The insertion of d-β-hydroxybutyrate apodehydrogenase into phospholipid monolayers and phospholipid vesicles

Berrez, Jean-Marc; Pattus, Franc; Latruffe, Norbert

doi:10.1016/0003-9861(85)90773-8

Cited by 10 publications

(6 citation statements)

References 33 publications

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“…Thus these variations in the surface charges according to the nature of phospholipid polar head composition can induce a conformational change in the D-,/-hydroxybutyrate dehydrogenase polypeptide chain. In agreement with these results, we have shown that hydrophilic interactions between phospholipid polar heads and D-,8-hydroxybutyrate dehydrogenase are essential for the penetration of the apoenzyme into phospholipid monolayers [5]. The highest D-,/-hydroxybutyrate dehydrogenase fluorescence intensity increase obtained in the presence of mitochondrial phospholipid confirms the crucial role of phosphatidylcholine in the correct insertion of this enzyme, its conformation and, consequently, its biological function.…”

Section: Discussionsupporting

confidence: 86%

“…mainly phosphatidylethanolamine and cardiolipin, together or each mixed with phosphatidylcholine, increased both the activity and the efficiency of re-activation [3]. Moreover, the negatively charged phospholipids, such as cardiolipins, appear to be involved in the enzyme insertion into phospholipid monolayers [5]. This phospholipid requirement makes D-/?-hydroxybutyrate dehydrogenase an interesting model for studying phospholipid-protein interactions.…”

Section: Introductionmentioning

confidence: 99%

“…n.m.r. [11], specific chemical modifications of essential amino acid residues [12,13], controlled proteolysis [14], apoenzyme insertion into phospholipid monolayers [5] and interactions of the apo-dehydrogenase with photoactivable phospholipids [15].…”

Section: Introductionmentioning

confidence: 99%

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Interactions between apo-(d-β-hydroxybutyrate dehydrogenase) and phospholipids studied by intrinsic and extrinsic fluorescence

Kebbaj¹,

Latruffe²,

Monsigny³

et al. 1986

Biochemical Journal

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Interactions of D-beta-hydroxybutyrate dehydrogenase with phospholipids were investigated by both intrinsic- and extrinsic-fluorescence approaches. The intrinsic fluorescence, mainly caused by tryptophan residues, increased upon re-activation in the presence of phospholipids bearing a positive charge, i.e. phosphatidylcholine, but decreased in the presence of non-re-activating phospholipids with a negative charge. This indicates either that the environment of tryptophan residues is affected by charges rather than by hydrophobic chains of phospholipids, or that the enzyme undergoes different conformational changes depending on the nature of the phospholipids. On the other hand, the graph of the temperature-dependence of the fluorescence intensities of the enzyme embedded in dimyristoylphosphatidylcholine liposomes exhibits a break around 21 degrees C. This indicates either that at least one tryptophan residue is closely in contact with the hydrophobic chains of phospholipids or that there is a change in the environment of tryptophan residues owing to the physical state of the phospholipids. The addition of D-beta-hydroxybutyrate apo-dehydrogenase to phospholipid liposomes containing diphenylhexatriene (a fluorescent probe) increased the diphenylhexatriene fluorescence polarization. Moreover, there was a partial fluorescence energy transfer from tryptophan to diphenylhexatriene. These results strongly favour the possibility that there is a portion of the enzyme polypeptide chain inserted into the phospholipid hydrophobic region. All these results demonstrate that D-beta-hydroxybutyrate apo-dehydrogenase interacts with both polar and hydrophobic parts of phospholipids and leads to small, but essential, conformational changes of the enzyme.

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Section: Discussionsupporting

confidence: 86%

Section: Introductionmentioning

confidence: 99%

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Interactions between apo-(d-β-hydroxybutyrate dehydrogenase) and phospholipids studied by intrinsic and extrinsic fluorescence

Kebbaj¹,

Latruffe²,

Monsigny³

et al. 1986

Biochemical Journal

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“…Although the apoenzyme interacts with every pure PL tested, it interacts most strongly with films containing CL. Berrez et al 33 propose that CL molecules on the inner face govern the binding to the inner membrane. The ~-hydroxybutyrate dehydrogenase is normally 'crypticized' and mostly inactive in intact mitochondria, and full expression of its activity in vitro requires membrane lysis.…”

Section: Substrate Dehydrogenasesmentioning

confidence: 99%

Lipids and thyroid hormones

Hoch

1988

Progress in Lipid Research

144

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“…Before compression, the components are spread on a water-containing subphase, using an organic solvent. In attempts to improve this model system, liposomes (1) or whole biomembranes (2)(3)(4)(5)(6) have been spread from aqueous solutions. This new approach is quite attractive but raises the question of how the films are organized at the gas-water interface.…”

Section: Introductionmentioning

confidence: 99%

Direct evidence for the formation of a monolayer from a bilayer. An ellipsometric study at the nitrogen-water interface

Salesse

Ducharme

Leblanc

1987

Biophysical Journal

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Direct evidence for the formation of a monolayer from a bilayer was measured by ellipsometry after spreading unilamellar vesicles of dioleoyl phosphatidylcholine (DOPC) at the nitrogen-water interface. The ellipsometric isotherms of DOPC vesicles and DOPC spread from an organic solvent were compared and found similar. From the observed ellipsometric angle (delta delta) in the plateau region (-1.04 degrees) and literature data for refractive indices of an anisotropic film similar to DOPC, we have calculated a thickness of 20 +/- 1 A. These results strongly suggest that, similarly to DOPC spread from an organic solvent, DOPC vesicles form a monolayer when spread at the nitrogen-water interface.

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The insertion of d-β-hydroxybutyrate apodehydrogenase into phospholipid monolayers and phospholipid vesicles

Cited by 10 publications

References 33 publications

Interactions between apo-(d-β-hydroxybutyrate dehydrogenase) and phospholipids studied by intrinsic and extrinsic fluorescence

Interactions between apo-(d-β-hydroxybutyrate dehydrogenase) and phospholipids studied by intrinsic and extrinsic fluorescence

Lipids and thyroid hormones

Direct evidence for the formation of a monolayer from a bilayer. An ellipsometric study at the nitrogen-water interface

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