searching for new clues about the molecular cause of endomyocardial fibrosis by way of in silico proteomics and analytical chemistry寻找新的线索endomyocardial纤维化的分子造成的硅片蛋白质组学和分析化学.pdfVIP

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2017-09-09 发布于上海
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searching for new clues about the molecular cause of endomyocardial fibrosis by way of in silico proteomics and analytical chemistry寻找新的线索endomyocardial纤维化的分子造成的硅片蛋白质组学和分析化学.pdf

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searching for new clues about the molecular cause of endomyocardial fibrosis by way of in silico proteomics and analytical chemistry寻找新的线索endomyocardial纤维化的分子造成的硅片蛋白质组学和分析化学

Searching for New Clues about the Molecular Cause of Endomyocardial Fibrosis by Way of In Silico Proteomics and Analytical Chemistry Misaki Wayengera* Division of Molecular Pathology, Department of Pathology, School of Biomedical Sciences, College of Health Sciences, Makerere University, Kampala, Uganda Abstract Background: Endomyocardial Fibrosis (EMF) –is a chronic inflammatory disease of the heart with related pathology to that of late stage Chaga’s disease. Indeed, both diseases are thought to result from auto-immune responses against myocardial tissue. As is the case that molecular mimicry between the acidic termini of Trypanosoma cruzi ribosomal P0, P1 and P2b (or simply TcP0, TcP1, and TcP2b) proteins and myocardial tissue causes Chaga’s disease, excessive exposure to certain infections, toxins including cassava ones, allergy and malnutrition has been suggested as the possible cause for EMF. Recent studies have defined the proteomic characteristics of the T. cruzi ribosomal P protein-C-termini involved in mediating auto- immunity against Beta1-adrenergic receptors of the heart in Chaga’s disease. This study aimed to investigate the similarity of C-termini of TcP0/TcP2b to sequences and molecules of several plants, microbial, viral and chemical elements- most prior thought to be possible causative agents for EMF. Methods and Principal Findings: Comparative Sequence alignments and phylogeny using the BLAST-P tool at the Swiss Institute of Biotechnology (SIB) revealed homologs of C-termini of TcP0 and TcP2b among related proteins from several eukaryotes including the animals (Homo sapiens, C. elegans, D. melanogaster), plants (Arabidopsis thaliana, Zea mays, Glycina Max, Oryza sativa, Rhizopus oryzae) and protozoa (P. falciparum, T. gondii, Leishmania spp).The chemical formulae of the two T.cruzi ribosomal protein C-terminal peptides were