TY - JOUR
T1 - Analysis of big endothelin-1 digestion by cathepsin D
AU - Sawamura, Tatsuya
AU - Shinmi, Osamu
AU - Kishi, Naoya
AU - Sugita, Yoshiki
AU - Yanagisawa, Masashi
AU - Goto, Katsutoshi
AU - Masaki, Tomoh
AU - Kimura, Sadao
N1 - Funding Information:
ACKNOWLEDGMENTS This work was in part supported by grants from University of Tsukuba Project Research, the Ministry of Education, Science and Culture of Japan, and National Cardiovascular Center for Research Institute.
PY - 1990/10/30
Y1 - 1990/10/30
N2 - Digestion of big endothelin(ET)-1 by cathepsin D, which is the only substantially identified protease showing ET converting enzyme activity, was characterized. Increased doses of cathepsin D showed decrease of immunoreactive (ir-) ET produced from big ET-1. Time course of big ET-1 conversion showed marked increase of ir-ET in a relatively short period, but further incubation resulted in the decrease of ir-ET. Incubation at various pHs with different doses of cathepsin D revealed that low doses of cathepsin D yielded the maximum production of ir-ET at pH 3.5 - 4.0, but higher doses of cathepsin D showed a bimodal curve of ir-ET production, which may be due to degradation of ir-ET. HPLC analysis revealed that cathepsin D cleaves Asn18-Ile19 bond in addition to Trp21-Val22 bond of big ET-1. These data suggests cathepsin D is not a physiological endothelin converting enzyme.
AB - Digestion of big endothelin(ET)-1 by cathepsin D, which is the only substantially identified protease showing ET converting enzyme activity, was characterized. Increased doses of cathepsin D showed decrease of immunoreactive (ir-) ET produced from big ET-1. Time course of big ET-1 conversion showed marked increase of ir-ET in a relatively short period, but further incubation resulted in the decrease of ir-ET. Incubation at various pHs with different doses of cathepsin D revealed that low doses of cathepsin D yielded the maximum production of ir-ET at pH 3.5 - 4.0, but higher doses of cathepsin D showed a bimodal curve of ir-ET production, which may be due to degradation of ir-ET. HPLC analysis revealed that cathepsin D cleaves Asn18-Ile19 bond in addition to Trp21-Val22 bond of big ET-1. These data suggests cathepsin D is not a physiological endothelin converting enzyme.
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U2 - 10.1016/0006-291X(90)90758-F
DO - 10.1016/0006-291X(90)90758-F
M3 - Article
C2 - 2241976
AN - SCOPUS:0025196036
SN - 0006-291X
VL - 172
SP - 883
EP - 889
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -