Abstract

Pulmonary Fibrosis and Proteostasis

Author(s): Pablo Rumano

The proteostasis network is made up of several specialized proteins that are required for the correct operation of processes that regulate the life cycle of all cellular proteins. Through the action of molecular chaperones, newly translated proteins are folded into their natural state and transported to specified subcellular sites. Damaged or no longer required proteins are destroyed by the ubiquitin-proteasome or lysosomal degradation processes. The intracellular proteome faces a major challenge when the proteostasis network is disrupted at any point, resulting in a relative imbalance in functional levels of critical proteins in subcellular compartments and the accumulation of misfolded or damaged proteins that are prone to aggregate or precipitate in the remarkably protein-rich intracellular environment. The molecular "chaperone" in humans is made up of 332 genes that play a variety of roles in protein folding. The Heat Shock Protein (HSP) family, as well as proteins involved in organelle-specific folding in the endoplasmic reticulum and mitochondria, is among these chaperones.