Identification and characterization of the interactive proteins with cytotoxic T-lymphocyte antigen-2α

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dc.creatorLuziga, C.
dc.creatorYamamoto, Y.
dc.creatorYamamoto, M.
dc.creatorNga, B. T.
dc.creatorKusakabe, K. T.
dc.date2018-06-11T06:38:04Z
dc.date2018-06-11T06:38:04Z
dc.date2014-12-17
dc.date.accessioned2022-10-25T08:50:43Z
dc.date.available2022-10-25T08:50:43Z
dc.descriptionCytotoxic 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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dc.identifierhttps://www.suaire.sua.ac.tz/handle/123456789/2274
dc.identifier.urihttp://hdl.handle.net/123456789/90560
dc.languageen
dc.subjectCTLA-2α
dc.subjectCathepsin L
dc.subjectTINAGL1
dc.subjectProteases inhibitor
dc.subjectCathepsin C
dc.titleIdentification and characterization of the interactive proteins with cytotoxic T-lymphocyte antigen-2α
dc.typeArticle

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