한국발생생물학회지:발생과생식 (Development and Reproduction)

  • 제22권3호
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  • Pages.289-295
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  • 2018
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  • 2465-9525(pISSN)
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  • 2465-9541(eISSN)
한국발생생물학회 (The Korean Society of Developmental Biology)
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Expression of Yolk Processing Enzyme Genes in Fertilized Eggs from Artificially Matured Female Eel, Anguilla japonica

  • Oh, Hyeon Ji (Dept. of Aquatic Life Medical Sciences, Sunmoon University) ;
  • Kim, Jung-Hyun (Aquaculture Research Team, NFRDI) ;
  • Mun, Seong Hee (Dept. of Aquatic Life Medical Sciences, Sunmoon University) ;
  • Kim, Jin Hui (Dept. of Aquatic Life Medical Sciences, Sunmoon University) ;
  • Kim, Dae-Jung (Aquaculture Research Team, NFRDI) ;
  • Kwon, Joon Yeong (Dept. of Aquatic Life Medical Sciences, Sunmoon University)
  • 투고 : 2018.07.31
  • 심사 : 2018.09.10
  • 발행 : 2018.09.30
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초록

Large quantity of eggs fail to be fertilized and many of fertilized eggs are unable to hatch in the eel, Anguilla japonica. Larvae of eel absorb egg yolk up to 8 days after hatching but the majority of hatched larvae die before they reach the stage of first feeding in this species. Genes of key enzymes for yolk processing (cathepsin B, D, L and lipoprotein lipase - abbreviated as ctsb, ctsd, ctsl and lpl, respectively) could be associated with egg quality. In this study, we investigated differences in the expression of these genes between floating eggs and sinking eggs, and also the relationship between the gene expressions of the enzymes and fertilization rates in the fertilized eggs obtained from artificially matured female eels. Expressions of yolk processing enzyme genes did not show significant difference between floating and sinking egg groups. Expression of ctsb decreased when fertilization rate was high. Expression of ctsd, ctsl and lpl, however, did not show any significant differences. These results suggest that ctsb expression could be an indicator of egg quality, and that some proteins prone to be digested by ctsb could be very important in the process of fertilization and normal cleavage in this species. Further study should identify these critical proteins to improve our understanding on the quality of fish eggs.

