7 research outputs found

    Harbour Grace Standard

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    The Harbor Grace Standard was published from December 1859 to 1936[?], providing coverage of the Conception Bay area as well as other news. The frequency was weekly save for a brief semiweekly interlude between 1888-94 and there is a publication gap between 1868 and February 1871. Many issues are missing in the later years.Alternative title from common misspelling, as the city's modern name features a "u.

    Expression of differentiation markers in both <i>in vivo</i> xenografts and <i>in vitro</i> differentiation cultures.

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    <p>Sections of xenografts formed from a single-cell-derived HSAEC_4T53RD clone were subjected to staining for (A) K5 (blue), K8 (green) and p63 (red); and (B) SCGB1A1 (green) and MUC5AC (red). Spheres formed by one of the single-cell-derived HSAEC_4T53RD clones were subjected to staining for (C) K5 (blue), K8 (green) and p63 (red); and (D) SCGB1A1 (green) and MUC5AC (red).</p

    Phenotype of HSAEC_4T53RD xenografts.

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    <p>Formalin-fixed, paraffin-embedded sections (4-μm thick) of xenografts derived from HSAEC_4T53RD cells were subjected to staining with (A) haematoxylin and eosin or (B) alcian blue; or with antibodies against (C) cytokeratins (AE1/AE3), (D) p63, (E) alpha-SMA (blue) and p53 (brown). (F) HSAEC_4T53RD cells cultured <i>in vitro</i> on collagen-coated dishes in serum-free SAGM medium were stained with anti-p63 antibody (green) and phalloidin (red).</p

    Increased expression of co-chaperone HOP with HSP90 and HSC70 and complex formation in human colonic carcinoma

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    Co-chaperone HOP (also called stress-inducible protein 1) is a co-chaperone that interacts with the cytosolic 70-kDa heat shock protein (HSP70) and 90-kDa heat shock protein (HSP90) families using different tetratricopeptide repeat domains. HOP plays crucial roles in the productive folding of substrate proteins by controlling the chaperone activities of HSP70 and HSP90. Here, we examined the levels of HOP, HSC70 (cognate of HSP70, also called HSP73), and HSP90 in the tumor tissues from colon cancer patients, in comparison with the non-tumor tissues from the same patients. Expression level of HOP was significantly increased in the tumor tissues (68% of patients, n = 19). Levels of HSC70 and HSP90 were also increased in the tumor tissues (95% and 74% of patients, respectively), and the HOP level was highly correlated with those of HSP90 (r = 0.77, p < 0.001) and HSC70 (r = 0.68, p < 0.01). Immunoprecipitation experiments indicated that HOP complexes with HSC70 or HSP90 in the tumor tissues. These data are consistent with increased formation of co-chaperone complexes in colon tumor specimens compared to adjacent normal tissue and could reflect a role for HOP in this process
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