No abstract

The potential for radiomics to support oncology decision-making has grown substantially in recent years, as these scanning techniques have been found to offer unique information regarding the tumor phenotype and microenvironment that is distinct from that provided by genomic or proteomic assays. Radiomic and genomic (or proteomic) data can be correlated with one another, thereby facilitating radiogenomic efforts. Radiogenomically-informed biopsies have the potential to yield better pathological outcomes and can aid in the planning of more appropriate treatment strategies for cancer patients. However, the field lacks a unified software platform wherein radiomic and genomics/proteomic data could be brought together to conduct a variety of correlational analyses and build robust artificial intelligence models that would aid the prediction of genomic/proteomic profiles of tumors from their radiological images. We have built such a comprehensive platform that could be utilized by scientists and clinicians globally to conduct radiogenomic studies for a variety of cancer types, and further validate and deploy it in clinics to aid effective monitoring, diagnosis, and treatment of cancer patients. Citation Format: Shrey S. Sukhadia, Shivashankar H. Nagaraj, Olivier Gevaert, Sivakumaran Theru Arumugam, Aayush Tyagi, Pritam Mukherjee, A.P. Prathosh. A sophisticated bioinformatics framework for integrative study of radiomics and genomics profiles of tumors [abstract]. In: Proceedings of the AACR Virtual Special Conference on Artificial Intelligence, Diagnosis, and Imaging; 2021 Jan 13-14. Philadelphia (PA): AACR; Clin Cancer Res 2021;27(5_Suppl):Abstract nr PO-036.

Proteome imbalance can lead to protein misfolding and aggregation which is associated with pathologies. Protein aggregation can also be an active, organized process and can be exploited by cells as a survival strategy. In adverse conditions, it is beneficial to deposit the proteins in a condensate rather degrading and resynthesizing. Membrane less organelles (MLOs) are biological condensates formed through liquid liquid phase separation (LLPS), involving cellular components such as nucleic acids and proteins. LLPS is a regulated process, which when perturbed, can undergo a transition from a physiological liquid condensate to pathological solid-like protein aggregates. To understand how the MLO-associated proteins (MLO-APs) behave during aging, we performed a comparative meta analysis with age related proteome of C. elegans. We found that the MLO-APs are highly abundant throughout the lifespan. Interestingly, they are aggregating more in long-lived mutant worms compared to the age matched wildtype worms. GO term analysis revealed that the cell cycle and embryonic development are among the top enriched processes in addition to RNA metabolism RNP components. Considering antagonistic pleotropic nature of these developmental genes and post mitotic status of C. elegans, we assume that these proteins phase transit during post development. As the organism ages, these MLO-APs either mature to become more insoluble or dissolve in uncontrolled manner. However, in the long-lived daf-2 mutant worms, the MLOs may attain protective states due to enhanced proteostasis components and altered metabolism that eventually make these worms more protected.