Cloning and expression analysis of cathepsin D in the olive flounder Paralichthys olivaceus.
We isolated a homolog of cathepsin D from the cDNA library of the olive flounder kidney. The olive flounder cathepsin D transcript consisted of 1,733 bp that encoded a polypeptide of 396 amino acids. The overall similarity between olive flounder cathepsin D and other cathepsin Ds was very high, with the highest amino acid sequence identity to barramundi perch (89%). RT-PCR revealed that cathepsin D was expressed in almost all tissues, with high expression in the liver, intestine, kidney, skin, and spleen. The accumulation of cathepsin D mRNA after bacterial infection, as determined by RT-PCR, was constitutive and increased greatly after bacterial infection.
Park
Eun-Mi
EM
Biotechnology Research Institute, National Fisheries Research and Development Institute, Busan, Republic of Korea.
Kim
Young-Ok
YO
Nam
Bo-Hye
BH
Kong
Hee Jeong
HJ
Kim
Woo-Jin
WJ
Lee
Sang-Jun
SJ
Kim
Kyung-Kil
KK
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002402:Cathepsin D / Q000737:chemistry / Q000235:genetics*; D002417:Cattle; D003001:Cloning, Molecular; D004285:Dogs; D005432:Flounder / Q000235:genetics*; D020869:Gene Expression Profiling; D005786:Gene Expression Regulation; D006801:Humans; D008969:Molecular Sequence Data; D010802:Phylogeny; D020133:Reverse Transcriptase Polymerase Chain Reaction; D016415:Sequence Alignment
D002402:Cathepsin D