Hsp60 is actively secreted by human tumor cells

Giovanni Zummo, Fabio Bucchieri, Claudia Campanella, Giosalba Burgio, Davide Corona, Francesco Cappello, Sabrina David, Giosalba Burgio, Everly Conway De Macario, Davide F. V. Corona, Francesco Cappello, Alberto J. L. Macario, Anna Ribbene, Anna Maria Merendino, Vito Marciano'

Risultato della ricerca: Article

107 Citazioni (Scopus)

Abstract

BACKGROUND:Hsp60, a Group I mitochondrial chaperonin, is classically considered an intracellular chaperone with residence in the mitochondria; nonetheless, in the last few years it has been found extracellularly as well as in the cell membrane. Important questions remain pertaining to extracellular Hsp60 such as how generalized is its occurrence outside cells, what are its extracellular functions and the translocation mechanisms that transport the chaperone outside of the cell. These questions are particularly relevant for cancer biology since it is believed that extracellular chaperones, like Hsp70, may play an active role in tumor growth and dissemination.METHODOLOGY/PRINCIPAL FINDINGS:Since cancer cells may undergo necrosis and apoptosis, it could be possible that extracellular Hsps are chiefly the result of cell destruction but not the product of an active, physiological process. In this work, we studied three tumor cells lines and found that they all release Hsp60 into the culture media by an active mechanism independently of cell death. Biochemical analyses of one of the cell lines revealed that Hsp60 secretion was significantly reduced, by inhibitors of exosomes and lipid rafts.CONCLUSIONS/SIGNIFICANCE:Our data suggest that Hsp60 release is the result of an active secretion mechanism and, since extracellular release of the chaperone was demonstrated in all tumor cell lines investigated, our observations most likely reflect a general physiological phenomenon, occurring in many tumors.
Lingua originaleEnglish
Numero di pagine7
RivistaPLoS One
Volume5(2)
Stato di pubblicazionePublished - 2010

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Tumors
Cells
cell lines
Physiological Phenomena
neoplasms
Tumor Cell Line
secretion
exosomes
Group I Chaperonins
chaperonins
Neoplasms
cells
Chaperonins
Exosomes
Mitochondria
cell membranes
cell death
necrosis
mitochondria
Cell death

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

Cita questo

Hsp60 is actively secreted by human tumor cells. / Zummo, Giovanni; Bucchieri, Fabio; Campanella, Claudia; Burgio, Giosalba; Corona, Davide; Cappello, Francesco; David, Sabrina; Burgio, Giosalba; De Macario, Everly Conway; Corona, Davide F. V.; Cappello, Francesco; Macario, Alberto J. L.; Ribbene, Anna; Merendino, Anna Maria; Marciano', Vito.

In: PLoS One, Vol. 5(2), 2010.

Risultato della ricerca: Article

Zummo, G, Bucchieri, F, Campanella, C, Burgio, G, Corona, D, Cappello, F, David, S, Burgio, G, De Macario, EC, Corona, DFV, Cappello, F, Macario, AJL, Ribbene, A, Merendino, AM & Marciano', V 2010, 'Hsp60 is actively secreted by human tumor cells', PLoS One, vol. 5(2).
Zummo, Giovanni ; Bucchieri, Fabio ; Campanella, Claudia ; Burgio, Giosalba ; Corona, Davide ; Cappello, Francesco ; David, Sabrina ; Burgio, Giosalba ; De Macario, Everly Conway ; Corona, Davide F. V. ; Cappello, Francesco ; Macario, Alberto J. L. ; Ribbene, Anna ; Merendino, Anna Maria ; Marciano', Vito. / Hsp60 is actively secreted by human tumor cells. In: PLoS One. 2010 ; Vol. 5(2).
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title = "Hsp60 is actively secreted by human tumor cells",
abstract = "BACKGROUND:Hsp60, a Group I mitochondrial chaperonin, is classically considered an intracellular chaperone with residence in the mitochondria; nonetheless, in the last few years it has been found extracellularly as well as in the cell membrane. Important questions remain pertaining to extracellular Hsp60 such as how generalized is its occurrence outside cells, what are its extracellular functions and the translocation mechanisms that transport the chaperone outside of the cell. These questions are particularly relevant for cancer biology since it is believed that extracellular chaperones, like Hsp70, may play an active role in tumor growth and dissemination.METHODOLOGY/PRINCIPAL FINDINGS:Since cancer cells may undergo necrosis and apoptosis, it could be possible that extracellular Hsps are chiefly the result of cell destruction but not the product of an active, physiological process. In this work, we studied three tumor cells lines and found that they all release Hsp60 into the culture media by an active mechanism independently of cell death. Biochemical analyses of one of the cell lines revealed that Hsp60 secretion was significantly reduced, by inhibitors of exosomes and lipid rafts.CONCLUSIONS/SIGNIFICANCE:Our data suggest that Hsp60 release is the result of an active secretion mechanism and, since extracellular release of the chaperone was demonstrated in all tumor cell lines investigated, our observations most likely reflect a general physiological phenomenon, occurring in many tumors.",
author = "Giovanni Zummo and Fabio Bucchieri and Claudia Campanella and Giosalba Burgio and Davide Corona and Francesco Cappello and Sabrina David and Giosalba Burgio and {De Macario}, {Everly Conway} and Corona, {Davide F. V.} and Francesco Cappello and Macario, {Alberto J. L.} and Anna Ribbene and Merendino, {Anna Maria} and Vito Marciano'",
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TY - JOUR

