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

Francesco Cappello, Felicia Farina, Alberto Giuseppe Fucarino, Sabrina David, Fabio Bucchieri, Giosalba Burgio, Giovanni Zummo, Claudia Campanella, Davide Corona, 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: Articlepeer review

75 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

All Science Journal Classification (ASJC) codes

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  • ???subjectarea.asjc.1100.1100???
  • General

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