Navegando por Palavras-chave "HSP70"

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    A new Paracoccidioides brasiliensis 70-kDa heat shock protein reacts with sera from paracoccidioidomycosis patients
    (Taylor & Francis Ltd, 2005-09-01) Bisio, L. C.; Silva, S. P.; Pereira, I. S.; Xavier, MAS; Venancio, E. J.; Puccia, R.; Soares, CMA; Felipe, MSS; Universidade de Brasília (UnB); Universidade Federal de Goiás (UFG); Universidade Federal de São Paulo (UNIFESP); Universidade Estadual de Londrina (UEL); Novo Nordisk Prod Farmaceut Brasil
    A cDNA coding for a new member of the 70-kDa heat shock proteins (HSP70) family from the dimorphic and pathogenic fungus, Paracoccidioides brasiliensis, was cloned and characterized. the cDNA-deduced sequence coded for 655 amino acid residues and showed 95% identity to a previously described P. brasiliensis hsp70 gene. Cytoplasmic and typical nuclear localization signals, which indicate induction upon stress, were identified in the deduced peptide. the complete hsp70 cDNA coding region was cloned into a pGEX 4T-3 plasmid and expressed in Escherichia coli as a glutathione-S-transferase-tagged fusion protein. the recombinant protein reacted with a rabbit polyclonal antibody against HSP70. Western immunoblot experiments demonstrated that sera from paracoccidioidomycosis patients recognized the purified recombinant protein, suggesting an immunological role for this protein in the infectious process. the antigenicity analysis of rHSP70 detected three internal peptides that could act as activators of T-cell proliferation.
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    Proteasome and heat shock protein 70 (HSP70) inhibitors as therapeutic alternative in multiple myeloma
    (Impact Journals Llc, 2017) Pereira Eugenio, Angela Isabel [UNIFESP]; Fook-Alves, Veruska Lia [UNIFESP]; de Oliveira, Mariana Bleker [UNIFESP]; Fernando, Rodrigo Carlini [UNIFESP]; Zanatta, Daniela B.; Strauss, Bryan Eric; Regis Silva, Maria Regina [UNIFESP]; Porcionatto, Marimelia Aparecida [UNIFESP]; Braga Colleoni, Gisele Wally [UNIFESP]
    HSP70 connects multiple signaling pathways that work synergistically to protect tumor cells from death by proteotoxic stress and represents a possible target to establish a new approach for multiple myeloma treatment. Therefore, bioluminescent cell lines RPMI8226-LUC-PURO and U266-LUC-PURO were treated with HSP70 (VER155008) and/or proteasome (bortezomib) inhibitors and immunodeficient mice were used for subcutaneous xenograft models to evaluate tumor growth reduction and tumor growth inhibition after treatment. Bioluminescence imaging was used to follow tumor response. Treatment with bortezomib showed similar to 60% of late apoptosis in RPMI8226-LUC-PURO (without additional benefit of VER155008 in this cell line). However, U266-LUC-PURO showed similar to 60% of cell death after treatment with VER155008 (alone or with bortezomib). RPMI8226-LUC-PURO xenograft presented tumor reduction by bioluminescence imaging after treatment with bortezomib, VER155008 or drug combination compared to controls. Treatment with bortezomib, alone or combined with VER155008, showed inhibition of tumor growth assessed by bioluminescence imaging after one week in both RPMI8226-LUC-PURO and U266-LUC-PURO cell lines when compared to controls. In conclusion, our study shows that the combination of proteasome and HSP70 inhibitors induced cell death in tumor cells in vitro (late apoptosis induction) and in vivo (inhibition of tumor growth) with special benefit in U266-LUC-PURO, bearing 17p deletion.