Cathepsin B & D and the Survival of Early Embryos in Red Spotted Grouper, Ephinephelus akaara
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Survival of embryos largely depends on yolk processing during early development. Proteolytic enzymes, ca-thepsin B & D (ctsb & ctsd) are known to have some important roles in yolk processing of various fish species. Mature female red spotted groupers were injected with human chorionic gonadotropin (HCG) to induce ovulation. The fertilized eggs and embryos were sampled at 0, 4 and 24 HPF (hours post fertilization). Survivals of each groups of embryos were checked at 24 and 48 HPH (hours post hatching). Transcripts of ctsb & ctsd showed the highest level at 0 HPF and relatively high at 4 HPF, but greatly decreased at 24 HPF. In bad egg quality group (BE, embryos survived until 24 HPH), transcript level of ctsb at 4 HPF were significantly lower than the transcript level at the same stage in good egg quality group (GE, embryos survived un-til 48 HPH) while no significant change of ctsb transcript level was observed at 0 or 24 HPF between BE and GE. Transcript level of ctsd was decreased at 24 HPF, but the difference was not as strong as the case of ctsb transcript. These results suggest that maternal ctsb transcript rather than ctsd transcript is likely to be involved in egg quality resulting in the difference of sur-vival rate of embryos at early developmental period in this species.
Abstract
Survival of embryos largely depends on yolk processing during early development. Proteolytic enzymes, ca-thepsin B & D (ctsb & ctsd) are known to have some important roles in yolk processing of various fish species. Mature female red spotted groupers were injected with human chorionic gonadotropin (HCG) to induce ovulation. The fertilized eggs and embryos were sampled at 0, 4 and 24 HPF (hours post fertilization). Survivals of each groups of embryos were checked at 24 and 48 HPH (hours post hatching). Transcripts of ctsb & ctsd showed the highest level at 0 HPF and relatively high at 4 HPF, but greatly decreased at 24 HPF. In bad egg quality group (BE, embryos survived until 24 HPH), transcript level of ctsb at 4 HPF were significantly lower than the transcript level at the same stage in good egg quality group (GE, embryos survived un-til 48 HPH) while no significant change of ctsb transcript level was observed at 0 or 24 HPF between BE and GE. Transcript level of ctsd was decreased at 24 HPF, but the difference was not as strong as the case of ctsb transcript. These results suggest that maternal ctsb transcript rather than ctsd transcript is likely to be involved in egg quality resulting in the difference of sur-vival rate of embryos at early developmental period in this species.
참고문헌 (33)
- Amano H, "Multiple vitellogenin‐derived yolk proteins in gray mullet (Mugil cephalus): disparate proteolytic patterns associated with ovarian follicle maturation", Mol Reprod Dev, 75, pp.1307~1317 (2008)
- Azaryan AV, "Unique cleavage specifi-city of ‘prohormone thiol protease’ related to proenke-phalin processing", FEBS Lett, 341, pp.197~202 (1994)
- Callegari EA, "PGF2αinduced differential expression of genes involved in turnover of extracellular matrix in rat decidual cells", Reprod Biol Endocrinol, 3, pp.3~ (2005)
- 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)
- Carnevali O, "Molecular cloning and expression of ovarian ca-thepsin D in seabream, Sparus aurata", Biol Reprod, 61, pp.785~791 (1999)
- Carnevali O, "Changes in cathepsin gene expression and rela-tive enzymatic activity during gilthead sea bream ooge-nesis", Mol Reprod Dev, 75, pp.97~104 (2008)
- Carnevali O, "Changes of lysosomal en-zyme activities in sea bass (Dicentrarchus labrax) eggs and developing embryos", Aquaculture, 202, pp.249~256 (2001)
- Dong ZD, "Molecular cloning, characterization and ex-pression of cathepsin D from grass carp (Ctenopharyn-godon idella)", Fish Shellfish Immunol, 33, pp.1207~1214 (2012)
