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  1. AU="Natália Pinto de Almeida"
  2. AU="Spagnolo-Allende, Antonio J"
  3. AU="Jenninger, B"
  4. AU="Kerenza Hood"
  5. AU="Khan Chachar, Aijaz Zeeshan"
  6. AU="Yuan, Weiming"

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  1. Article ; Online: Sheltered in Stromal Tissue Cells, Trypanosoma cruzi Orchestrates Inflammatory Neovascularization via Activation of the Mast Cell Chymase Pathway

    Lucas Vellasco / Erik Svensjö / Carlos Alberto Bulant / Pablo Javier Blanco / Fábio Nogueira / Gilberto Domont / Natália Pinto de Almeida / Clarissa Rodrigues Nascimento / Danielle Silva-dos-Santos / Carla Eponina Carvalho-Pinto / Emiliano Horácio Medei / Igor C. Almeida / Julio Scharfstein

    Pathogens, Vol 11, Iss 187, p

    2022  Volume 187

    Abstract: Microangiopathy may worsen the clinical outcome of Chagas disease. Given the obstacles to investigating the dynamics of inflammation and angiogenesis in heart tissues parasitized by Trypanosoma cruzi , here we used intravital microscopy (IVM) to ... ...

    Abstract Microangiopathy may worsen the clinical outcome of Chagas disease. Given the obstacles to investigating the dynamics of inflammation and angiogenesis in heart tissues parasitized by Trypanosoma cruzi , here we used intravital microscopy (IVM) to investigate microcirculatory alterations in the hamster cheek pouch (HCP) infected by green fluorescent protein-expressing T. cruzi (GFP- T. cruzi ). IVM performed 3 days post-infection (3 dpi) consistently showed increased baseline levels of plasma extravasation. Illustrating the reciprocal benefits that microvascular leakage brings to the host-parasite relationship, these findings suggest that intracellular amastigotes, acting from inside out, stimulate angiogenesis while enhancing the delivery of plasma-borne nutrients and prosurvival factors to the infection foci. Using a computer-based analysis of images (3 dpi), we found that proangiogenic indexes were positively correlated with transcriptional levels of proinflammatory cytokines (pro-IL1β and IFN-γ). Intracellular GFP-parasites were targeted by delaying for 24 h the oral administration of the trypanocidal drug benznidazole. A classification algorithm showed that benznidazole (>24 h) blunted angiogenesis (7 dpi) in the HCP. Unbiased proteomics (3 dpi) combined to pharmacological targeting of chymase with two inhibitors (chymostatin and TY-51469) linked T. cruzi -induced neovascularization (7 dpi) to the proangiogenic activity of chymase, a serine protease stored in secretory granules from mast cells.
    Keywords Trypanosoma cruzi ; angiogenesis ; inflammation ; mast cell ; chymase ; Medicine ; R
    Language English
    Publishing date 2022-01-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Monitoring casbene synthase in Jatropha curcas tissues using targeted proteomics

    Natália Pinto de Almeida / Domingos Ferreira Mélo Neto / Gabriel Reis Alves Carneiro / Andreza Raquel Barbosa de Farias / Gilberto Barbosa Domont / Francisco de Assis de Paiva Campos / Fábio César Sousa Nogueira

    Plant Methods, Vol 17, Iss 1, Pp 1-

    2021  Volume 13

    Abstract: Abstract Background Casbene synthase (CS) is responsible for the first committed step in the biosynthesis of phorbol esters (PE) in the Euphorbiaceae. PE are abundant in the seeds of the biofuel crop Jatropha curcas and its toxicity precludes the use of ... ...

    Abstract Abstract Background Casbene synthase (CS) is responsible for the first committed step in the biosynthesis of phorbol esters (PE) in the Euphorbiaceae. PE are abundant in the seeds of the biofuel crop Jatropha curcas and its toxicity precludes the use of the protein-rich cake obtained after oil extraction as an animal feed and the toxicity of the fumes derived from burning PE containing biofuel is also a matter of concern. This toxicity is a major hindrance to exploit the potential of this crop as a source of raw material to produce biodiesel. For this reason, the current research on J. curcas is mainly focused on the understanding of the biosynthesis and site of synthesis of PE, as an avenue for the development of genotypes unable to synthesize PE in its seeds. Results Here, we present targeted proteomics assays (SRM and PRM) to detect and quantify CS in leaves, endosperm, and roots of two J. curcas genotypes with contrasting levels of PE. These assays were based on the use of reference isotopic labeled synthetic peptides (ILSP) predicted from 12 gene models of CS from the J. curcas genome. Conclusion Our targeted proteomics methods were able to detect and quantify, for the first time, CS gene products and demonstrate the distribution of CS isoforms only in roots from J. curcas genotypes with a high and low concentration of PE. These methods can be expanded to monitor CS, at the protein level, in different tissues and genotypes of J. curcas.
    Keywords Biofuel crops ; Secondary metabolism ; Phorbol esters ; Mass spectrometry ; Targeted proteomics ; Selected reaction monitoring ; Plant culture ; SB1-1110 ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2021-02-01T00:00:00Z
    Publisher BMC
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: The human melanoma proteome atlas—Defining the molecular pathology

