Molecular cloning and mRNA expression of cathepsin C gene in black tiger shrimp (Penaeus monodon)

详细信息    查看全文

• 作者：Lihua Qiu ; Shigui Jiang ; Jianhua Huang ; Weifang Wang ; Dianchang Zhang ; Qiaer Wu ; Keng Yang
• 关键词：Molecular cloning ; Cathepsin C ; mRNA expression ; Penaeus monodon
• 刊名：Comparative Biochemistry and Physiology - Part A: Molecular & Integrative Physiology
• 出版年：2008
• 出版时间：July 2008
• 年：2008
• 卷：150
• 期：3
• 页码：320-325
• 全文大小：1259 K

文摘

Cathepsin C (dipeptidyl-peptidase I, DPPI) is a lysosomal cysteine proteinase belonging to the papain superfamily, which is capable of removing dipeptides sequentially from the amino terminus of peptide and protein substrates. In the present study, the cDNA of a cathepsin C was cloned from black tiger shrimp Penaeus monodon (designated PmcathepsinC) by homology cloning and rapid amplification of cDNA ends (RACE) approaches. The full-length cDNA of PmcathepsinC consisted of 2051 nucleotides with a canonical polyadenylation signal sequence AATAAA and a poly(A) tail, and an open reading frame (ORF) of 1350 bp encoding a polypeptide of 449 amino acid residues with a predicted molecular weight of 50.0 kDa and theoretical isoelectric point of 5.65. The high identity of PmcathepsinC with Cathepsin C in other organisms indicated that PmcathepsinC should be a new member of the Cathepsin C family. By fluorescent quantitative real-time PCR, mRNA transcript of PmcathepsinC was detectable in all the examined tissues with higher level in ovary and heart. The temporal expression of PmcathepsinC mRNA in the hepatopancreas was up-regulated by lipopolysaccharide (LPS) stimulation and reached the maximum level at 4 h post-stimulation, and then dropped back to the original level gradually. These results indicated that PmcathepsinC was a constitutive and inducible acute-phase protein that perhaps involved in the immune defense of P. monodon.