NDLI: Calpeptin, not calpain, directly inhibits an ion channel of the inner mitochondrial membrane

Content Provider	Springer Nature Link
Author	Derksen, Maria Vorwerk, Christian Siemen, Detlef
Copyright Year	2015
Abstract	The permeability transition pore (PTP) of inner mitochondrial membranes is a large conductance pathway for ions up to 1500 Da which opening is responsible for ion equilibration and loss of membrane potential in apoptosis and thus in several neurodegenerative diseases. The PTP can be regulated by the Ca2+-activated mitochondrial K channel (BK). Calpains are Ca2+-activated cystein proteases; calpeptin is an inhibitor of calpains. We wondered whether calpain or calpeptin can modulate activity of PTP or BK. Patch clamp experiments were performed on mitoplasts of rat liver (PTP) and of an astrocytoma cell line (BK). Channel-independent open probability (P o) was determined (PTP) and, taking into account the number of open levels, NPo by single channel analysis (BK). We find that PTP in the presence of Ca2+ (200 μM) is uninfluenced by calpain (13 nM) and shows insignificant decrease by the calpain inhibitor calpeptin (1 μM). The NPo of the BK is insensitive to calpain (54 nM), too. However, it is significantly and reversibly inhibited by the calpain inhibitor calpeptin (IC50 = 42 μM). The results agree with calpeptin-induced activation of the PTP via inhibition of the BK. Screening experiments with respirometry show calpeptin effects, fitting to inhibition of the BK by calpeptin, and strong inhibition of state 3 respiration.
Starting Page	835
Ending Page	843
Page Count	9
File Format	PDF
ISSN	0033183X
Journal	Protoplasma
Volume Number	253
Issue Number	3
e-ISSN	16156102
Language	English
Publisher	Springer Vienna
Publisher Date	2015-06-25
Publisher Place	Vienna
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Calpain Calpeptin Calpain inhibitor Mitochondria Patch clamp BK channel Permeability transition pore Cell Biology Plant Sciences Zoology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science Medicine

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