Participation of a Cathepsin L-Type Protease in the Activation of Caspase-3.
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- Ishisaka Rumi
- Institute of Medical Science, Kurashiki Medical Center, 250 Bakuro-cho, Kurashiki 710-8522, Japan
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- Utsumi Toshihiko
- Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, 1677-1 Yoshida, Yamaguchi 753-8515, Japan
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- Kanno Tomoko
- Institute of Medical Science, Kurashiki Medical Center, 250 Bakuro-cho, Kurashiki 710-8522, Japan
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- Arita Kayo
- Institute of Medical Science, Kurashiki Medical Center, 250 Bakuro-cho, Kurashiki 710-8522, Japan
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- Katsumura Nobuhiko
- Institute for Health Science, Tokushima Bunri University, Tokushima 770-8514, Japan
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- Akiyama Jitsuo
- Doonan Institute of Medical Science, Hakodate 041-8502, Japan
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- Utsumi Kozo
- Institute of Medical Science, Kurashiki Medical Center, 250 Bakuro-cho, Kurashiki 710-8522, Japan
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抄録
A previous paper from this laboratory reported the activation of a caspase-3-like protease by a digitonin-treated lysosomal fraction [FEBS Lett. 435, 233-236, 1998]. In this study, we examined the effects of specific inhibitors of lysosomal cysteine proteases, such as cathepsins B, S, and L, on the activation of caspase-3 to find out which cathepsin is responsible for the activation. Pro-caspase-3 in the cytosol was cleaved by a lysosomal protease(s) contained in the supernatant of a digitonin-treated crude mitochondrial fraction containing lysosomes (ML) and the cleaved product was detected by Western blotting using anti-caspase-3 antibody. The activation of caspase-3 by the lysosomal protease(s) was pH dependent and the optimun pH for activation was pH 6.6-6.8. This activation was not inhibited by CA-074, a specific inhibitor of cathepsin B, but was strongly inhibited by CLIK-066 and CLIK-181, specific inhibitors of cathepsin L. The inhibitory effect of CLIK-060, a specific inhibitor of cathepsin S, was very weak. Furthermore, the activation of caspase-3 was enhanced by addition of purified cathepsin L only in the presence of the supernatant of the digitonin-treated ML. These results suggested that a cathepsin L-type protease activity might participate in the activation mechanism of caspase-3 in the presence of the supernatnat from the ML.
収録刊行物
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- Cell Structure and Function
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Cell Structure and Function 24 (6), 465-470, 1999
日本細胞生物学会
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詳細情報 詳細情報について
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- CRID
- 1390001204695633664
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- NII論文ID
- 10009625489
- 30023110068
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- NII書誌ID
- AA0060007X
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- COI
- 1:CAS:528:DC%2BD3cXhtlGmsr4%3D
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- ISSN
- 13473700
- 03867196
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- NDL書誌ID
- 4988095
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- PubMed
- 10698261
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可