http://www.cnr.it/ontology/cnr/individuo/prodotto/ID196382
The Odyssey of Hsp60 from Tumor Cells to Other Destinations Includes Plasma Membrane-Associated Stages and Golgi and Exosomal Protein-Trafficking Modalities (Articolo in rivista)
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- Label
- The Odyssey of Hsp60 from Tumor Cells to Other Destinations Includes Plasma Membrane-Associated Stages and Golgi and Exosomal Protein-Trafficking Modalities (Articolo in rivista) (literal)
- Anno
- 2012-01-01T00:00:00+01:00 (literal)
- Alternative label
Claudia Campanella, Fabio Bucchieri, Anna M. Merendino, Alberto Fucarino, Giosalba Burgio, Davide F. V. Corona, Giovanna Barbieri, Sabrina David, Felicia Farina, Giovanni Zummo, Everly Conway de Macario, Alberto J. L. Macario, Francesco Cappello. (2012)
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
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Claudia Campanella, Fabio Bucchieri, Anna M. Merendino, Alberto Fucarino, Giosalba Burgio, Davide F. V. Corona, Giovanna Barbieri, Sabrina David, Felicia Farina, Giovanni Zummo, Everly Conway de Macario, Alberto J. L. Macario, Francesco Cappello. (literal)
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- Rivista
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- Dipartimento BIONEC, Sezione di Anatomia Umana, University of Palermo, Palermo, Italy;
Istituto Euro-Mediterraneo di Scienza e Tecnologia, Palermo, Italy;
Dipartimento STEMBIO, University of Palermo, Palermo, Italy:
Dulbecco Telethon Institute, Palermo, Italy;
Istituto di Biomedicina e Immunologia Molecolare, C.N.R., Palermo, Italy;
Department of Microbiology and Immunology, School of Medicine, University of Maryland at Baltimore, and IMET, Baltimore, Maryland, United States of
America (literal)
- Titolo
- The Odyssey of Hsp60 from Tumor Cells to Other Destinations Includes Plasma Membrane-Associated Stages and Golgi and Exosomal Protein-Trafficking Modalities (literal)
- 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. (literal)
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