The Impact of Classification of Interest on Predictive Toxicogenomics

The era of toxicogenomics has introduced a new way of monitoring the effect of environmental stressors and toxicants on biological systems via quantification of changes in gene expression. Because the liver is one of the major organs for synthesis and secretion of substances which metabolize endogenous and exogenous materials, there has been a great deal of interest in elucidating predictive and mechanistic genomic markers of hepatotoxicity. This mini-review will bring context to a limited number of toxicogenomics studies which used genomics to evaluate the transcriptional changes in blood and liver in response to acetaminophen (APAP) or other liver toxicants, but differed according to the classification of interest (COI), i.e., the partitioning of the samples a priori according to a common toxicological characteristic. The toxicogenomics studies highlighted are characterized by a classification of either no/low vs. high APAP dose exposure, none vs. observed necrosis, and severity of necrosis. The overlap or lack thereof between the gene classifiers and the modulated biological processes that are elucidated will be discussed to enhance the understanding of the effect of the particular COI model and experimental design used for prediction

The role of molecular chaperonins in warm ischemia and reperfusion injury in the steatotic liver: A proteomic study

BACKGROUND: The molecular basis of the increased susceptibility of steatotic livers to warm ischemia/reperfusion (I/R) injury during transplantation remains undefined. Animal model for warm I/R injury was induced in obese Zucker rats. Lean Zucker rats provided controls. Two dimensional differential gel electrophoresis was performed with liver protein extracts. Protein features with significant abundance ratios (p < 0.01) between the two cohorts were selected and analyzed with HPLC/MS. Proteins were identified by Uniprot database. Interactive protein networks were generated using Ingenuity Pathway Analysis and GRANITE software. RESULTS: The relative abundance of 105 proteins was observed in warm I/R injury. Functional grouping revealed four categories of importance: molecular chaperones/endoplasmic reticulum (ER) stress, oxidative stress, metabolism, and cell structure. Hypoxia up-regulated 1, calcium binding protein 1, calreticulin, heat shock protein (HSP) 60, HSP-90, and protein disulfide isomerase 3 were chaperonins significantly (p < 0.01) down-regulated and only one chaperonin, HSP-1was significantly upregulated in steatotic liver following I/R. CONCLUSION: Down-regulation of the chaperones identified in this analysis may contribute to the increased ER stress and, consequently, apoptosis and necrosis. This study provides an initial platform for future investigation of the role of chaperones and therapeutic targets for increasing the viability of steatotic liver allografts

Valley View Farm: Main House

Prepared by the Fall 2011 Conservation of Historic Building Materials class. This historic structure report provided an assessment of present conditions, historic context, and recommendations for on going preservation of the main house located at Valley View Farm in Cartersville, Georgia. The purpose of this HSR is to provide the owners of the main house with a holistic examination of the structure and integrity of the house. Recommendations made are based on the Secretary of Interior’s Standards for Treatment of Historic Properties to maximize optimal long term preservation of this National Register property.https://scholarworks.gsu.edu/history_heritagepreservation/1041/thumbnail.jp

Description of S-Score: Expression Analysis of Affymetrix GeneChips from Probe-Level Data

2 What’s new in this version 2 3 Reading in data and generating S-Scores

Description of S-Score: Expression Analysis of Affymetrix GeneChips from Probe-Level Data

2 What’s new in this version 2 3 Reading in data and generating S-Scores

Targeting of venom phospholipases: The strongly anticoagulant phospholipase A2 from Naja nigricollis venom binds to coagulation factor Xa to inhibit the prothrombinase complex

10.1006/abbi.1999.1345Archives of Biochemistry and Biophysics3691107-113ABBI