Kinetic study of the action of snake venom phospholipase A2 on human serum high density lipoprotein 3.

Pattnaik, Nikhil M.; Kézdy, Ferenc J.; Scanu, Angelo M.

doi:10.1016/s0021-9258(17)33644-x

Cited by 53 publications

(14 citation statements)

References 27 publications

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“…Both the unmodified 9.2-nm rHDL and phospholipid-depleted, 8.0-nm rHDL contain three apoA-I molecules per particle. This is in agreement with what has been reported in earlier studies in which plasma HDL were incubated with phospholipase A 2 (3,4). It also suggests that the reduction in rHDL size is a direct consequence of phospholipid depletion.…”

Section: Discussionsupporting

confidence: 92%

Influence of phospholipid depletion on the size, structure, and remodeling of reconstituted high density lipoproteins

Rye

Duong

2000

Journal of Lipid Research

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This study shows that phospholipid depletion has a major impact on the size and structure of spherical, reconstituted high density lipoproteins (rHDL) and their remodeling by cholesteryl ester transfer protein (CETP). Spherical rHDL, 9.2 nm in diameter with a phospholipid/cholesteryl ester/unesterified cholesterol/apolipoprotein A-I (apoA-I) (PL/CE/UC/A-I) molar ratio of 37.3/24.5/4.1/1.0, were depleted progressively of phospholipids by incubation with phospholipase A 2 . After 30 min of incubation the PL/CE/ UC/A-I molar ratio of the rHDL was 8.0/31.2/4.4/1.0 and their diameter had decreased to 8.0 nm. Comparable changes in rHDL size and composition were also apparent when the incubations were carried out in the presence of other lipoprotein classes and lipoprotein-deficient plasma. The changes in size and composition were not accompanied by the dissociation of apoA-I from the rHDL. Phospholipid depletion did not affect rHDL surface charge or the structure and stability of apoA-I. The remodeling of unmodified and phospholipid-depleted rHDL by CETP was also investigated. When the rHDL were incubated for 3 h with CETP and Intralipid, transfers of core lipids between the phospholipid-depleted rHDL and Intralipid were decreased relative to unmodified rHDL. This difference was no longer apparent when the incubations were extended beyond 3 h. In these incubations apoA-I dissociated from the phospholipid-depleted and unmodified rHDL at 3 and 12 h, respectively. At 24 h the respective diameters of the unmodified rHDL and phospholipid-depleted rHDL were 8.0 and 7.8 nm. In conclusion, phospholipid depletion has a major impact on rHDL size and their remodeling by CETP. -Rye, K-A., and M. N. Duong. Influence of phospholipid depletion on the size, structure, and remodeling of reconstituted high density lipoproteins.

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Section: Discussionsupporting

confidence: 92%

Influence of phospholipid depletion on the size, structure, and remodeling of reconstituted high density lipoproteins

Rye

Duong

2000

Journal of Lipid Research

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“…a-Phospholipase /42. The preparation of HDL3 was done as previously reported (Henderson et al, 1975;Pattnaik et al, 1976). An electrophoretically homogeneous a-phospholipase A2 purified from the venom of C. adamanteus according to the method of Wells & Hanahan (1969) was a gift from Dr. Betty W, Shen, Department of Biochemistry, University of Chicago.…”

Section: Methodsmentioning

confidence: 99%

“…the particles in such a way as to maximize hydrophilic interactions between these components and the surrounding aqueous milieu (Henderson et al, 1975;; Shipley et al, 1972;Finer et al, 1975;Pattnaik et al, 1976; Verdery & Nichols, 1975;Segrest et al, 1974;Stoffel et al, 1974). This surface distribution of phospholipids and polar regions of proteins has been incorporated into various structural models (Verdery & Nichols, 1975;Segrest et al, 1974;Stoffel et al, 1974;Faggner et al, 1973).…”

mentioning

confidence: 99%

“…No change in the NMR signals of the phospholipids in HDF was apparent; thus, there appears to be no immobilization of the HDF phospholipids. Recently, Pattnaik et al (1976) studied the action of Crotalus adamanteus «-phospholipase A2 on HDF3 and found that all of the phospholipids except for sphingomyelin are accessible to the enzyme and are converted into their lyso derivatives. They also observed that the reaction follows first-order kinetics and that, in spite of extensive hydrolysis, there were no significant changes in the properties of the digested particles.…”

mentioning

confidence: 99%

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Action of α-phospholipase A₂ on human serum high density lipoprotein-3: kinetic study of the reaction by ³¹P nuclear magnetic resonance spectroscopy

