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Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition
Open accessAbstract
A fusion protein between cyclophilin-D (CyP-D) and glutathione S-transferase (GST) was shown to bind to purified liver inner mitochondrial membranes (IMMs) in a cyclosporin A (CsA)-sensitive manner. Binding was enhanced by diamide treatment of the IMMs. Immobilized GST–CyP-D avidly bound a single 30 kDa protein present in Triton X-100-solubilized IMMs; immunoblotting showed this to be the adenine nucleotide translocase (ANT). Binding was prevented by pretreatment of the CyP-D with CsA, but not with cyclosporin H. Purified ANT also bound specifically to GST–CyP-D, but porin did not, even in the presence of ANT.
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Retracted
Metadata
- Authors
- WOODFIELD, K., RÜCK, A., BRDICZKA, D., & HALESTRAP, A. P.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1998-12-01
- Volume
- 336
- Issue
- 2
- Pages
- 287-290
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1909302202
- Cited by
- 386
- References
- 1
- FWCI
- 4.95
- Type
- journal article
- Language
- en
- Open access
- bronze
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