The influence of phosphatidate bilayers on pig heart AMP deaminase. Crucial role of pH-dependent lipid-phase transition

Woźniak, Michał; Kossowska, E; Purzycka-Preis, J; Zydowo, M

doi:10.1042/bj2550977

Cited by 9 publications

(10 citation statements)

References 24 publications

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“…The interaction was observed with egg‐PC but not with DPPC membranes, and it caused an increase in the enzymatic activity. AMP‐deaminase interacted also with DOPA membranes,32 which are in a fluid state at room temperature and exerted a noncompetitive inhibition 33. This effect was observed also with other phosphatidate species containing saturated fatty acids, but only when the bilayer was in a fluid state 33…”

Section: Discussionmentioning

confidence: 87%

Effect of acidic phospholipids on the structural properties of recombinant cytosolic human glyoxalase II

et al. 2002

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A peculiar characteristic of highly concentrated cytosolic recombinant human glyoxalase II (GII) solutions is to undergo partial precipitation. Previous work indicated that anionic phospholipids (PLs) exert a noncompetitive inhibition on the enzymatic activity of the soluble enzyme. In this study, FTIR spectroscopy was used to analyze the structural properties and the thermal stability of the soluble protein in the absence and in the presence of liposomes made of different phospholipids (PLs). The structural analysis was performed on the precipitate as well. The interaction of acidic PLs with GII lowered the thermal stability of the enzyme and inhibited protein intermolecular interactions (aggregation) brought about by thermal denaturation. Infrared data indicated that ionic and hydrophobic interactions occur between GII and acidic PLs causing small changes in the secondary structure of the enzyme. No interactions of the protein with egg phosphatidylcholine liposomes were detected. The results are consistent with the destabilization of the protein tertiary structure, and indicate that GII possesses hydrophobic part(s) that interact with the acyl chains of PLs. Data on precipitated GII did not show remarkable modification of secondary structure, suggesting that hydrophobic stretches of the enzyme may also be involved in the protein-protein association (precipitation) at high GII concentration. The alterations in the GII structure and the noncompetitive inhibition exerted by acidic PLs are strictly related.

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Section: Discussionmentioning

confidence: 87%

Effect of acidic phospholipids on the structural properties of recombinant cytosolic human glyoxalase II

et al. 2002

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“…Phosphatidate species containing saturated fatty acids were either non-inhibitory or inhibited enzyme activity rather poorly [8]. Nevertheless, fluidization of the saturated phosphatidate species by alkalinization of the medium resulted in the appearance of an inhibitory effect of dilauroyl phosphatidate bilayers on pig heart AMP deaminase [8]. An activitory effect of PC bilayers on pig heart AMP deaminase described previously [7] involved natural egg yolk PC.…”

Section: Introductionmentioning

confidence: 84%

“…Phosphatidylcholine (PC)-containing liposomes were found to activate this enzyme in the presence of ATP [7]. On the other hand, phosphatidate bilayers composed of dioleoyl phosphatidate were found to exert non-competitive inhibition on the AMP deaminase with a K, of 15 ,uM, three orders of magnitude lower than that for orthophosphate, a well-known negative allosteric effector of AMP deaminase [8]. Another interesting finding was the established dependence of the inhibition by phosphatidate 'effectors' on membrane fluidity.…”

Section: Introductionmentioning

confidence: 99%

“…Another interesting finding was the established dependence of the inhibition by phosphatidate 'effectors' on membrane fluidity. Phosphatidate species containing saturated fatty acids were either non-inhibitory or inhibited enzyme activity rather poorly [8]. Nevertheless, fluidization of the saturated phosphatidate species by alkalinization of the medium resulted in the appearance of an inhibitory effect of dilauroyl phosphatidate bilayers on pig heart AMP deaminase [8].…”

Section: Introductionmentioning

confidence: 99%

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The interaction of phospholipid bilayers with pig heart AMP deaminase: Fourier-transform infrared spectroscopic and kinetic studies

Tanfani

Kossowska

Purzycka-Preis

et al. 1993

Biochemical Journal

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The interaction of pig heart AMP deaminase with different chemical species of phosphatidylcholine and with natural plasma membranes has been investigated. Phospholipids added to the system either as natural biological membranes (plasma membrane vesicles) or in the form of liposomes containing unsaturated phosphatidylcholine considerably enhanced AMP deaminase activity. The secondary structure of pig heart AMP deaminase in the absence and in the presence of dioleoyl phosphatidylcholine and dipalmitoyl phosphatidylcholine liposomes was investigated by Fourier-transform infrared spectroscopy. Quantitative analysis of the amide I band showed that the enzyme contains 45% beta-sheets, 28% alpha-helix, 16% turns and 11% non-ordered structure. In the presence of dioleoyl phosphatidylcholine liposomes, the beta/alpha content ratio decreased; this decrease was dependent on the amount of lipid added. This phenomenon was not observed in the case of dipalmitoyl phosphatidylcholine liposomes. These data suggest a possible role for membrane phospholipids in the regulation of AMP deaminase activity.

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“…It has also been shown that the first 48 amino acids of the N-terminus of isoform E, that is highly expressed in skeletal muscle type I fibers [ 41 ], dramatically suppress contractile protein binding capacity of this enzyme [ 69 ], a behavior that could facilitate other intracellular interactions. More recently, a series of studies has shown that interactions between purified pig heart AMPD, the porcine ortholog of human isoform E [ 72 ], and isolated cytoplasmic membrane vesicles and artificial lipid bilayers [ 73 , 74 , 75 ], alters secondary structure and regulatory behavior of the enzyme. The association of the N-terminal domain of AMPD3 with the cytoplasmic face of erythrocyte ghost membranes is accompanied by reduced catalytic activity of the enzyme [ 27 ].…”

Section: A Highly Differentiated N-terminal Region Of Ampd Is Prodmentioning

confidence: 99%

Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour of the Enzyme

Ronca

Raggi

2018

Biomolecules

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Multiple muscle-specific isoforms of the Zn2+ metalloenzyme AMP deaminase (AMPD) have been identified based on their biochemical and genetic differences. Our previous observations suggested that the metal binding protein histidine-proline-rich glycoprotein (HPRG) participates in the assembly and maintenance of skeletal muscle AMP deaminase (AMPD1) by acting as a zinc chaperone. The evidence of a role of millimolar-strength phosphate in stabilizing the AMPD-HPRG complex of both AMPD1 and cardiac AMP deaminase (AMPD3) is suggestive of a physiological mutual dependence between the two subunit components with regard to the stability of the two isoforms of striated muscle AMPD. The observed influence of the HPRG content on the catalytic behavior of the two enzymes further strengthens this hypothesis. Based on the preferential localization of HPRG at the sarcomeric I-band and on the presence of a Zn2+ binding motif in the N-terminal regions of fast TnT and of the AMPD1 catalytic subunit, we advance the hypothesis that the Zn binding properties of HPRG could promote the association of AMPD1 to the thin filament.

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The influence of phosphatidate bilayers on pig heart AMP deaminase. Crucial role of pH-dependent lipid-phase transition

Cited by 9 publications

References 24 publications

Effect of acidic phospholipids on the structural properties of recombinant cytosolic human glyoxalase II

Effect of acidic phospholipids on the structural properties of recombinant cytosolic human glyoxalase II

The interaction of phospholipid bilayers with pig heart AMP deaminase: Fourier-transform infrared spectroscopic and kinetic studies

Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour of the Enzyme

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