T1 - Hsp60 is actively secreted by human tumor cells

AU - Zummo, Giovanni

AU - Bucchieri, Fabio

AU - Campanella, Claudia

AU - Burgio, Giosalba

AU - Corona, Davide

AU - Cappello, Francesco

AU - David, Sabrina

AU - Burgio, Giosalba

AU - De Macario, Everly Conway

AU - Corona, Davide F. V.

AU - Cappello, Francesco

AU - Macario, Alberto J. L.

AU - Ribbene, Anna

AU - Merendino, Anna Maria

AU - Marciano', Vito

PY - 2010

Y1 - 2010

N2 - BACKGROUND:Hsp60, a Group I mitochondrial chaperonin, is classically considered an intracellular chaperone with residence in the mitochondria; nonetheless, in the last few years it has been found extracellularly as well as in the cell membrane. Important questions remain pertaining to extracellular Hsp60 such as how generalized is its occurrence outside cells, what are its extracellular functions and the translocation mechanisms that transport the chaperone outside of the cell. These questions are particularly relevant for cancer biology since it is believed that extracellular chaperones, like Hsp70, may play an active role in tumor growth and dissemination.METHODOLOGY/PRINCIPAL FINDINGS:Since cancer cells may undergo necrosis and apoptosis, it could be possible that extracellular Hsps are chiefly the result of cell destruction but not the product of an active, physiological process. In this work, we studied three tumor cells lines and found that they all release Hsp60 into the culture media by an active mechanism independently of cell death. Biochemical analyses of one of the cell lines revealed that Hsp60 secretion was significantly reduced, by inhibitors of exosomes and lipid rafts.CONCLUSIONS/SIGNIFICANCE:Our data suggest that Hsp60 release is the result of an active secretion mechanism and, since extracellular release of the chaperone was demonstrated in all tumor cell lines investigated, our observations most likely reflect a general physiological phenomenon, occurring in many tumors.

AB - BACKGROUND:Hsp60, a Group I mitochondrial chaperonin, is classically considered an intracellular chaperone with residence in the mitochondria; nonetheless, in the last few years it has been found extracellularly as well as in the cell membrane. Important questions remain pertaining to extracellular Hsp60 such as how generalized is its occurrence outside cells, what are its extracellular functions and the translocation mechanisms that transport the chaperone outside of the cell. These questions are particularly relevant for cancer biology since it is believed that extracellular chaperones, like Hsp70, may play an active role in tumor growth and dissemination.METHODOLOGY/PRINCIPAL FINDINGS:Since cancer cells may undergo necrosis and apoptosis, it could be possible that extracellular Hsps are chiefly the result of cell destruction but not the product of an active, physiological process. In this work, we studied three tumor cells lines and found that they all release Hsp60 into the culture media by an active mechanism independently of cell death. Biochemical analyses of one of the cell lines revealed that Hsp60 secretion was significantly reduced, by inhibitors of exosomes and lipid rafts.CONCLUSIONS/SIGNIFICANCE:Our data suggest that Hsp60 release is the result of an active secretion mechanism and, since extracellular release of the chaperone was demonstrated in all tumor cell lines investigated, our observations most likely reflect a general physiological phenomenon, occurring in many tumors.

UR - http://hdl.handle.net/10447/54468

M3 - Article

VL - 5(2)

JO - PLoS One

JF - PLoS One

SN - 1932-6203

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