Lipid-protein interactions in biomembranes studied through the phospholipid specificity of d-β-hydroxybutyrate dehydrogenase

Latruffe, Norbert; Berrez, Jean-Marc; Kebbaj, M'Hammed Saïd El

doi:10.1016/s0300-9084(86)80015-3

Cited by 19 publications

(8 citation statements)

References 69 publications

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“…Lateral and vertical heterogeneity within a given membrane with respect to lipid composition, protein distribution, and physicochemical state contribute to the existence of membrane domains with different characteristics (Melchior, 1986;Treistman et al, 1987). Furthermore, specific interactions between membrane proteins and certain membrane lipids (Latruffe et al, 1986;Marsh, 1987) define a specific lipid boundary layer around functional membrane proteins such as the nicotinic acetylcholine receptor (Jones et al, 1988). Attempts to reconstitute ligand binding to the partially purified p- (Hasegawa et al, 1987) and 6- (Scheideler and Zukin, 1990) opioid receptors have indicated requirements for specific phospholipids.…”

Section: Discussionmentioning

confidence: 99%

Altered Microviscosity at Brain Membrane Surface Induces Distinct and Reversible Inhibition of Opioid Receptor Binding

Lazar

Medzihradsky

1992

Journal of Neurochemistry

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In synaptosomal membranes from rat and monkey brain cortex, the addition of petroselenic (18:1, cis-delta 6) acid, oleic (18:1, cis-delta 9) acid, and vaccenic (18:1, cis-delta 11) acid or their corresponding methyl esters at 0.5 mumol/mg of membrane protein caused a similar 7-10% decrease in the microviscosity of the membrane core, whereas at the membrane surface the microviscosity was reduced 5-7% by the fatty acids but only 1% by their methyl esters. Concomitantly, the fatty acids, but not the methyl esters, inhibited the specific binding of the tritiated mu-, delta-, and kappa-opioids Tyr-D-Ala-Gly-(Me)Phe-Gly-ol (DAMGO), [D-Pen2,D-Pen5]enkephalin (DPDPE), and U69,593, respectively. As shown with oleic acid, the sensitivity of opioid receptor binding toward inhibition by fatty acids was in the order delta greater than mu much greater than kappa, whereby the binding of [3H]DPDPE was abolished, but significant inhibition of [3H]U69,593 binding, determined in membranes from monkey brain, required membrane modification with a twofold higher fatty acid concentration. Except for the unchanged KD of [3H]U69,593, the inhibition by oleic acid involved both the Bmax and affinity of opioid binding. Cholesteryl hemisuccinate (0.5-3 mumol/mg of protein), added to membranes previously modified by fatty acids, reversed the fluidization caused by the latter compounds and restored inhibited mu-, delta-, and kappa-opioid binding toward control values. In particular, the Bmax of [3H]-DPDPE binding completely recovered after being undetectable.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionmentioning

confidence: 99%

Altered Microviscosity at Brain Membrane Surface Induces Distinct and Reversible Inhibition of Opioid Receptor Binding

Lazar

Medzihradsky

1992

Journal of Neurochemistry

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“…(R)-3-Hydroxybutyrate dehydrogenase (EC 1.1. 1.30) (BDH) has a specific requirement for phosphatidylcholine (PC) for enzymic activity [1] and is one of the best-studied examples of a lipidrequiring enzyme [2][3][4][5]. BDH was first highly purified from bovine heart mitochondria by Bock and Fleischer [6].…”

Section: Introductionmentioning

confidence: 99%

Effect of selective thiol-group derivatization on enzyme kinetics of (R)-3-hydroxybutyrate dehydrogenase

Dalton

McIntyre

Fleischer

1993

Biochemical Journal

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(R)-3-Hydroxybutyrate dehydrogenase (BDH) is a phosphatidylcholine-requiring tetrameric enzyme with two thiol groups (SH-1 and SH-2) per protomer. By first protecting the more rapidly reacting thiol group (SH-1) with diamide [1,1'-azobis-(NN'-dimethylformamide), DM] to form DM(SH-1)BDH, SH-2 can be selectively derivatized by reaction with maleimide reagents such as 4-maleimido-2,2,6,6-tetramethyl-piperidine-N-oxyl (MSL), which gives DM(SH-1)MSL(SH-2)BDH. Reduction with dithiothreitol (DTT) regenerates SH-1, yielding MAL(SH-2)BDH (where MAL is the diamagnetic reduction product of MSL-BDH and DTT). The enzymic activity of DM(SH-1)BDH is decreased to approx. 4% relative to the native purified enzyme, and the apparent Km for substrate, KmBOH, is increased approx. 100-fold. Reduction of DM(SH-1)BDH with DTT regenerates SH-1 and restores normal enzymic function. Modification of SH-2 with piperidinylmaleimide [MAL(SH-2)BDH] diminishes enzymic activity to approx. 35% of its original value, but has no significant effect on apparent KmBOH. The doubly derivatized enzyme, DM(SH-1)MSL(SH-2)BDH, has lower enzymic activity [about half that for DM(SH-2)BDH] and a yet higher apparent KmBOH than DM(SH-1)BDH. Derivatization of SH-2 with different maleimide reagents results in diminished activity approximately proportional to the size of the maleimide substituent, suggesting that this inhibition is steric. Whereas modification of SH-1 results in marked changes in kinetic parameters (increased apparent Km and reduced apparent Vmax), derivatization of SH-2 has a lesser effect on enzymic function. Thus SH-1 is postulated to be closer to the active centre than is SH-2, although neither is involved in catalysis, since: (1) the activity of the derivatized enzyme is not abolished; and (2) activity can be enhanced by increasing substrate (and cofactor) concentrations.

