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Molecular and Cellular Biology, March 2002, p. 1926-1935, Vol. 22, No. 6
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.6.1926-1935.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

BMAP-28, an Antibiotic Peptide of Innate Immunity, Induces Cell Death through Opening of the Mitochondrial Permeability Transition Pore

Department of Biotechnology and Biomedical Sciences,¹ Department of Biology and Agro-Industrial Economics, University of Udine, I-33100 Udine,² C.N.R. Center for the Study of Biomembranes at the Department of Biomedical Sciences, University of Padua, I-35121 Padua,³ Department of Biochemistry, Biophysics, and Chemistry of Macromolecules, University of Trieste, Trieste, Italy⁴

Received 22 May 2001/ Returned for modification 27 July 2001/ Accepted 13 November 2001

BMAP-28, a bovine antimicrobial peptide of the cathelicidin family, induces membrane permeabilization and death in human tumor cell lines and in activated, but not resting, human lymphocytes. In addition, we found that BMAP-28 causes depolarization of the inner mitochondrial membrane in single cells and in isolated mitochondria. The effect of the peptide was synergistic with that of Ca²⁺ and inhibited by cyclosporine, suggesting that depolarization depends on opening of the mitochondrial permeability transition pore. The occurrence of a permeability transition was investigated on the basis of mitochondrial permeabilization to calcein and cytochrome c release. We show that BMAP-28 permeabilizes mitochondria to entrapped calcein in a cyclosporine-sensitive manner and that it releases cytochrome c in situ. Our results demonstrate that BMAP-28 is an inducer of the mitochondrial permeability transition pore and that its cytotoxic potential depends on its effects on mitochondrial permeability.

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