TY - JOUR
T1 - Molecular cloning of a novel mouse aspartic protease-like protein that is expressed abundantly in the kidney
AU - Mori, Kiyoshi
AU - Ogawa, Yoshihiro
AU - Tamura, Naohisa
AU - Ebihara, Ken
AU - Aoki, Tomohiro
AU - Muro, Seiji
AU - Ozaki, Shoichi
AU - Tanaka, Issei
AU - Tashiro, Kei
AU - Nakao, Kazuwa
N1 - Funding Information:
We thank Prof. T. Honjo, Department of Medical Chemistry, Kyoto University Graduate School of Medicine for encouragement, Prof. T. Uchiyama, Virus Research Institute, Kyoto University for anti-Tac antibody, Prof. T. Nakano, Research Institute for Microbial Diseases, Osaka University, Dr. T. Kuwahara, Department of Nephrology, Saiseikai Nakatsu Hospital, and Dr. T. Nakamura, Department of Medical Chemistry, Kyoto University Graduate School of Medicine for discussions. The authors also acknowledge Mr. T. Okazaki and Mr. N. Isse for their excellent technical assistance. This work was supported in part by research grants from the Japanese Ministry of Education, Science and Culture, the Japanese Ministry of Health and Welfare.
PY - 1997/1/20
Y1 - 1997/1/20
N2 - By use of the signal sequence trap method, we isolated a cDNA encoding a novel aspartic protease-like protein from the mouse kidney, and termed it 'kidney-derived aspartic protease-like protein (KAP)'. The protein, a 419-amino-acid polypeptide with a 16-amino-acid signal sequence, had 47% identity with mouse cathepsin D, and its overall structure was closely related to known aspartic proteases. Northern blot analysis revealed that KAP mRNA is expressed at the highest level in the kidney, at a moderate level in the lung, and at low levels in the spleen and adipose tissue. In situ hybridization analysis demonstrated that the mRNA is expressed abundantly in the proximal straight tubule and slightly, but significantly, in the proximal convoluted tubule in the kidney. This intra-renal distribution differs distinctly from those of previously reported proteases such as cathepsins B, D, and H.
AB - By use of the signal sequence trap method, we isolated a cDNA encoding a novel aspartic protease-like protein from the mouse kidney, and termed it 'kidney-derived aspartic protease-like protein (KAP)'. The protein, a 419-amino-acid polypeptide with a 16-amino-acid signal sequence, had 47% identity with mouse cathepsin D, and its overall structure was closely related to known aspartic proteases. Northern blot analysis revealed that KAP mRNA is expressed at the highest level in the kidney, at a moderate level in the lung, and at low levels in the spleen and adipose tissue. In situ hybridization analysis demonstrated that the mRNA is expressed abundantly in the proximal straight tubule and slightly, but significantly, in the proximal convoluted tubule in the kidney. This intra-renal distribution differs distinctly from those of previously reported proteases such as cathepsins B, D, and H.
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U2 - 10.1016/S0014-5793(96)01473-1
DO - 10.1016/S0014-5793(96)01473-1
M3 - Article
C2 - 9013890
AN - SCOPUS:0031031854
SN - 0014-5793
VL - 401
SP - 218
EP - 222
JO - FEBS Letters
JF - FEBS Letters
IS - 2-3
ER -