LUCIANA NOGUEIRA DE SOUSA ANDRADE

(Fonte: Lattes)
Índice h a partir de 2011
10
Projetos de Pesquisa
Unidades Organizacionais
Instituto do Câncer do Estado de São Paulo, Hospital das Clínicas, Faculdade de Medicina
LIM/24 - Laboratório de Oncologia Experimental, Hospital das Clínicas, Faculdade de Medicina

Resultados de Busca

Agora exibindo 1 - 6 de 6
  • article 13 Citação(ões) na Scopus
    Binding Affinity, Specificity and Comparative Biodistribution of the Parental Murine Monoclonal Antibody MX35 (Anti-NaPi2b) and Its Humanized Version Rebmab200
    (2015) LINDEGREN, Sture; ANDRADE, Luciana N. S.; BACK, Tom; MACHADO, Camila Maria L.; HORTA, Bruno Brasil; BUCHPIGUEL, Carlos; MORO, Ana Maria; OKAMOTO, Oswaldo Keith; JACOBSSON, Lars; CEDERKRANTZ, Elin; WASHIYAMA, Kohshin; ANEHEIM, Emma; PALM, Stig; JENSEN, Holger; TUMA, Maria Carolina B.; CHAMMAS, Roger; HULTBORN, Ragnar; ALBERTSSON, Per
    The aim of this preclinical study was to evaluate the characteristics of the monoclonal antibody Rebmab200, which is a humanized version of the ovarian-specific murine antibody MX35. This investigation contributes to the foundation for future clinical alpha-radioimmunotherapy of minimal residual ovarian cancer with At-211-Rebmab200. Here, the biodistribution of 211At-Rebmab200 was evaluated, as was the utility of Tc-99m-Rebmab200 for bioimaging. Rebmab200 was directly compared with its murine counterpart MX35 in terms of its in-vitro capacity for binding the immobilized NaPi2B epitope and live cells; we also assessed its biodistribution in nude mice carrying subcutaneous OVCAR-3 tumors. Tumor antigen and cell binding were similar between Rebmab200 and murine MX35, as was biodistribution, including normal tissue uptake and in-vivo tumor binding. We also demonstrated that Tc-99m-Rebmab200 can be used for single-photon emission computed tomography of subcutaneous ovarian carcinomas in tumor-bearing mice. Taken together, our data support the further development of Rebmab200 for radioimmunotherapy and diagnostics.
  • article 4 Citação(ões) na Scopus
    Extracellular Vesicle-Packaged miR-195-5p Sensitizes Melanoma to Targeted Therapy with Kinase Inhibitors
    (2023) SANTOS, Nathalia L.; BUSTOS, Silvina O.; REIS, Patricia P.; CHAMMAS, Roger; ANDRADE, Luciana N. S.
    Management of advanced melanoma remains challenging, with most BRAF (B-Raf proto-oncogene, serine/threonine kinase)-mutated metastatic patients relapsing within a few months upon MAPK inhibitors treatment. Modulation of tumor-derived extracellular vesicle (EVs) cargo with enrichment of antitumoral molecules is a promising strategy to impair tumor progression and increase treatment response. Herein, we report that restored expression of miR-195-5p, down-regulated in melanoma favoring drug resistance, increases the release of EVs enriched in the tumor suppressor miRNAs, miR-195-5p, miR-152-3p, and miR-202-3p. Incorporating these EVs by bystander tumor cells resulted in decreased proliferation and viability, accompanied by a reduction in CCND1 and YAP1 mRNA levels. Upon treatment with MAPK inhibitors, miR-195 EVs significantly decreased BCL2-L1 protein levels and increased cell death ratio and treatment efficacy. Additionally, EVs exogenously loaded with miR-195-5p by electroporation reduced tumor volume in vivo and impaired engraftment and growth of xenografts implanted with melanoma cells exposed to MAPK inhibitors. Our study shows that miR-195-5p antitumoral activity can be spread to bystander cells through EVs, improving melanoma response to targeted therapy and revealing a promising EV-based strategy to increase clinical response in patients harboring BRAF mutations.
  • conferenceObject
    7-Ketocholesterol loaded-phosphatidylserine liposome induces cell death, autophagy, and growth inhibition of melanoma and breast adenocarcinoma.
    (2018) FAVERO, Giovani Marino; TORTELLI JR., Tharcisio Citrangulo; FERNANDES, Daniel; PRESTES, Ana Paula; KMETIUK, Louise N. B.; OTAKE, Andreia Hanada; ANDRADE, Luciana N. S.; FARIA, Daniele de Paula; CARNEIRO, Camila de Godoi; GARCEZ, Alexandre Teles; MARQUES, Fabio L. N.; CHAMMAS, Roger