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참고문헌

  1. Carnevali O, Carletta R, Cambi A, Vita A, Bromage N (1999a) Yolk formation and degradation during oocyte maturation in seabream Sparus aurata: Involvement of two lysosomal proteinases. Biol Reprod 60:140-146. https://doi.org/10.1095/biolreprod60.1.140
  2. Carnevali O, Centonze F, Brooks S, Marota I, Sumpter JP (1999b) Molecular cloning and expression of ovarian cathepsin D in seabream, Sparus aurata. Biol Reprod 61:785-791. https://doi.org/10.1095/biolreprod61.3.785
  3. Carnevali O, Cionna C, Tosti L, Cerda J, Gioacchini G (2008) Changes in cathepsin gene expression and relative enzymatic activity during gilthead sea bream oogenesis. Mol Reprod Dev 75:97-104. https://doi.org/10.1002/mrd.20768
  4. Carnevali O, Mosconi G, Cambi A, Ridolfi S, Zanuy S, Polzonetti-Magni AM (2001) Changes of lysosomal enzyme activities in sea bass (Dicentrarchus labrax) eggs and developing embryos. Aquaculture 202:249-256. https://doi.org/10.1016/S0044-8486(01)00775-X
  5. Carnevali O, Mosconi G, Roncarati A, Belvedere P, Limatola E, Polozoneni-Magni AM (1993) Yolk protein changes dying oocyte growth in European sea bass Dicentrarchus labrax L. J Appl Ichthyol 9:175-194. https://doi.org/10.1111/j.1439-0426.1993.tb00393.x
  6. de Duve C (1983) Lysosomes revisited. FEBS J 137:391-397.
  7. Gwon SH, Kim HK, Baek HJ, Lee YD, Kwon JY (2017) Cathepsin B & D and the survival of early embryos in red spotted grouper, Ephinephelus akaara. Dev Reprod 21:457-466. https://doi.org/10.12717/DR.2017.21.4.457
  8. Hiramatsu N, Ichikawa N, Fukada H, Fujita T, Sullivan CV, Hara A (2002) Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids. J Exp Zool 292:11-25. https://doi.org/10.1002/jez.1138
  9. Kim DJ, Lee NS, Lee BI, Kim SK, Kim KK (2013) Development changes in the external structure of the head and the histological structure of the eye in artificially reared Japanese eel, Anguilla japonica, leptocephalus and glass eel. J Life Sci 23:1288-1294. https://doi.org/10.5352/JLS.2013.23.10.1288
  10. Kim DJ, Lee NS, Kim KK, Chang DS (2014) Effects of starvation, water temperature, and water flow on the metamorphosis of leptocephalus of Japanese eel Anguilla japonica. Fish Aquatic Sci 47:597-602.
  11. Kwon JY, Prat F, Randall C, Tyler CR (2001) Molecular characterization of putative yolk processing enzymes and their expression during oogenesis and embryogenesis in rainbow trout (Oncorhynchus mykiss). Biol Reprod 65:1701-1709. https://doi.org/10.1095/biolreprod65.6.1701
  12. Liaudet-Coopman E, Beaujouin M, Derocq D, Garcia M, Glondu-Lassis M, Laurent-Matha V, Prebois C, Rochefort H, Vignon F (2006) Cathepsin D: Newly discovered functions of a longstanding aspartic protease in cancer and apoptosis. Cancer Lett 237:167-179. https://doi.org/10.1016/j.canlet.2005.06.007
  13. Matsubara T, Sawano K (1995) Proteolytic cleavage of vitellogenin and yolk proteins during vitellogenin uptake and oocyte maturation in barfin flounder (Verasper moseri). J Exp Zool 272:34-45. https://doi.org/10.1002/jez.1402720105
  14. Ohkubo N, Sawaguchi S, Nomura K, Tanaka H, Matsubara T (2008) Utuilization of free amino acids, yolk protein and lipids in developing eggs and yolk-sac larvae of Japanese eel Anguilla japonica. Aquaculture 282:130-137. https://doi.org/10.1016/j.aquaculture.2008.06.017
  15. Palomino J, Herrera G, Torres-Fuentes J, Dettleff P, Patel A, Martinez V (2017) Assessment of cathepsin mRNA expression and enzymatic activity during early embryonic development in the yellowtail kingfish Seriola lalandi. Anim Reprod 180:23-29. https://doi.org/10.1016/j.anireprosci.2017.02.009
  16. Roverts R (2005) Lysosomal cysteine proteases: Structure, function and inhibition of cathepsin. Drug News Perspect 18:605-614. https://doi.org/10.1358/dnp.2005.18.10.949485
  17. Sire MF, Babin PJ, Vernier JM (1994) Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout. J Exp Zool 269:69-83. https://doi.org/10.1002/jez.1402690109
  18. Tanaka H, Kagawa H, Ohta H, Unuma T, Nomura K (2003) The first production of glass eel in captivity:Fish reproductive physiology facilitates great progress in aquaculture. Fish Physiol Biochem 28:493-497. https://doi.org/10.1023/B:FISH.0000030638.56031.ed
  19. Tingaud-Sequeira A, Carnevali O, Cerda J (2011) Cathepsin B differential expression and enzyme processing and activity during Fundulus heteroclitus embryogenesis. Comp Biochem Physiol A Mol Integr Physiol 158:221-228. https://doi.org/10.1016/j.cbpa.2010.11.002
  20. Unuma T, Kondo S, Tanaka H, Kagawa H, Nomura K, Ohta H (2005) Relationship between egg specific gravity and egg quality in the Japanese eel, Anguilla japonica. Aquaculture 246:493-500. https://doi.org/10.1016/j.aquaculture.2005.01.011