Biology subjects

Bhunia, P. K.

Publications and source records attributed to Bhunia, P. K..

2 recordsLinked to original sources

bioRxiv2024

A meta-analysis of age-dependent changes in extracellular vesicle proteins in C. elegans

Extracellular vesicles (EVs) contribute to the maintenance of organism-wide proteostasis by mediating intercellular communication. Loss of proteostasis and altered intercellular communication are associated with aging and age-related diseases, suggesting key roles for EVs. However, it is unclear how the proteome of the EVs changes with age. To identify EV-associated proteins (EVAPs) and their fate with age, we curated publicly available proteome data from C. elegans model organism. Our analysis reveals that EVs carry proteins that involve protein quality control. We found that abundance of the EV proteins changes significantly with age. Many of these EV proteins also aggregate with age and overlap with A{beta} driven protein aggregates. We also observe that a subset of proteins that alter their abundance in response to heat stress and pathogen infections are also associated with the EVs. Further, we identify human orthologs of C. elegans EVAPs from human brain tissues affected with Alzheimers disease. This meta-analysis highlights EVs proteome composition, their abundance changes, and aggregation during aging, disease and stress conditions. Overall, this study provides new insights into the dynamics of EV proteins during aging and may possibly help in identifying potential biomarkers for age-related diseases.

biochemistry↗

bioRxiv2024

The abundance change of age-regulated secreted proteins affects lifespan of C. elegans

Proteome integrity is vital for survival and failure to maintain it results in uncontrolled protein abundances, misfolding and aggregation which cause proteotoxicity. In multicellular organisms, proteotoxic stress is communicated among tissues to maintain proteome integrity for organismal stress resistance and survival. However, nature of these signalling molecules and their regulation in extracellular space is largely unknown. Secreted proteins are induced in response to various stresses and aging, indicating their roles in the inter tissue communication. To study fates of age-regulated proteins with potential localization to extracellular, we analysed publicly available age-related proteome data of C. elegans. We found that abundance of proteins with signal peptides (SP) increases with age and result in their aggregation. Intriguingly, these changes are differentially regulated in the lifespan mutants. A subset of these SP proteins is also found in the cargo of extracellular vesicles. Many of these proteins are novel and functionally uncharacterized. Reducing levels of a few extracellular proteins result in increasing lifespan. This suggest that uncontrolled levels of extracellular proteins might disturb proteostasis and limit the lifespan. Overall, our findings suggest that the age induced secreted proteins might be the potential candidates to be considered as biomarkers or for mitigating age-related pathological conditions.

biochemistry↗