    Lazaro Hiram Betancourt / Jeovanis Gil / Yonghyo Kim / Viktória Doma / Uğur Çakır / Aniel Sanchez / Jimmy Rodriguez Murillo / Magdalena Kuras / Indira Pla Parada / Yutaka Sugihara / Roger Appelqvist / Elisabet Wieslander / Charlotte Welinder / Erika Velasquez / Natália Pinto deAlmeida / Nicole Woldmar / Matilda Marko‐Varga / Krzysztof Pawłowski / Jonatan Eriksson /
    Beáta Szeitz / Bo Baldetorp / Christian Ingvar / Håkan Olsson / Lotta Lundgren / Henrik Lindberg / Henriett Oskolas / Boram Lee / Ethan Berge / Marie Sjögren / Carina Eriksson / Dasol Kim / Ho Jeong Kwon / Beatrice Knudsen / Melinda Rezeli / Runyu Hong / Peter Horvatovich / Tasso Miliotis / Toshihide Nishimura / Harubumi Kato / Erik Steinfelder / Madalina Oppermann / Ken Miller / Francesco Florindi / Qimin Zhou / Gilberto B. Domont / Luciana Pizzatti / Fábio C. S. Nogueira / Peter Horvath / Leticia Szadai / József Tímár / Sarolta Kárpáti / A. Marcell Szász / Johan Malm / David Fenyö / Henrik Ekedahl / István Balázs Németh / György Marko‐Varga

    Clinical and Translational Medicine, Vol 11, Iss 7, Pp n/a-n/a (2021)

    2021  

    Abstract: Abstract The MM500 study is an initiative to map the protein levels in malignant melanoma tumor samples, focused on in‐depth histopathology coupled to proteome characterization. The protein levels and localization were determined for a broad spectrum of ... ...

    Abstract Abstract The MM500 study is an initiative to map the protein levels in malignant melanoma tumor samples, focused on in‐depth histopathology coupled to proteome characterization. The protein levels and localization were determined for a broad spectrum of diverse, surgically isolated melanoma tumors originating from multiple body locations. More than 15,500 proteoforms were identified by mass spectrometry, from which chromosomal and subcellular localization was annotated within both primary and metastatic melanoma. The data generated by global proteomic experiments covered 72% of the proteins identified in the recently reported high stringency blueprint of the human proteome. This study contributes to the NIH Cancer Moonshot initiative combining detailed histopathological presentation with the molecular characterization for 505 melanoma tumor samples, localized in 26 organs from 232 patients.
    Keywords heterogeneity ; histopathology ; metastatic malignant melanoma ; proteogenomics ; subcellular localization ; Medicine (General) ; R5-920
    Language English
    Publishing date 2021-07-01T00:00:00Z
    Publisher Wiley
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: The Human Melanoma Proteome Atlas—Complementing the melanoma transcriptome

    Lazaro Hiram Betancourt / Jeovanis Gil / Aniel Sanchez / Viktória Doma / Magdalena Kuras / Jimmy Rodriguez Murillo / Erika Velasquez / Uğur Çakır / Yonghyo Kim / Yutaka Sugihara / Indira Pla Parada / Beáta Szeitz / Roger Appelqvist / Elisabet Wieslander / Charlotte Welinder / Natália Pinto deAlmeida / Nicole Woldmar / Matilda Marko‐Varga / Jonatan Eriksson /
    Krzysztof Pawłowski / Bo Baldetorp / Christian Ingvar / Håkan Olsson / Lotta Lundgren / Henrik Lindberg / Henriett Oskolas / Boram Lee / Ethan Berge / Marie Sjögren / Carina Eriksson / Dasol Kim / Ho Jeong Kwon / Beatrice Knudsen / Melinda Rezeli / Johan Malm / Runyu Hong / Peter Horvath / A. Marcell Szász / József Tímár / Sarolta Kárpáti / Peter Horvatovich / Tasso Miliotis / Toshihide Nishimura / Harubumi Kato / Erik Steinfelder / Madalina Oppermann / Ken Miller / Francesco Florindi / Quimin Zhou / Gilberto B. Domont

    Clinical and Translational Medicine, Vol 11, Iss 7, Pp n/a-n/a (2021)

    2021  

    Abstract: Abstract The MM500 meta‐study aims to establish a knowledge basis of the tumor proteome to serve as a complement to genome and transcriptome studies. Somatic mutations and their effect on the transcriptome have been extensively characterized in melanoma. ...

    Abstract Abstract The MM500 meta‐study aims to establish a knowledge basis of the tumor proteome to serve as a complement to genome and transcriptome studies. Somatic mutations and their effect on the transcriptome have been extensively characterized in melanoma. However, the effects of these genetic changes on the proteomic landscape and the impact on cellular processes in melanoma remain poorly understood. In this study, the quantitative mass‐spectrometry‐based proteomic analysis is interfaced with pathological tumor characterization, and associated with clinical data. The melanoma proteome landscape, obtained by the analysis of 505 well‐annotated melanoma tumor samples, is defined based on almost 16 000 proteins, including mutated proteoforms of driver genes. More than 50 million MS/MS spectra were analyzed, resulting in approximately 13,6 million peptide spectrum matches (PSMs). Altogether 13 176 protein‐coding genes, represented by 366 172 peptides, in addition to 52 000 phosphorylation sites, and 4 400 acetylation sites were successfully annotated. This data covers 65% and 74% of the predicted and identified human proteome, respectively. A high degree of correlation (Pearson, up to 0.54) with the melanoma transcriptome of the TCGA repository, with an overlap of 12 751 gene products, was found. Mapping of the expressed proteins with quantitation, spatiotemporal localization, mutations, splice isoforms, and PTM variants was proven not to be predicted by genome sequencing alone. The melanoma tumor molecular map was complemented by analysis of blood protein expression, including data on proteins regulated after immunotherapy. By adding these key proteomic pillars, the MM500 study expands the knowledge on melanoma disease.
    Keywords acetylation stoichiometry ; BRAF ; driver mutations ; histopathology ; metastatic melanoma ; phosphorylation ; Medicine (General) ; R5-920
    Subject code 572
    Language English
    Publishing date 2021-07-01T00:00:00Z
    Publisher Wiley
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Inter-library loan at ZB MED

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