bioRxiv Science⌕ Search

Biology subjects

Thomas, C. T.

Publications and source records attributed to Thomas, C. T..

3 recordsLinked to original sources

Transcriptome features of striated muscle aging and predictability of protein level changes

RNA and protein levels correlate only partially and some transcripts are better correlated with their protein counterparts than others. This suggests that in aging and disease studies, some transcriptomics markers may carry more information in predicting protein-level changes. Here we applied a computational data analysis workflow to predict which transcriptomic changes are more likely relevant to protein-level regulation in striated muscle aging. The protein predictability of each transcript is estimated from existing large proteogenomics data sets, then transferred to new total RNA sequencing data comparing skeletal muscle and cardiac muscle in young adult (~4 months) mice vs. early aging (~20 months) mice. Aging cardiac and skeletal muscles both invoke transcriptomic changes in innate immune system and mitochondria pathways but diverge in extracellular matrix processes. On an individual gene level, we identified 611 age-associated signatures in skeletal and cardiac muscles at 10% FDR, including a number of myokine and cardiokine encoding genes. We estimate that about 48% of the aging-associated transcripts may predict protein levels well (r [≥] 0.5). In parallel, a comparison of the identified aging-regulated genes with public human transcriptomics data showed that only 35-45% of the identified genes show an age-dependent expression in corresponding human tissues. Finally, integrating both RNA-protein correlation and human conservation across data sources, we nominate 134 prioritized aging striated muscle signature genes that are predicted to correlate strongly with protein levels and that show age-dependent expression in humans. These prioritized signatures may hold promise to understanding heart and skeletal muscle physiology in human and mouse aging.

physiology↗

Proteomic signatures of acute oxidative stress response to paraquat in the mouse heart

The heart is sensitive to oxidative damage but a global view on how the cardiac proteome responds to oxidative stressors has yet to fully emerge. Using quantitative tandem mass spectrometry, we assessed the effects of acute exposure of the oxidative stress inducer paraquat on protein expression in mouse hearts. We observed widespread protein expression changes in the paraquat-exposed heart especially in organelle-containing subcellular fractions. During cardiac response to acute oxidative stress, proteome changes are consistent with a rapid reduction of mitochondrial metabolism, coupled with activation of multiple antioxidant proteins, reduction of protein synthesis and remediation of proteostasis. In addition to differential expression, we saw evidence of spatial reorganizations of the cardiac proteome including the translocation of hexokinase 2 to more soluble fractions. Treatment with the antioxidants Tempol and MitoTEMPO reversed many proteomic signatures of paraquat but this reversal was incomplete. We also identified a number of proteins with unknown function in the heart to be triggered by paraquat, suggesting they may have functions in oxidative stress response. Surprisingly, protein expression changes in the heart correlate poorly with those in the lung, consistent with differential sensitivity or stress response in these two organs. The results provide insights into oxidative stress responses in the heart and may avail the search for new therapeutic targets.

physiology↗

Identifying high-priority proteins across the human diseasome using semantic similarity

Knowledge of \"popular proteins\" has been a focus of multiple Human Proteome Organization (HUPO) initiatives and can guide the development of proteomics assays targeting important disease pathways. We report here an updated method to identify prioritized protein lists from the research literature, and apply it to catalog lists of important proteins across multiple cell types, sub-anatomical regions, and disease phenotypes of interest. We provide a systematic collection of popular proteins across 10,129 human diseases as defined by the Disease Ontology, 10,642 disease phenotypes defined by Human Phenotype Ontology, and 2,370 cellular pathways defined by Pathway Ontology. This strategy allows instant retrieval of popular proteins across the human \"diseasome\", and further allows reverse queries from protein to disease, enabling functional analysis of experimental protein lists using bibliometric annotations.

bioinformatics↗