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Eradication of Glioblastoma, and Breast and Colon Carcinoma Xenografts by Hsp70 Depletion1

Al Musella's Comments: (This is his personal views and are not necessarily the views of the Musella Foundation!)


Posted on: 12/28/2002

[Cancer Research 62, 7139-7142, December 15, 2002]
© 2002 American Association for Cancer Research
Advances in Brief

Eradication of Glioblastoma, and Breast and Colon Carcinoma Xenografts by Hsp70 Depletion1

Jesper Nylandsted, Wolfgang Wick, Ulrich A. Hirt, Karsten Brand, Mikkel Rohde, Marcel Leist, Michael Weller and Marja Jäättelä2

Apoptosis Laboratory, Institute for Cancer Biology, Danish Cancer Society, DK-2100 Copenhagen, Denmark [J. N., M. R., M. J.]; Laboratory of Molecular Neuro-Oncology, Department of Neurology, University of Tübingen, Medical School, D-72076 Tübingen, Germany [W. W., M. W.]; Faculty of Biology, University of Konstanz, D-78457 Konstanz, Germany [U. A. H.]; Max Delbrück Centre for Molecular Medicine, D-13122 Berlin-Buch, Germany [K. B.]; and H. Lundbeck A/S, DK-2500 Valby, Denmark [M. L.]

Heat shock protein 70 (Hsp70) is an antiapoptotic chaperone protein highly expressed in human tumors. Here we demonstrate that locoregional application of adenovirus expressing antisense Hsp70 cDNA (Ad.asHsp70) eradicates orthotopic xenografts of glioblastoma and breast carcinoma, as well as s.c. xenografts of colon carcinoma in immunodeficient mice. Ad.asHsp70-treated tumors showed massive apoptosis-like cell death and recruitment of macrophages. Human monocyte-derived macrophages effectively removed the corpses of Ad.asHsp70-treated tumor cells in vitro. Interestingly, both tumor cell death and phagocytosis were caspase-independent. Thus, Hsp70 appears as a promising target for the treatment of cancers resistant to classic caspase-mediated apoptosis.

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