Functional Proteomics Analysis of Signal Transduction Pathways of the Platelet-Derived Growth Factor β Receptor

Šoškić, Vukic; Görlach, Matthias; Poznanović, Slobodan; Boehmer, Frank‐D.; Godovac‐Zimmermann, Jasminka

doi:10.1021/bi982093r

Cited by 190 publications

(146 citation statements)

References 45 publications

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“…Protein identification was carried out by peptide mass fingerprinting on an Ettan matrix-assisted laser desorption/ ionization (MALDI) time of flight (TOF) Pro mass spectrometer (Amersham Biosciences), as previously described [35,36]. Electrophoretic spots, visualized by a colloidal Coomassie staining protocol, were manually excised, destained, and acetonitrile-dehydratated.…”

Section: Protein Identification By Mass Spectrometrymentioning

confidence: 99%

Exploring the biochemical mechanisms of cytotoxic gold compounds: a proteomic study

et al. 2010

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We have recently shown that a group of structurally diverse gold compounds are highly cytotoxic toward a panel of 36 human tumor cell lines through a variety of biochemical mechanisms. A classic proteomic approach is exploited here to gain deeper insight into those mechanisms. This investigation is focused on Auoxo6, a novel binuclear gold(III) complex, and auranofin, a clinically established gold(I) antiarthritic drug. First, the 72-h cytotoxicity profiles of Auoxo6 and auranofin were determined against A2780 human ovarian carcinoma cells. Subsequently, protein extraction from gold-treated A2780 cells sensitive to cisplatin and 2D gel electrophoresis separation were carried out according to established procedures. Notably, both metallodrugs caused relatively modest changes in protein expression in comparison with controls as only 11 out of approximately 1,300 monitored spots showed appreciable quantitative changes. Very remarkably, six altered proteins were in common between the two treatments. Eight altered proteins were identified by mass spectrometry; among them was ezrin, a protein associated with the cytoskeleton and involved in apoptosis. Interestingly, two altered proteins, i.e., peroxiredoxins 1 and 6, are known to play crucial roles in the cell redox metabolism. Increased cleavage of heterogeneous ribonucleoprotein H was also evidenced, consistent with caspase 3 activation. Overall, the results of the present proteomic study point out that the mode of action of Auoxo6 is strictly related to that of auranofin, that the induced changes in protein expression are limited and selective, that both gold compounds trigger caspase 3 activation and apoptosis, and that a few affected proteins are primarily involved in cell redox homeostasis.

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Section: Protein Identification By Mass Spectrometrymentioning

confidence: 99%

Exploring the biochemical mechanisms of cytotoxic gold compounds: a proteomic study

et al. 2010

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“…Functional proteomics of signal transduction pathways on growth-and bradikinin-receptors were investigated [126,127].…”

Section: Examples Of Successful Application Of Proteomicsmentioning

confidence: 99%

Two‐dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry

2006

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The proteome analysis by 2-DE is one of the most potent methods of analyzing the complete proteome of cells, cell lines, organs and tissues in proteomics studies. It allows a fast overview of changes in cell processes by analysis of the entire protein extracts in any biological and medical research projects. New instrumentation and advanced technologies provide proteomics studies in a wide variety of biological and biomedical questions. Proteomics work is being applied to study antibiotics-resistant strains and human tissues of various brain, lung, and heart diseases. It cumulated in the identification of antigens for the design of new vaccines. These advances in proteomics have been possible through the development of advanced high-resolution 2-DE systems allowing resolution of up to 10 000 protein spots of entire cell lysates in combination with protein identification by new highly sensitive mass spectrometric techniques. The present technological achievements are suited for a high throughput screening of different cell situations. Proteomics may be used to investigate the health effects of radiation and electromagnetic field to clarify possible dangerous alterations in human beings.

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“…The proteins were digested in-gel with trypsin as described by Hellman et al (16). Protein identification was performed using peptide mass fingerprinting with an Ettan MALDI-TOF Pro mass spectrometer (GE Healthcare Bio-Sciences, Uppsala, Sweden) as described previously (16,17).…”

Section: Laboratory Methodsmentioning

confidence: 99%

Serum albumin fragmentation in end-stage renal disease patients – a pilot study

Donadio

Pennacchio²,

Dimuccio³

et al. 2009

Clinical Chemistry and Laboratory Medicine

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Background: The goal of this study was to detect modification in the expression of plasma proteins and/or post-translational modifications of their structure in patients with end stage renal disease. Methods: Serum samples from 19 adult patients treated by maintenance hemodialysis (MHD) were analyzed in comparison to sera from six healthy controls using sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and two-dimensional electrophoresis (2DE). Spots of interest were identified by mass spectrometry analysis. In addition, the 2DE maps were incubated with a human anti-albumin polyclonal antibody. Results: SDS-PAGE gels, 2DE maps and matrix-assisted laser desorption/ionization time of flight analysis indicated over-expression of low-molecular weight proteins (LMWP) in sera from patients. Unexpectedly, another 15 spots with estimated M r of 12.5-29 kDa from the 2DE maps of six patients were identified as fragments of albumin. 2D immunoblotting of sera from 12 other patients detected numerous albumin fragments. Conclusions:These results indicate that in addition to increased expression of LMWP, a relevant amount of albumin fragments are detectable in the serum of patients undergoing MHD. Uremia appears to facilitate the fragmentation of albumin and/or the retention of albumin fragments in blood. Clin Chem Lab Med 2009;47:1373-9.

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Functional Proteomics Analysis of Signal Transduction Pathways of the Platelet-Derived Growth Factor β Receptor

Cited by 190 publications

References 45 publications

Exploring the biochemical mechanisms of cytotoxic gold compounds: a proteomic study

Exploring the biochemical mechanisms of cytotoxic gold compounds: a proteomic study

Two‐dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry

Serum albumin fragmentation in end-stage renal disease patients – a pilot study

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