We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Heat shock protein A2 is a novel extracellular vesicle-associated protein.
- Authors
Sojka, Damian Robert; Abramowicz, Agata; Adamiec-Organiściok, Małgorzata; Karnas, Elżbieta; Mielańczyk, Łukasz; Kania, Daria; Blamek, Sławomir; Telka, Ewa; Scieglinska, Dorota
- Abstract
70-kDa Heat Shock Proteins (HSPA/HSP70) are chaperones playing a central role in the proteostasis control mechanisms. Their basal expression can be highly elevated as an adaptive response to environmental and pathophysiological stress conditions. HSPA2, one of poorly characterised chaperones of the HSPA/HSP70 family, has recently emerged as epithelial cells differentiation-related factor. It is also commonly expressed in cancer cells, where its functional significance remains unclear. Previously, we have found that proteotoxic stress provokes a decrease in HSPA2 levels in cancer cells. In the present study we found that proteasome inhibition-related loss of HSPA2 from cancer cells neither is related to a block in the gene transcription nor does it relate to increased autophagy-mediated disposals of the protein. Proteotoxic stress stimulated extracellular release of HSPA2 in extracellular vesicles (EVs). Interestingly, EVs containing HSPA2 are also released by non-stressed cancer and normal cells. In human urinary EVs levels of HSPA2 were correlated with the levels of TSG101, one of the main EVs markers. We conclude that HSPA2 may constitute basic components of EVs. Nevertheless, its specific role in EVs and cell-to-cell communication requires further investigation.
- Subjects
HEAT shock proteins; CANCER cells; EXTRACELLULAR vesicles; TUMOR susceptibility gene 101; EPITHELIAL cells; PROTEINS
- Publication
Scientific Reports, 2023, Vol 13, Issue 1, p1
- ISSN
2045-2322
- Publication type
Article
- DOI
10.1038/s41598-023-31962-5