The odyssey of Hsp60 from tumor cells to other destinations includes plasma membrane-associated stages and Golgi and exosomal protein-trafficking modalities.
The odyssey of Hsp60 from tumor cells to other destinations includes plasma membrane-associated stages and Golgi and exosomal protein-trafficking modalities.
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DOI:
10.1371/journal.pone.0042008
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发表时间:
2012
期刊:
影响因子:
3.7
通讯作者:
Cappello F
中科院分区:
文献类型:
--
作者:
Campanella C;Bucchieri F;Merendino AM;Fucarino A;Burgio G;Corona DF;Barbieri G;David S;Farina F;Zummo G;de Macario EC;Macario AJ;Cappello F
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. 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. 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.
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DOI:
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发表时间:
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期刊:
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影响因子:
--
作者:
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通讯作者:
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影响因子:
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影响因子:
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DOI:
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发表时间:
2007-01-01
期刊:
STRESS RESPONSES IN BIOLOGY AND MEDICINE
影响因子:
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作者:
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通讯作者:
De Macario, Everly Conway
影响因子:
20.3
作者:
de Gassart, A;Géminard, C;Vidal, M
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