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Heat shock protein A2 is a novel extracellular vesicle-associated protein.
Sojka, Damian Robert; Abramowicz, Agata; Adamiec-Organisciok, Malgorzata; Karnas, Elzbieta; Mielanczyk, Lukasz; Kania, Daria; Blamek, Slawomir; Telka, Ewa; Scieglinska, Dorota.
Afiliación
  • Sojka DR; Maria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeze Armii Krajowej 15, 44-102, Gliwice, Poland.
  • Abramowicz A; Maria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeze Armii Krajowej 15, 44-102, Gliwice, Poland.
  • Adamiec-Organisciok M; Maria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeze Armii Krajowej 15, 44-102, Gliwice, Poland.
  • Karnas E; Department of Systems Biology and Engineering, Silesian University of Technology, Institute of Automatic Control, Akademicka 16, 44-100, Gliwice, Poland.
  • Mielanczyk L; Department of Cell Biology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7 St., 30-387, Kraków, Poland.
  • Kania D; Department of Histology and Cell Pathology, Faculty of Medical Sciences in Zabrze, Medical University of Silesia, Katowice, Poland.
  • Blamek S; Maria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeze Armii Krajowej 15, 44-102, Gliwice, Poland.
  • Telka E; Maria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeze Armii Krajowej 15, 44-102, Gliwice, Poland.
  • Scieglinska D; Maria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeze Armii Krajowej 15, 44-102, Gliwice, Poland.
Sci Rep ; 13(1): 4734, 2023 03 23.
Article en En | MEDLINE | ID: mdl-36959387
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Vesículas Extracelulares / Neoplasias Tipo de estudio: Risk_factors_studies Límite: Humans Idioma: En Revista: Sci Rep Año: 2023 Tipo del documento: Article País de afiliación: Polonia Pais de publicación: Reino Unido
Texto completo
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XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Vesículas Extracelulares / Neoplasias Tipo de estudio: Risk_factors_studies Límite: Humans Idioma: En Revista: Sci Rep Año: 2023 Tipo del documento: Article País de afiliación: Polonia Pais de publicación: Reino Unido