Department of Anatomy, Histology and Cell Biology

Permanent URI for this communityhttp://10.10.97.169:4000/handle/123456789/100

Browse

Browsing Department of Anatomy, Histology and Cell Biology by Subject "Cathepsin L"

Now showing 1 - 2 of 2
  • Thumbnail Image
    Item
    Identification and characterization of the interactive proteins with cytotoxic T-lymphocyte antigen-2α
    (2014-12-17) Luziga, C.; Yamamoto, Y.; Yamamoto, M.; Nga, B. T.; Kusakabe, K. T.
    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.
  • Thumbnail Image
    Item
    Localization profile of cathepsin L in the brain of African giant rat (Cricestomys gambianus)
    (2016) Luziga, C.; Nga, B. T. T.; Kashoma, I.; Katakweba, A.; Yoshimi, Y.
    Cathepsins, are members of the papain superfamily of mammalian lysosomal cysteine proteases. Among others there are two prominent members with broad substrate specificity, these are cathepsin B and cathepsin L that are known to be involved in the process of intra- and extra-cellular protein degradation and turnover. However, the in vivo targets of cathepsin L in nervous tissues are yet to be identified. We examined by immunofluorescence studies the distribution pattern of cathepsin L protein and determine the specific cell types synthesizing the enzyme in the brain of African giant rats (Cricetomys gambianus). Results showed that Cathepsin L protein was localized in various brain regions of the giant rats. In the telencephalon, immunoreactivity was identified in cerebral cortex and subcortical structures, hippocampus, amygdala and basal ganglia. Within the diencephalon high density of positive signals was observed in mediodorsal and lateral posterior thalamic nuclei and medial habenular nucleus. In the mesencephalon, cathepsin L was detected in the substantia nigra and cerebral peduncles. Strong labeling in the hypothalamus was present in the anterior commissure and median eminence while in the cerebellum cathepsin L was observed in the deep white matter, granule cell layer, stellate, and basket cells of cerebellar cortex and in the Purkinje neurons. The distribution pattern and functional implications of cathespin L in relation to spatial memory establishment, learning coordination and disease mechanisms is discussed.