Effects of Toxic Agents at the Protein Level: Quantitative Measurement of 213 Mouse Liver Proteins following Xenobiotic Treatment

Anderson, N. Leigh; GIERE, FREDERIC A.; NANCE, SHARRON L.; GEMMELL, M. ANNE; TOLLAKSEN, SANDRA L.; ANDERSON, NORMAN G.

doi:10.1093/toxsci/8.1.39

Cited by 8 publications

(8 citation statements)

References 7 publications

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“…Later similar methods were applied to analyze the effects of drugs and other toxic agents in rodent tissues, particularly liver. These studies examined the relationships between the effects of compounds within a mechanistic class (143,144) and showed that a mechanism outside the known class could be recognized based on a multivariate protein pattern change (145). Quantitative serum protein proteomics was used to show that a panel of high abundance acute phase-related proteins could give a better statistical measure of inflammation than the classical marker serum amyloid A (41).…”

Section: Plasma Diagnosticsmentioning

confidence: 99%

The Human Plasma Proteome

Anderson¹,

Anderson²

2002

Molecular & Cellular Proteomics

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The human plasma proteome holds the promise of a revolution in disease diagnosis and therapeutic monitoring provided that major challenges in proteomics and related disciplines can be addressed. Plasma is not only the primary clinical specimen but also represents the largest and deepest version of the human proteome present in any sample: in addition to the classical "plasma proteins," it contains all tissue proteins (as leakage markers) plus very numerous distinct immunoglobulin sequences, and it has an extraordinary dynamic range in that more than 10 orders of magnitude in concentration separate albumin and the rarest proteins now measured clinically. Although the restricted dynamic range of conventional proteomic technology (two-dimensional gels and mass spectrometry) has limited its contribution to the list of 289 proteins (tabulated here) that have been reported in plasma to date, very recent advances in multidimensional survey techniques promise at least double this number in the near future. Abundant scientific evidence, from proteomics and other disciplines, suggests that among these are proteins whose abundances and structures change in ways indicative of many, if not most, human diseases. Nevertheless, only a handful of proteins are currently used in routine clinical diagnosis, and the rate of introduction of new protein tests approved by the United States Food and Drug Administration (FDA) has paradoxically declined over the last decade to less than one new protein diagnostic marker per year. We speculate on the reasons behind this large discrepancy between the expectations arising from proteomics and the realities of clinical diagnostics and suggest approaches by which protein-disease associations may be more effectively translated into diagnostic tools in the future.

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Section: Plasma Diagnosticsmentioning

confidence: 99%

The Human Plasma Proteome

Anderson¹,

Anderson²

2002

Molecular & Cellular Proteomics

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3,840

1,585

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“…In a number of studies the effects of two or more stressors were compared and stressor-specific patterns of induced hsps have been described in various eukaryotes (Li, 1983; Anderson et al, 1987;F'ipkin et al, 1987;Aoki et al, 1990;Bounias-Vardiabasis et al, 1990; Deaton et al, 1990;Lai et al, 1993). In general, these studies favour the idea that different sets of proteins…”

Section: Incmentioning

confidence: 99%

Is heat shock protein re-induction during tolerance related to the stressor-specific induction of heat shock proteins?

et al. 1996

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The existence of stressor-specific induction programs of heat shock proteins (hsps) leads us to analyze the possible occurrence of a stressor-specific tolerance induced by either heat shock, arsenite, or cadmium. As a measure of this tolerance re-induction of hsps was studied. In this paper, we tested whether the refractory state is either valid for each specific hsp (implying independent regulation of every member of the heat shock protein family) or extends from small subsets of the hsp-family to even larger groups of proteins (indicating a more common denominator in their regulation). (re-)induction of hsps does not seem to be regulated at the level of each individual hsp since differences in induced synthesis of hsps between two stressor conditions are not supplemented systematically upon the sequential application of the two stressors. The most notable example in this respect is hsp60. A pretreatment with cadmium, which hardly induces synthesis of this hsp, does induce a tolerance to (re)-induction by heat shock, which normally induces hsp60. This suggests the existence of a more common denominator regulating the coordinate expression of at least some hsps. From our data we conclude that the degree, but not the pattern, of hsp re-induction is influenced by the type of stressor used in the pretreatment. The pattern of hsps induced by a secondary applied stressor still shows most of its stressor-specificity and seems to be independent of any pretreatment. The possible implications of stressor-specificity are discussed.

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“…In order to facilitate comparison of the Wistarlivl with the F344MST3 pattern (master based on Fischer rat liver proteins [7]), spots present in both rat strains had been given identical master numbers. In this way the populations of liver proteins previously defined as components of subcellular organelles in the F344MST3 [8] could be transferred almost completely to the Wistarlivl pattern. In both experiments around 100 initial matches were set manually in each sample (object) pattern before the automatic matching procedure was started.…”

Section: Discussionmentioning

confidence: 95%

Effects of cyclosporine A on the rat liver and kidney protein pattern, and the influence of vitamin E and C coadministration

et al. 1995

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The effects of cyclosporine A (CsA), a potent immunosuppressive drug, were examined in rat liver and kidney samples using two-dimensional electrophoretic protein analysis. Of a total of 370 liver and 336 kidney spots analyzed, 8% (29 spots) and 6% (19 spots), respectively, showed a significant drug-induced change (p < 0.01), which was predominantly reflected in increased protein abundance (62% and 74% of the changes, respectively). Of the 48 proteins changed in either organ, 14 were most probably common to both tissues and one of these was significantly increased in both the liver and the kidney. Most of the other 13 showed similar trends (either increases or decreases) in both organs. However, the most striking drug effect seen in this study concerned an unidentified protein present only in the kidney, which completely disappeared upon CsA treatment. It was also investigated whether the drug-induced changes could be prevented by the coadministration of the radical scavengers vitamin E and C with CsA. Spots changed by the administration of the drug were classified according to three different categories, based on their response profiles in rats treated with CsA in combination with the vitamins: (i) spots which were changed by CsA as well as by CsA in combination with the vitamins (12 liver and 4 kidney spots), (ii) spots which were changed by CsA and showed an additional increase of this change by CsA plus the vitamins (no liver and 4 kidney spots), and (iii) spots which were changed by CsA but not by CsA in combination with the vitamins (8 liver and 6 kidney spots). These results showed that in both organs the vitamins were able to prevent around 30% of the effects caused by CsA, and that two-dimensional gel electrophoresis is an excellent tool to demonstrate such drug interactions at the molecular level.

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Effects of Toxic Agents at the Protein Level: Quantitative Measurement of 213 Mouse Liver Proteins following Xenobiotic Treatment

Cited by 8 publications

References 7 publications

The Human Plasma Proteome

The Human Plasma Proteome

Is heat shock protein re-induction during tolerance related to the stressor-specific induction of heat shock proteins?

Effects of cyclosporine A on the rat liver and kidney protein pattern, and the influence of vitamin E and C coadministration

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