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“…Figure 7 and table I (part F) show that a hyperlipidic diet (essentially after a 15-day period) gives an increase of BDH mRNA level in fiver as well as an increase of immunodetected BDH and BDH activity. The high increase of fiver BDH mRNA level means that the positive effect of lipid diet is not due to a BDH regulation by changes in membrane phospholipid composition as we could expect since BDH is a membrane lipid requiring enzyme [3] modulated by phospholipid fatty acid composition. Furthermore, in 1983 Mc Murchie et al [30] reported an increase of unsaturated fatty acid content in fiver mitochondrial membrane under hyper-lipidic diet.…”

Section: Influence Of Estradiolmentioning

confidence: 83%

“…It is synthesized in the cytosol as a larger precursor followed by a specific insertion-maturation in the inner membrane [2]. We previously showed that BDH is a lecithin-requiring enzyme [3] which is known to play an essential role in energy metabolism as a ketone bodiesconverting enzyme [4]. Unfortunately until now, only limited information was available concerning the gene regulation of this enzyme since studies were done mostly at the enzyme activity level [5][6][7], except in the last few years when works were undertaken at the post-translational level using a monospecific BDH antibody [g, 9].…”

Section: Introductionmentioning

confidence: 99%

Post‐transcriptional analysis of rat mitochondrial D‐3‐hydroxybutyrate dehydrogenase control through development and physiological stages^*

Bailly

Lone

Latruffe

1991

Biology of the Cell

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The nuclear encoded mitochondrial D-3-hydroxybutyrate dehydrogenase (BDH) is synthesized in the cytosal as a larger precursor. This membrane enzyme which requires lecithin for activity plays an essential role in energy metabolism as a ketone bodies-converting enzyme. A cDNA clone of the rat liver enzyme encompassing an antigenic determinant peptide has been isolated after immunoscreening of a lambda gt11 expression library. The nucleotide sequence of this 279-base cDNA insert contains a single open reading frame of 93 amino-acids, which represents about a third of the mature enzyme. Amino-acid sequence analysis predicts a hydrophobic stretch of 29 amino-acids long which probably functions as membrane anchor domain, or as an important region for the enzyme activation by phospholipid. By using this cDNA probe the BDH gene has been investigated at the mRNA level. There is only one mRNA (2-kb size) for BDH whatever the studied tissue. The rat gene is differently expressed since its mRNA is already present in the foetus liver while the BDH polypeptide amount is low and its enzymatic activity is not detectable even in the late stage of foetal development. The mRNA content is higher in the liver than in extrahepatic tissues. Adrenalectomy and ovariectomy increase liver mRNA content and polypeptide level, as well as activity of BDH. These effects are totally or partially abolished by corticosterone and estradiol treatments respectively. In addition, a 15-day hyperlipidic diet stimulates BDH gene expression. Present results show that the gene expression of this mitochondrial enzyme is modulated through development and hormonal and metabolic conditions mentioned above.

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Lipid-protein interactions in biomembranes studied through the phospholipid specificity of d-β-hydroxybutyrate dehydrogenase

Cited by 19 publications

References 69 publications

Altered Microviscosity at Brain Membrane Surface Induces Distinct and Reversible Inhibition of Opioid Receptor Binding

Altered Microviscosity at Brain Membrane Surface Induces Distinct and Reversible Inhibition of Opioid Receptor Binding

Effect of selective thiol-group derivatization on enzyme kinetics of (R)-3-hydroxybutyrate dehydrogenase

Post‐transcriptional analysis of rat mitochondrial D‐3‐hydroxybutyrate dehydrogenase control through development and physiological stages^*

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Lipid-protein interactions in biomembranes studied through the phospholipid specificity of d-β-hydroxybutyrate dehydrogenase

Cited by 19 publications

References 69 publications

Altered Microviscosity at Brain Membrane Surface Induces Distinct and Reversible Inhibition of Opioid Receptor Binding

Altered Microviscosity at Brain Membrane Surface Induces Distinct and Reversible Inhibition of Opioid Receptor Binding

Effect of selective thiol-group derivatization on enzyme kinetics of (R)-3-hydroxybutyrate dehydrogenase

Post‐transcriptional analysis of rat mitochondrial D‐3‐hydroxybutyrate dehydrogenase control through development and physiological stages*

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Post‐transcriptional analysis of rat mitochondrial D‐3‐hydroxybutyrate dehydrogenase control through development and physiological stages^*