Identification and molecular characterization of <i>Cathepsin L</i> gene and its expression analysis during early ontogenetic development of kuruma shrimp <i>Marsupenaeus japonicus</i>

QIAO Ying; WANG Jun; MAO Yong; LIU Min; SONG Xiaohong; SU Yongquan; WANG Chunzhong; ZHENG Zhipeng

doi:10.1007/s13131-017-0983-5

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Article Navigation > Acta Oceanologica Sinica > 2017 > 36(6): 52-60

QIAO Ying, WANG Jun, MAO Yong, LIU Min, SONG Xiaohong, SU Yongquan, WANG Chunzhong, ZHENG Zhipeng. Identification and molecular characterization of Cathepsin L gene and its expression analysis during early ontogenetic development of kuruma shrimp Marsupenaeus japonicus[J]. Acta Oceanologica Sinica, 2017, 36(6): 52-60. doi: 10.1007/s13131-017-0983-5

Citation:

QIAO Ying, WANG Jun, MAO Yong, LIU Min, SONG Xiaohong, SU Yongquan, WANG Chunzhong, ZHENG Zhipeng. Identification and molecular characterization of Cathepsin L gene and its expression analysis during early ontogenetic development of kuruma shrimp Marsupenaeus japonicus[J]. Acta Oceanologica Sinica, 2017, 36(6): 52-60. doi: 10.1007/s13131-017-0983-5

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Identification and molecular characterization of Cathepsin L gene and its expression analysis during early ontogenetic development of kuruma shrimp Marsupenaeus japonicus

doi: 10.1007/s13131-017-0983-5

1.
State Key Laboratory of Marine Environmental Sciences, Xiamen University, Xiamen 361102, China
2.
Putian Tian-ran-xing Agricultural Development Co. Ltd., Fujian 351100, China

Received Date: 2016-02-16
Rev Recd Date: 2016-03-29

Abstract

Abstract

Cathepsin L gene is a member of the cysteine proteinase gene group. In this study Cathepsin L gene was isolated from Kuruma shrimp Marsupenaeus japonicus (Mj-Cathepsin L) and the full-length DNA sequence was 1 963 bp. Mj-Cathepsin L protein showed high homologies with other Cathepsin L proteins documented in vertebrates, mollusks and other crustaceans. Expression analysis of Mj-Cathepsin L gene in different tissues revealed that it was predominant in hepatopancreas. During early ontogenetic development stages Mj-Cathepsin L showed a development-regulated expression, and the Mj-Cathepsin L showed a molting stage-regulated expression during the five molting stages, inferring its role in the ontogenic development of M. japonicus. Two kinds of forms of Mj-Cathepsin L protein:pro-Cathepsin L and Cathepsin L were measured in hepatopancreas, stomach and intestine by Western Blotting.
- Cathepsin L gene,
- larval development,
- molting cycle,
- tissue distribution,
- Marsupenaeus japonicus,

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References(30)

References

Aoki H, Ahsan M N, Watabe S. 2004. Molecular and enzymatic properties of a cathepsin L-like proteinase with distinct substrate specificity from northern shrimp (Pandalus borealis). J Comp Physiol B, 174(1):59-69

Arockiaraj J, Gnanam A J, Muthukrishnan D, et al. 2013. Macrobrachium rosenbergii cathepsin L:molecular characterization and gene expression in response to viral and bacterial infections. Microbiol Res, 168(9):569-579

Chauhan S S, Ray D, Kane S E, et al. 1998. Involvement of carboxy-terminal amino acids in secretion of human lysosomal protease cathepsin L. Biochemistry, 37(23):8584-8594

Dahl S W, Halkier T, Lauritzen C, et al. 2001. Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing. Biochemistry, 40(6):1671-1678

Darias M J, Murray H M, Gallant J W, et al. 2006. Characterization of a partial α-amylase clone from red porgy (Pagrus pagrus):expression during larval development. Comp Biochem Physiol B Biochem Mol Bio, 143(2):209-218

de Oliveira Cesar J R, Zhao Baoping, Malecha S, et al. 2006. Morphological and biochemical changes in the muscle of the marine shrimp Litopenaeus vannamei during the molt cycle. Aquaculture, 261(2):688-694

Dhar A K, Bowers R M, Licon K S, et al. 2009. Validation of reference genes for quantitative measurement of immune gene expression in shrimp. Mol Immunol, 46(8-9):1688-1695

Glenn K L, Grapes L, Suwanasopee T, et al. 2005. SNP analysis of AMY2 and CTSL genes in Litopenaeus vannamei and Penaeus monodon shrimp. Anim Genet, 36(3):235-236