- Duve C, "Lysosomes revisited", FEBS J, 137, pp.391~397 (1983)
- Fernández CG, "Expression of developmental-stage-specific genes in the gilthead sea bream Sparus aurata L", Mar Biotechnol, 15, pp.313~320 (2013)
- Finn RN, "The maturational disassembly and differ-ential proteolysis of paralogous vitellogenins in a marine pelagophil teleost: a conserved mechanism of oocyte hy-dration", Biol Reprod, 76, pp.936~948 (2007)
- Follo C, "Knockdown of cathepsin D in zebrafish fertilized eggs determines congenital myopathy", Biosci Rep, 33, pp.e00034~ (2013)
- Hiramatsu N, "Identification and characterization of pro-teases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids", J Exp Zool A Ecol Genet Physiol, 292, pp.11~25 (2002)
- 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)
- LaFleur Jr GJ, "Derivation of major yolk proteins from parental vitellogenins and alternative pro-cessing during oocyte maturation in Fundulus hetero-clitus", Biol Reprod, 73, pp.815~824 (2005)
- Langdon YG, "Split top: a maternal cathepsin B that regulates dorsoventral patterning and morphogenesis", Development, 143, pp.1016~1028 (2016)
- Lemanski LF, "Role of acid phosphatase in the breakdown of yolk platelets in developing amphib-ian embryos", J Morphol, 153, pp.419~425 (1977)
- Liaudet-Coopman E, "Cathepsin D: newly discovered functions of a long-standing aspartic protease in cancer and apoptosis", Can-cer Lett, 237, pp.167~179 (2006)
- Matsubara T, "Proteolytic cleavage of vitellogenin and yolk proteins during vitellogenin uptake and oocyte maturation in barfin flounder (Verasper mo-seri)", J Exp Zool A Ecol Genet Physiol, 272, pp.34~45 (1995)
- Matsubara T, "Multiple vitellogenins and their unique roles in marine teleosts", Fish Physiol Bio-chem, 28, pp.295~299 (2003)
- Ohkubo N, "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, pp.187~196 (2002)
- Palomino J, "Assessment of cathepsin mRNA expression and enzymatic activity during early embryo-nic development in the yellowtail kingfish Seriola lalan-di", Anim Reprod Sci, 180, pp.23~29 (2017)
- Pelegri F, "Maternal factors in zebrafish development", Dev Dyn, 228, pp.535~554 (2003)
- Perona R, "The lysosomal proteinase of Artemia", FEBS J, 124, pp.357~362 (1982)
- Pierre S, "Grouper aquaculture: Asian success and Mediterranean trials", Aquat Conserv, 18, pp.297~308 (2008)
- Roberts R, "Lysosomal cysteine proteases: structure, function and inhibition of cathepsins", Drug News Per-spect, 18, pp.605~614 (2005)
- Sire MF, "Involvement of the lysosomal system in yolk protein deposit and degrada-tion during vitellogenesis and embryonic development in trout", J Exp Zool A Ecol Genet Physiol, 269, pp.69~83 (1994)
- Tingaud-Sequeira A, "Phylogenetic relation-ships and gene expression pattern of three different ca-thepsin L (Ctsl) isoforms in zebrafish: Ctsla is the puta-tive yolk processing enzyme", Gene, 386, pp.98~106 (2007)
- Tingaud-Sequeira A, "Cathep-sin B differential expression and enzyme processing and activity during Fundulus heteroclitus embryogenesis", Comp Biochem Physiol A Mol Integr Physiol, 158, pp.221~228 (2011)
- Tobin DJ, "The lysosomal pro-tease cathepsin L is an important regulator of kerati-nocyte and melanocyte differentiation during hair follicle morphogenesis and cycling", Am J Pathol, 160, pp.1807~1821 (2002)
- Vogel AM, "Expression of a zebrafish ca-thepsin L gene in anterior mesendoderm and hatching gland", Dev Genes Evol, 206, pp.477~479 (1997)
- Wang H, "Selection and evaluation of new reference genes for RT-qPCR analysis in Epinephelus akaara based on transcriptome data", PloS one, 12, pp.e0171646~ (2017)
- Yasothornsrikul S, "Cathepsin L in secretory vesicles functions as a prohormone-pro-cessing enzyme for production of the enkephalin peptide neurotransmitter", Proc Natl Acad Sci, 100, pp.9590~9595 (2003)
