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Studies of Inhibitory Mechanisms of Propeptide-Like Cysteine Protease Inhibitors
Joint Authors
Nga, Bui T. T.
Yamamoto, Yoshimi
Takeshita, Yuki
Yamamoto, Misa
Source
Issue
Vol. 2014, Issue 2014 (31 Dec. 2014), pp.1-10, 10 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2014-06-19
Country of Publication
Egypt
No. of Pages
10
Main Subjects
Abstract EN
Mouse cytotoxic T-lymphocyte antigen-2α (CTLA-2α), Drosophila CTLA-2-like protein (crammer), and Bombyx cysteine protease inhibitor (BCPI) belong to a novel family of cysteine protease inhibitors (I29).
Their inhibitory mechanisms were studied comparatively.
CTLA-2α contains a cysteine residue (C75), which is essential for its inhibitory potency.
The CTLA-2α monomer was converted to a disulfide-bonded dimer in vitro and in vivo.
The dimer was fully inhibitory, but the monomer, which possessed a free thiol residue, was not.
A disulfide-bonded CTLA-2α/cathepsin L complex was isolated, and a cathepsin L subunit with a molecular weight of 24,000 was identified as the interactive enzyme protein.
Crammer also contains a cysteine residue (C72).
Both dimeric and monomeric forms of crammer were inhibitory.
A crammer mutant with Cys72 to alanine (C72A) was fully inhibitory, while the replacement of Gly73 with alanine (G73A) caused a significant loss in inhibitory potency, which suggests a different inhibition mechanism from CTLA-2α.
BCPI does not contain cysteine residue.
C-terminal region (L77-R80) of BCPI was essential for its inhibitory potency.
CTLA-2α was inhibitory in the acidic pH condition but stabilized cathepsin L under neutral pH conditions.
The different inhibition mechanisms and functional considerations of these inhibitors are discussed.
American Psychological Association (APA)
Nga, Bui T. T.& Takeshita, Yuki& Yamamoto, Misa& Yamamoto, Yoshimi. 2014. Studies of Inhibitory Mechanisms of Propeptide-Like Cysteine Protease Inhibitors. Enzyme Research،Vol. 2014, no. 2014, pp.1-10.
https://search.emarefa.net/detail/BIM-503073
Modern Language Association (MLA)
Nga, Bui T. T.…[et al.]. Studies of Inhibitory Mechanisms of Propeptide-Like Cysteine Protease Inhibitors. Enzyme Research No. 2014 (2014), pp.1-10.
https://search.emarefa.net/detail/BIM-503073
American Medical Association (AMA)
Nga, Bui T. T.& Takeshita, Yuki& Yamamoto, Misa& Yamamoto, Yoshimi. Studies of Inhibitory Mechanisms of Propeptide-Like Cysteine Protease Inhibitors. Enzyme Research. 2014. Vol. 2014, no. 2014, pp.1-10.
https://search.emarefa.net/detail/BIM-503073
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-503073