin F sequences with 87-98% identity. In this study, we examined the gene expression analysis of cathepsin F in various tissues at variety age flounder. Tissue distribution of the cathepsin F mRNA has been shown to be ubiquitous and constitutive pattern regardless of age in each group, although derived from cDNA library using liver sample. The mRNA level of cathepsin F more increased as developmental proceed during embryogenesis and early developmental stage, especially increased in the blastula, hatching stage and 3 days post hatching (dph). As a result, it may suggest that the proteolysis of yolk proteins (YPs) has been implicated as a mechanism for nutrient supply during early larval stages in olive flounder.
참고문헌 (28)
- Ahn SJ, "Molecular cloning, mRNA expression and enzymatic characterization of cathepsin F from olive flounder (Paralichthys olivaceus)", Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, 154(2), pp.211~220 (2009), Elsevier BV
- Alt B, "Analysis of origin and growth of the thyroid gland in zebrafish", Dev Dyn, 235, pp.1872~1883 (2006)
- Bond JS, "Intracellular proteases", Annu Rev Biochem, 56, pp.333~364 (1987)
- Brocklehurst KB, "Cysteine proteinases", New Compr Biochem, 16, pp.39~58 (1987)
- Cardinaletti G, "Environmental and neuroendocrine control of fish reproduction", Book Chapter in Rec Adv Reprod Biol, 2010, pp.65~87 (2010)
- Carvalho L, "The yolk syncytial layer in early zebrafish delopment", Trend Cell Biol, 20, pp.586~592 (2010)
- Carnevali O, "Influence of diet on yolk protein components in sea bass, Dicentrarchus labrax", Sci Mar, 62, pp.311~318 (1998)
- Carnevali O, "Yolk formation and degradation during oocyte maturation in seabream Sparus aurata: involvement of two lysosomal proteinases", Biol Reprod, 60, pp.140~146 (1999)
- Carnevalli O, "Changes of lysosomal enzyme activities in sea bass (Dicentrarchus labrax) eggs and developing embryos", Aquac, 202, pp.249~256 (2001)
- Cho WL, "Mosquito cathepsin B-like protease involved in embryonic degradation of vitellin is produced as a latent extraovarian precursor", J Biol Chem, 274, pp.13311~13321 (1999)
- Drasdo D, "Modeling the interplay of generic and genetic mechanisms in cleavage, blastulation, and gastrulation", Dev Dyn, 219, pp.182~191 (2000)
- Fabra M, "Ovarian cysteine proteinases in the teleost Fundulus heteroclitus: molecular cloning and gene expression during vitellogenesis and oocyte maturation", Mol Reprod Dev, 67, pp.282~294 (2004)
- Hiramatsu N, "Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids", J Exp Zool, 292, pp.11~25 (2002)
- 김영옥, "Molecular cloning and characterization of cathepsin F gene from olive flounder Paralichthys Olivaceus", Genes & Genomics, 32(2), pp.137~142 (2010), 한국유전학회
- Kirschke H, "Protein Profiles (Sheterline, P ed) vol.2" (1995), Academic Press
- Kumar S, "MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment", Brief Bioinform, 5, pp.150~163 (2004)
- Kwon JY, "Molecular characterization of putative yolk processing enzymes and their expression during oogenesis and embryogenesis in rainbow trout (Oncorhynchus mykiss)", Biol Reprod, 65, pp.1701~1709 (2001)
- 1Mallya S, Partin JS, Valdizan MC, "Proteolysis of the major yolk glycoproteins is regulated by acidification of the yolk platelets in sea urchin embryos", J Cell Biol, 117, pp.1211~1221 (1992)
- McGrath ME, "The lysosomal cystein proteases", Annu Rev Biophys Biomol Struct, 28, pp.181~204 (1999)
- Parsons JD, "Improved tools for DNA comparison and clustering", Comput Appl Biosci, 11, pp.603~613 (1995)
- Pfaffl MW, "A new mathematical model for relative quantification in real-time RT-PCR", Nucleic Acids Res, 29, pp.e45~ (2001)
- Retzek H, "Molecular cloning and functional characterization of chicken cathepsin-D, a key enzyme for yolk formation", DNA Cell Biol, 11, pp.661~672 (1992)
- Rozen S, "Primer3 on the WWW for General Users and for Biologist Programmers, In Bioinformatics Methods and Protocols: Methods in Molecular Biology", pp.365~386 (2000), Humana Press Inc
- Tingaud-Sequeira, Cerdà, "Phylogenetic relationships and gene expression patterns of three different cathepsin L (Ctsl) isoform in zebrafish: Ctsla is the putative yolk processing enzyme", Gen, 386, pp.98~106 (2007)
- Thompson JD, "CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice", Nuc Acids Res, 22, pp.4673~4680 (1994)
- Turk V, "Lysosomal cathepsins: structure, role in antigen processing and presentation and cancer", Adv Enzyme Regul, 42, pp.285~303 (2002)
- Vihtelic TS, "Expressed sequence tag analysis of zebrafish eye tissues for NEIBank", Mol Vis, 11, pp.1083~1100 (2005)
- Wiegand MD, "Composition, accumulation and utilization of yolk lipids in teleost fish", Rev Fish Biol Fish, 6, pp.259~286 (1996)
