The odyssey of Hsp60 from tumor cells to other destinations includes plasma membrane-associated stages and Golgi and exosomal protein-trafficking modalities

Giosalba Burgio, Alberto Giuseppe Fucarino, Fabio Bucchieri, Giovanni Zummo, Felicia Farina, Sabrina David, Francesco Cappello, Davide Corona, Claudia Campanella, Claudia Campanella, Giosalba Burgio, Fabio Bucchieri, Davide F. V. Corona, Giovanna Barbieri, Francesco Cappello, Everly Conway De Macario, Alberto J. L. Macario, Anna Maria Merendino

Risultato della ricerca: Article

56 Citazioni (Scopus)

Abstract

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.
Lingua originaleEnglish
Numero di pagine8
RivistaPLoS One
Volume7
Stato di pubblicazionePublished - 2012

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exosomes
protein transport
Protein Transport
Cell membranes
Exosomes
Tumors
plasma membrane
research planning
Cells
Cell Membrane
chaperonins
Golgi apparatus
traffic
Chaperonins
organelles
Neoplasms
Proteins
Oncology
Medical Oncology
Golgi Apparatus

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

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. / The odyssey of Hsp60 from tumor cells to other destinations includes plasma membrane-associated stages and Golgi and exosomal protein-trafficking modalities. In: PLoS One. 2012 ; Vol. 7.
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abstract = "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.",
author = "Giosalba Burgio and Fucarino, {Alberto Giuseppe} and Fabio Bucchieri and Giovanni Zummo and Felicia Farina and Sabrina David and Francesco Cappello and Davide Corona and Claudia Campanella and Claudia Campanella and Giosalba Burgio and Fabio Bucchieri and Corona, {Davide F. V.} and Giovanna Barbieri and Francesco Cappello and {Conway De Macario}, Everly and Macario, {Alberto J. L.} and Merendino, {Anna Maria}",
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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 -