Identification and characterization of the interactive proteins with cytotoxic T-lymphocyte antigen-2α
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Date
2014-12-17
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Abstract
Cytotoxic T-lymphocyte antigen-2α (CTLA-2α) is
a potent inhibitor of cathepsin L-like cysteine proteases.
Recombinant CTLA-2α is known to be a
potent, competitive inhibitor of cathepsin L-like cysteine
proteases. In this study, cathepsin L, cathepsin
C, and tubulointerstitial nephritis antigen-related
protein 1 (TINAGL1) were identified as novel interactive
proteins of CTLA-2α by the yeast two-hybrid
screening system. The direct interactions and colocalization
of these proteins with CTLA-2α were
confirmed using co-immunoprecipitation and immunofluorescence
staining, respectively. The disulfidebonded
CTLA-2α/cathepsin L complex was isolated
from mouse tissue. CTLA-2α was found to be specific
and consistently expressed on the maternal side
of the mouse placenta. Double immunofluorescence
analysis showed that CTLA-2α was co-localized with
cathepsin L, cathepsin C, and TINAGL1 in placenta.
A simple cell-based fluorescence assay
revealed that CTLA-2α exhibited inhibitory activity
toward cathepsin C in live cells, which indicated
that CTLA-2α is a novel endogenous inhibitor of
cathepsin C.
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Keywords
CTLA-2α, Cathepsin L, TINAGL1, Proteases inhibitor, Cathepsin C