21 research outputs found
Comparison of the proteome profiling of Iranian isolates of Leishmania tropica, L. major and L. infantum by two-dimensional electrophoresis (2-DE) and mass-spectrometry
Background:
The mechanisms of virulence and species differences of Leishmania parasites are under the influence of gene expression regulations at posttranscriptional stages. In Iran, L. major and L. tropica are known as principal agents of cutaneous leishmaniasis, while L. infantum causes visceral leishmaniasis.
Methods:
As a preliminary study, we compared the proteome mapping of the above three Iranian isolates of Leishmania species through the 2-dimension electrophoresis (2-DE), and identified the prominent proteins by Liquid Chromatography (LC) mass spectrometry.
Results:
We reproducibly detected about 700 protein spots in each species by using the Melanie software. Totally, 264 proteins exhibited significant changes among 3 species. Forty nine protein spots identified in both L. tropica and L. major were similar in position in the gel, whereas only 35 of L. major proteins and 10 of L. tropica proteins were matched with those of L. infantum. Having identified 24 proteins in the three species, we sought to provide possible explanations for their differential expression patterns and discuss their relevance to cell biology.
Conclusion:
The comparison of proteome profiling pattern of the 3 species identified limit up and limit down regulated or absent /present proteins. In addition, the LC-MS data analysis showed that most of the protein spots with differential abundance in the 3 species are involved in cell motility and cytoskeleton, cell signaling and vesicular trafficking, intracellular survival / proteolysis, oxidative stress defense, protein synthesis, protein ubiquitination / proteolysis, and stress related proteins. Differentially proteins distributed among the species maybe implicated in host pathogenecity interactions and parasite tropism to cutaneous or visceral tissue macrophages
200+Protein Concentrations in Healthy Human Blood Plasma: Targeted Quantitative SRM SIS Screening of Chromosomes 18, 13, Y, and the Mitochondrial Chromosome Encoded Proteome
Mitochondria are undeniably the cell powerhouse,
directly affecting cell survival and fate. Growing
evidence suggest that mitochondrial protein repertoire affects
metabolic activity and plays an important role in determining
cell proliferation/differentiation or quiescence shift. Consequently,
the bioenergetic status of a cell is associated with
the quality and abundance of the mitochondrial populations
and proteomes. Mitochondrial morphology changes in the
development of different cellular functions associated with
metabolic switches. It is therefore reasonable to speculate that
different cell lines do contain different mitochondrialassociated
proteins, and the investigation of these pools may
well represent a source for mining missing proteins (MPs). A
very effective approach to increase the number of IDs through mass spectrometry consists of reducing the complexity of the
biological samples by fractionation. The present study aims at investigating the mitochondrial proteome of five phenotypically
different cell lines, possibly expressing some of the MPs, through an enrichment 12fractionation approach at the organelle and
protein level. We demonstrate a substantial increase in the proteome coverage, which, in turn, increases the likelihood of
detecting low abundant proteins, often falling in the category of MPs, and resulting, for the present study, in the identification of
METTL12, FAM163A, and RGS13. All MS data have been deposited to the MassIVE data repository (https://massive.ucsd.
edu) with the data set identifier MSV000082409 and PXD010446