Brasure¹,

Henderson²,

Glonek³

et al. 1978

Biochemistry

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31P nuclear magnetic resonance spectroscopy (31P NMR) was used to monitor the hydrolysis of phospholipids in human serum high-density lipoprotein-3 (HDL3) by «-phospholipase A2 purified from Crotalus adamanteus venom. The 31P NMR spectra obtained at regular intervals during incubation of HDL3 with the enzyme indicated that phosphatidylcholine was completely converted into lysophosphatidylcholine. The proton-decoupled line widths of the phosphatidylcholine in untreated HDL3, and of the lysophosphatidylcholine produced by the enzymatic digestion of the lipoprotein particle, were ca. 7.5 Hz over the entire course of the reaction. Moreover, the chemical shifts of phosphatidylcholine and lysophosphatidylcholine (+1.11 and 0.64 ppm, respectively, with 0.0 ppm assigned to 85% H3PO4) were invariant under these conditions. From these studies, it was determined that the «-phospholipase A2 catalyzed hydrolysis of phosphatidylcholine in HDF3 follows first-order kinetics, in confirmation 1 he lipid composition of the various classes of human serum lipoproteins has been determined. In all classes, phospholipids, specifically phosphatidylcholine (PC),1 are the predominant polar lipid components (for recent reviews, cf. Morrisett et al., 1975). Despite this abundance of compositional information, neither the function nor structural arrangement of the phospholipids in these complexes is well understood.Several laboratories have been investigating the structural arrangement of the components of HDL3 and of other serum lipoproteins by means of a wide array of chemical and physical techniques (cf. Morrisett et al., 1975). Several lines of evidence indicate that the phospholipids are oriented on the surface of f From the

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“…At higher pressures, the monolayer deviated from ideality, and the Recent physical and chemical studies on both high-density lipoproteins (HDL) and low-density lipoproteins (LDL) have suggested that apoproteins, cholesterol, and phospholipids form a monolayer at the outer surface of these lipoproteins (Morrisett et al, 1975). The enzymatic proteolysis of the intact lipoproteins (Aggerbeck et Camejo, 1969;Pattnaik et al, 1976) results in aggregation, indicating that the apoproteins play an important role in maintaining the lipoprotein structure. Such stabilization should be intimately related to the surface properties of the apoproteins.…”

mentioning

confidence: 99%

Properties of human apolipoprotein A-I at the air-water inferface

Shen¹,

Scanu²

1980

Biochemistry

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In order to study the properties and structure of human apolipoprotein A-I (apo-A-I) at the air-water interface, we formed monolayers of apo-A-I by either spreading or spontaneous adsorption from the subphase. The rate of monolayer formation, force-area (II-A) curves, and surface potentials were analyzed quantitatively. We constructed force-area curves by keeping constant either (a) the total area or (b) the total number of molecules. The results obtained by method a were reproducible and superimposable with those obtained from adsorbed monolayers. In turn, the results obtained by method b indicated aging effects by both pressure and potential measurements, suggesting irreversible denaturation of apo-A-I at areas larger than 50 A2/amino acid. At pressures lower than 0.5 dyn/cm, apo-A-I monolayers followed the two-dimensional ideal gas law; the molecular weight of the apoprotein calculated from the intercept on the ordinate of the IL4 vs. plot had an average value of 25 000. At higher pressures, the monolayer deviated from ideality, and the Recent physical and chemical studies on both high-density lipoproteins (HDL) and low-density lipoproteins (LDL) have suggested that apoproteins, cholesterol, and phospholipids form a monolayer at the outer surface of these lipoproteins (Morrisett et al., 1975). The enzymatic proteolysis of the intact lipoproteins (Aggerbeck et Camejo, 1969;Pattnaik et al., 1976) results in aggregation, indicating that the apoproteins play an important role in maintaining the lipoprotein structure. Such stabilization should be intimately related to the surface properties of the apoproteins. In order to explore the behavior of apolipoproteins at amphiphilic interfaces and their relation to the surface organization of human serum HDL3, we turned our attention to apolipoprotein A-I (apo-A-I), which is the major protein component of plasma HDL.

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Kinetic study of the action of snake venom phospholipase A2 on human serum high density lipoprotein 3.

Cited by 53 publications

References 27 publications

Influence of phospholipid depletion on the size, structure, and remodeling of reconstituted high density lipoproteins

Influence of phospholipid depletion on the size, structure, and remodeling of reconstituted high density lipoproteins

Action of α-phospholipase A₂ on human serum high density lipoprotein-3: kinetic study of the reaction by ³¹P nuclear magnetic resonance spectroscopy

Properties of human apolipoprotein A-I at the air-water inferface

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Kinetic study of the action of snake venom phospholipase A2 on human serum high density lipoprotein 3.

Cited by 53 publications

References 27 publications

Influence of phospholipid depletion on the size, structure, and remodeling of reconstituted high density lipoproteins

Influence of phospholipid depletion on the size, structure, and remodeling of reconstituted high density lipoproteins

Action of α-phospholipase A2 on human serum high density lipoprotein-3: kinetic study of the reaction by 31P nuclear magnetic resonance spectroscopy

Properties of human apolipoprotein A-I at the air-water inferface

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Action of α-phospholipase A₂ on human serum high density lipoprotein-3: kinetic study of the reaction by ³¹P nuclear magnetic resonance spectroscopy