  • conferenceObject
    MicroRNA-195 acts as a tumor suppressor miRNA in human melanoma cells by targeting Prohibitin 1.
    (2018) CIRILO, Priscila D. R.; CORREA, Bruna R. S.; QIAO, Mei; ANDRADE, Luciana N. S.; CHAMMAS, Roger; PENALVA, Luiz O. F.
  • article 10 Citação(ões) na Scopus
    NDRG4 promoter hypermethylation is a mechanistic biomarker associated with metastatic progression in breast cancer patients
    (2019) JANDREY, Elisa H. F.; MOURA, Ricardo P.; ANDRADE, Luciana N. S.; MACHADO, Camila L.; CAMPESATO, Luiz Felipe; LEITE, Katia Ramos M.; INOUE, Lilian T.; ASPRINO, Paula F.; SILVA, Ana Paula M. da; BARROS, Alfredo Carlos S. D. de; CARVALHO, Andre; LIMA, Vladmir C. de; CARRARO, Dirce M.; BRENTANI, Helena P.; CUNHA, Isabela W. da; SOARES, Fernando A.; PARMIGIANI, Raphael B.; CHAMMAS, Roger; CAMARGO, Anamaria A.; COSTA, Erico T.
    The risk of developing metastatic disease in breast cancer patients is traditionally predictable based on the number of positive axillary lymph nodes, complemented with additional clinicopathological factors. However, since lymph node-negative patients have a 20-30% probability of developing metastatic disease, lymph node information alone is insufficient to accurately assess individual risk. Molecular approaches, such as multigene expression panels, analyze a set of cancer-related genes that more accurately predict the early risk of metastasis and the treatment response. Here, we present N-Myc downstream-regulated gene 4 (NDRG4) epigenetic silencing as a mechanistic biomarker of metastasis in ductal invasive breast tumors. While aberrant NDRG4 DNA hypermethylation is significantly associated with the development of metastatic disease, downregulation of NDRG4 transcription and protein expression is functionally associated with enhanced lymph node adhesion and cell mobility. Here, we show that epigenetic silencing of NDRG4 modulates integrin signaling by assembling beta 1-integrins into large punctate clusters at the leading edge of tumor cells to promote an ""adhesive switch,"" decreasing cell adhesion to fibronectin and increasing cell adhesion and migration towards vitronectin, an important component of human lymph nodes. Taken together, our functional and clinical observations suggest that NDRG4 is a potential mechanistic biomarker in breast cancer that is functionally associated with metastatic disease.
  • article 1 Citação(ões) na Scopus
    Membrane-derived particles shed by PSMA-positive cells function as pro-angiogenic stimuli in tumors
    (2023) MACHADO, Camila M. L.; SKUBAL, Magdalena; HAEDICKE, Katja; SILVA, Fabio P.; STATER, Evan P.; SILVA, Thais L. A. de O.; COSTA, Erico T.; MASOTTI, Cibele; OTAKE, Andreia H.; ANDRADE, Luciana N. S.; JUNQUEIRA, Mara de S.; HSU, Hsiao-Ting; DAS, Sudeep; LARNEY, Benedict Mc; PRATT, Edwin C.; ROMIN, Yevgeniy; FAN, Ning; MANOVA-TODOROVA, Katia; POMPER, Martin; GRIMM, Jan
    Cell membrane-derived particles (Mp) are rounded membrane-enclosed particles that are shed from tumor cells. Mp are formed from tumor membranes and are capable of tumor targeting and immunotherapeutic agents because they share membrane homology with parental cells; thus, they are under consideration as a drug de-livery vehicle. Prostate-specific membrane antigen (PSMA), a transmembrane glycoprotein with enzymatic functionality, is highly expressed in Mp and extracellular vesicles (EV) from prostate cancer (PCa) with poor clinical prognosis. Although PSMA expression was previously shown in EV and Mp isolated from cell lines and from the blood of patients with high-grade PCa, no pathophysiological effects have been linked to PCa-derived Mp. Here, we compared Mp from PSMA-expressing (PSMA-Mp) and PSMA-non-expressing (WT-Mp) cells side by side in vitro and in vivo. PSMA-Mp can transfer PSMA and new phenotypic characteristics to the tumor micro -environment. The consequence of PSMA transfer to cells and increased secretion of vascular endothelial growth factor-A (VEGF-A), pro-angiogenic and pro-lymphangiogenic mediators, with increased 4E binding protein 1 (4EBP-1) phosphorylation.