Hu Kejin, Leung P C. 2004. Shrimp cathepsin L encoded by an intronless gene has predominant expression in hepatopancreas, and occurs in the nucleus of oocyte. Comp Biochem Physiol B Biochem Mol Biol, 137(1):21-33

Hu Kejin, Leung P C. 2007. Food digestion by cathepsin L and digestion-related rapid cell differentiation in shrimp hepatopancreas. Comp Biochem Physiol B Biochem Mol Biol, 146(1):69-80

Hu K J, Leung P C. 2006. Complete, precise, and innocuous loss of multiple introns in the currently intronless, active cathepsin L-like genes, and inference from this event. Mol Phylogenet Evol, 38(3):685-696

Johnson K S, Rabosky D. 2000. Phylogenetic distribution of cysteine proteinases in beetles:evidence for an evolutionary shift to an alkaline digestive strategy in Cerambycidae. Comp Biochem Physiol B Biochem Mol Biol, 126(4):609-619

Johnston D J. 2003. Ontogenetic changes in digestive enzyme activity of the spiny lobster, Jasus edwardsii (Decapoda; Palinuridae). Marine Biology, 143(6):1071-1082

Karrer K M, Peiffer S L, Ditomas M E. 1993. Two distinct gene subfamilies within the family of cysteine protease genes. Proc Natl Acad Sci U S A, 90(7):3063-3067

Laycock M V, Hirama T, Hasnain S, et al. 1989. Purification and characterization of a digestive cysteine proteinase from the American lobster (Homarus americanus). Biochem J, 263(2):439-444

Le Boulay C, Van Wormhoudt A, Sellos D. 1995. Molecular cloning and sequencing of two cDNAs encoding cathepsin L-related cysteine proteinases in the nervous system and in the stomach of the Norway lobster (Nephrops norvegicus). Comp Biochem Physiol B Biochem Mol Bio, 111(3):353-359

Le Boulay C, Van Wormhoudt A, Sellos D. 1996. Cloning and expression of cathepsin L-like proteinases in the hepatopancreas of the shrimp Penaeus vannamei during the intermolt cycle. J Comp Physiol B, 166(5):310-318

Le Boulay C, Sellos D, Van Wormhoudt A. 1998. Cathepsin L gene organization in crustaceans. Gene, 218(1-2):77-84

Lemos D, Rodríguez A. 1998. Nutritional effects on body composition, energy content and trypsin activity of Penaeus japonicus during early postlarval development. Aquaculture, 160(1-2):103-116

Lima A P C A, dos Reis F C G, Serveau C, et al. 2001. Cysteine protease isoforms from Trypanosoma cruzi, cruzipain 2 and cruzain, present different substrate preference and susceptibility to inhibitors. Mol Biochem Parasitol, 114(1):41-52

Livak K J, Schmittgen T D. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods, 25:402-408

Ma Jianjun, Zhang Dianchang, Jiang Jingjing, et al. 2010. Molecular characterization and expression analysis of cathepsin L1 cysteine protease from pearl oyster Pinctada fucata. Fish Shellfish Immunol, 29(3):501-507

McIntyre G F, Godbold G D, Erickson A H. 1994. The pH-dependent membrane association of procathepsin L is mediated by a 9-residue sequence within the propeptide. J Biol Chem, 269(1):567-572

Miyamoto K, Iwadate M, Yanagisawa Y, et al. 2011. Cathepsin L is highly expressed in gastrointestinal stromal tumors. Int J Oncol, 39(5):1109-1115

Nakagawa T, Roth W, Wong P, et al. 1998. Cathepsin L:critical role in Ii degradation and CD4 T cell selection in the thymus. Science, 280(5362):450-453

Pan Luqing, Liu Hong yu, Xiao Guoqiang. 2006. A review on digestive enzyme of crustacean larvae. J Fishery Sci China, 13(3):492-501

Qian Zhaoying, Li Xilian, Xin Jingjing, et al. 2013. PCR-SSCP Polymorphism of CTSL gene and its correlation with growth traits of Litopenaeus vannamei and the different mRNA expressions of CTSL. Haiyang Xuebao, 35(6):121-127

Rodriguez A, Le Vay L, Mourente G, et al. 1994. Biochemical composition and digestive enzyme activity in larvae and postlarvae of Penaeus japonicus during herbivorous and carnivorous feeding. Marine Biology, 118(1):45-51

Roth W, Deussing J, Botchkarev V A, et al. 2000. Cathepsin L deficiency as molecular defect of furless:hyperproliferation of keratinocytes and pertubation of hair follicle cycling. FASEB J, 14(13):2075-2086

Zhang W, Wang S, Wang Q, et al. 2014. Overexpression of cysteine cathepsin L is a marker of invasion and metastasis in ovarian cancer. Oncol Rep, 31(3):1334-1342

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