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

dc.contributor.authorLuziga, C.
dc.contributor.authorYamamoto, Y.
dc.contributor.authorYamamoto, M.
dc.contributor.authorNga, B. T.
dc.contributor.authorKusakabe, K. T.
dc.date.accessioned2018-06-11T06:38:04Z
dc.date.available2018-06-11T06:38:04Z
dc.date.issued2014-12-17
dc.description.abstractCytotoxic 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.en_US
dc.identifier.urihttps://www.suaire.sua.ac.tz/handle/123456789/2274
dc.language.isoenen_US
dc.subjectCTLA-2αen_US
dc.subjectCathepsin Len_US
dc.subjectTINAGL1en_US
dc.subjectProteases inhibitoren_US
dc.subjectCathepsin Cen_US
dc.titleIdentification and characterization of the interactive proteins with cytotoxic T-lymphocyte antigen-2αen_US
dc.typeArticleen_US
dc.urlhttp://dx.doi.org/10.1080/09168451.2014.991686en_US

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