Further aspects of the Ca2+-dependent polymorphism of bovine heart cardiolipin

Kruijff, Ben de; Verkleij, Arie J.; Leunissen‐Bijvelt, J.; Echteld, C.J.A. van; Hille, J. D. R.; Rijnbout, H.

doi:10.1016/0005-2736(82)90464-3

Cited by 98 publications

(68 citation statements)

References 43 publications

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“…The VDAC gating obtained in the multichannel membranes made of PE, a nonlamellar lipid with high negative spontaneous curvature and high packing stress, is more asymmetric in voltage than in the membranes formed from PC, a lamellar lipid with relaxed bilayer structure. We also demonstrate that CL, which induces negative curvature (47,48), promotes similar voltage-gating asymmetry. As an internal control of the membrane mechanical properties, we use gramicidin A channels, whose association-dissociation kinetics is known to depend on several bilayer parameters, such as thickness, compression-expansion modulus, bending rigidity, interfacial tension (39), and dipole potential (49), but also on the lipid packing stress.…”

supporting

confidence: 55%

“…Previously, it was demonstrated that 6 -8 mM Ca 2ϩ induced mild leakage in liposomes made of the membranes with high CL content, namely CL/DOPC in a 1:2 molar ratio (7). In the 1-3 mM concentration range, Ca 2ϩ induces a hexagonal phase in aqueous dispersion of sodium salt of bovine cardiolipin due to the 1:1 binding of Ca 2ϩ to the negatively charged CL molecule (47,48). In order to test the possible effect of Ca 2ϩ on PC/CL membranes, we performed experiments with gramicidin channels in PC/CL (4 mol %) in the presence of 1 mM CaCl 2 .…”

Section: Resultsmentioning

confidence: 99%

“…An ability of CL to induce formation of CL-enriched clusters was shown with submitochondrial particles (inverted liposomes from the mitochondrial inner membrane) in the presence of millimolar concentrations of Ca 2ϩ (89). In a model system of a 1:1 mixture of lamellar DOPC with CL in the presence of Ca 2ϩ , the formation of a new nonbilayer lipid structure, the "lipid particle," was reported (47). The lipid microdomains in mitochondria and their contribution to apoptosis-associated modification of mitochondria were recently described for T cells (90).…”

Section: Discussionmentioning

confidence: 98%

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Voltage Gating of VDAC Is Regulated by Nonlamellar Lipids of Mitochondrial Membranes

Rostovtseva

Kazemi

Weinrich

et al. 2006

Journal of Biological Chemistry

117

178

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Evidence is accumulating that lipids play important roles in permeabilization of the mitochondria outer membrane (MOM) at the early stage of apoptosis. Lamellar phosphatidylcholine (PC) and nonlamellar phosphatidylethanolamine (PE) lipids are the major membrane components of the MOM. Cardiolipin (CL), the characteristic lipid from the mitochondrial inner membrane, is another nonlamellar lipid recently shown to play a role in MOM permeabilization. We investigate the effect of these three key lipids on the gating properties of the voltage-dependent anion channel (VDAC), the major channel in MOM. We find that PE induces voltage asymmetry in VDAC currentvoltage characteristics by promoting channel closure at cis negative applied potentials. Significant asymmetry is also induced by CL. The observed differences in VDAC behavior in PC and PE membranes cannot be explained by differences in the insertion orientation of VDAC in these membranes. Rather, it is clear that the two nonlamellar lipids affect VDAC gating. Using gramicidin A channels as a tool to probe bilayer mechanics, we show that VDAC channels are much more sensitive to the presence of CL than could be expected from the experiments with gramicidin channels. We suggest that this is due to the preferential insertion of VDAC into CL-rich domains. We propose that the specific lipid composition of the mitochondria outer membrane and/or of contact sites might influence MOM permeability by regulating VDAC gating.

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supporting

confidence: 55%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 98%

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Voltage Gating of VDAC Is Regulated by Nonlamellar Lipids of Mitochondrial Membranes

Rostovtseva

Kazemi

Weinrich

et al. 2006

Journal of Biological Chemistry

117

178

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“…It is worth noting that the observed chemical shift anisotropy is considerably smaller than the 21 ppm chemical shift anisotropy of the calcium induced H n phase of cardiolipin (Ref. 52 or Fig. 2f).…”

Section: ~P_nmrmentioning

confidence: 72%

Melittin induces HII phase formation in cardiolipin model membranes

Batenburg

Hibbeln

Verkleij

et al. 1987

Biochimica et Biophysica Acta (BBA) - Biomembranes

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The interaction of melittin with bovine heart cardiolipin model membranes was investigated via binding assays, 3t P-NMR, freeze-fracture electron microscopy, small angle X-ray diffraction and fluorescence based fusion assays. A strong binding (K d < 10-7 M) appeared to be accompanied by the formation of large structures, resulting from a fusion process of extremely fast initial rate. As the melittin content is increased, bilayer structure is gradually lost and from a cardiolipin to melittin ratio of about 6 the lipid starts to organize itself in an hexagonal H ii phase. At lower temperatures (T < 40 ° C) the coexistence of another structure is observed, characterized by a broad isotropic 31p-NMR signal and giving rise to sharp X-ray reflections, most probably a cubic phase, as suggested also by freeze-fracture images, showing orderly stacked particles. The results are discussed in relation to contrasting observations on the structural changes induced by melittin in the zwitterionic phospholipid system of dipalmitoylphosphatidylcholine (Dufourcq, J. et al. (1986) Biochim. Biophys. Acta 859, 33-48). The biological relevance of the observations with respect to the process of protein insertion into membranes is indicated.

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“…3C, D) [2,23,37]. It is of importance to note that 31p-NMR measurements 51 in this case detect an isotropic signal during the transition, which may reflect the presence of lipidic particles [23,37].…”

Section: Lib Hi1 Phase-lamellar Transitions M Single Lipid Systemsmentioning

confidence: 84%