Abstract
| Lingua originale | English |
|---|---|
| Numero di pagine | 8 |
| Rivista | PLoS One |
| Volume | 7 |
| Stato di pubblicazione | Published - 2012 |
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All Science Journal Classification (ASJC) codes
- Biochemistry, Genetics and Molecular Biology(all)
- Agricultural and Biological Sciences(all)
- General
Cita questo
The odyssey of Hsp60 from tumor cells to other destinations includes plasma membrane-associated stages and Golgi and exosomal protein-trafficking modalities. / Burgio, Giosalba; Fucarino, Alberto Giuseppe; Bucchieri, Fabio; Zummo, Giovanni; Farina, Felicia; David, Sabrina; Cappello, Francesco; Corona, Davide; Campanella, Claudia; Campanella, Claudia; Burgio, Giosalba; Bucchieri, Fabio; Corona, Davide F. V.; Barbieri, Giovanna; Cappello, Francesco; Conway De Macario, Everly; Macario, Alberto J. L.; Merendino, Anna Maria.
In: PLoS One, Vol. 7, 2012.Risultato della ricerca: Article
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TY - JOUR
T1 - The odyssey of Hsp60 from tumor cells to other destinations includes plasma membrane-associated stages and Golgi and exosomal protein-trafficking modalities
AU - Burgio, Giosalba
AU - Fucarino, Alberto Giuseppe
AU - Bucchieri, Fabio
AU - Zummo, Giovanni
AU - Farina, Felicia
AU - David, Sabrina
AU - Cappello, Francesco
AU - Corona, Davide
AU - Campanella, Claudia
AU - Campanella, Claudia
AU - Burgio, Giosalba
AU - Bucchieri, Fabio
AU - Corona, Davide F. V.
AU - Barbieri, Giovanna
AU - Cappello, Francesco
AU - Conway De Macario, Everly
AU - Macario, Alberto J. L.
AU - Merendino, Anna Maria
PY - 2012
Y1 - 2012
N2 - BACKGROUND:In a previous work we showed for the first time that human tumor cells secrete Hsp60 via exosomes, which are considered immunologically active microvesicles involved in tumor progression. This finding raised questions concerning the route followed by Hsp60 to reach the exosomes, its location in them, and whether Hsp60 can be secreted also via other mechanisms, e.g., by the Golgi. We addressed these issues in the work presented here.PRINCIPAL FINDINGS:We found that Hsp60 localizes in the tumor cell plasma membrane, is associated with lipid rafts, and ends up in the exosomal membrane. We also found evidence that Hsp60 localizes in the Golgi apparatus and its secretion is prevented by an inhibitor of this organelle.CONCLUSIONS/SIGNIFICANCE:We propose a multistage process for the translocation of Hsp60 from the inside to the outside of the cell that includes a combination of protein traffic pathways and, ultimately, presence of the chaperonin in the circulating blood. The new information presented should help in designing future strategies for research and for developing diagnostic-monitoring means useful in clinical oncology.
AB - BACKGROUND:In a previous work we showed for the first time that human tumor cells secrete Hsp60 via exosomes, which are considered immunologically active microvesicles involved in tumor progression. This finding raised questions concerning the route followed by Hsp60 to reach the exosomes, its location in them, and whether Hsp60 can be secreted also via other mechanisms, e.g., by the Golgi. We addressed these issues in the work presented here.PRINCIPAL FINDINGS:We found that Hsp60 localizes in the tumor cell plasma membrane, is associated with lipid rafts, and ends up in the exosomal membrane. We also found evidence that Hsp60 localizes in the Golgi apparatus and its secretion is prevented by an inhibitor of this organelle.CONCLUSIONS/SIGNIFICANCE:We propose a multistage process for the translocation of Hsp60 from the inside to the outside of the cell that includes a combination of protein traffic pathways and, ultimately, presence of the chaperonin in the circulating blood. The new information presented should help in designing future strategies for research and for developing diagnostic-monitoring means useful in clinical oncology.
UR - http://hdl.handle.net/10447/74549
M3 - Article
VL - 7
JO - PLoS One
JF - PLoS One
SN - 1932-6203
ER -