Effects of human plasma apolipoproteins C‐I, C‐II and C‐III on the phase‐transition of sonicated vesicles of dipalmitoylphosphatidylcholine

Cardin, Alan D.; Jackson, Richard L.; Johnson, J D

doi:10.1016/0014-5793(82)80045-8

Cited by 10 publications

(5 citation statements)

References 12 publications

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“…This value compares favorably with previous data Jain et al, 1982). Since the polarization values measured above and below Tm are similar to those obtained for DPPC vesicles (Cardin et al, 1982), the local environment of the DPH probe in C,4-ether-PC vesicles is similar to that in DPPC vesicles in corresponding gel and liquid-crystalline phases. Addition of LpL to the sonicated vesicles increases Tm slightly to 27.3 °C.…”

Section: Resultssupporting

confidence: 90%

“…Significant changes in bilayer structure have been observed following addition of apolipoproteins: the polarization of DPH as a function of temperature in DMPC bilayers is altered (Rosseneu et al, 1979;Cardin et al, 1982), and apoA-I added to lipid bilayer vesicles containing entrapped carboxyfluorescein causes a rapid release of the vesicle contents (Figure 2; Kanellis et al, 1980;Segrest et al, 1983). In contrast, the effects of LpL on C14-ether-PC vesicle physical properties (DPH polarization and carboxyfluorescein leakage) are minimal.…”

Section: Discussionmentioning

confidence: 99%

“…The vesicles were incubated at room temperature until the fluorescence of DPH reached a maximal value. Polarization measurements were made as described previously (Cardin et al, 1982).…”

Section: Methodsmentioning

confidence: 99%

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Interaction of lipoprotein lipase with phospholipid vesicles: effect on protein and lipid structure

McLean¹,

Larsen²,

Jackson³

1986

Biochemistry

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The interaction of lipoprotein lipase (LpL) and a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), has been studied by several physical methods. Analysis of the circular dichroic spectrum of LpL gave the following fractional conformation: 35% alpha-helix, 30% beta-pleated sheet, and 45% remaining structure. No significant change in the circular dichroic spectrum of LpL was observed on addition of C14-ether-PC vesicles. The quenching of LpL fluorescence by acrylamide and iodide ion was decreased only slightly by addition of C14-ether-PC vesicles. Addition of LpL to sonicated C14-ether-PC vesicles containing entrapped carboxyfluorescein caused the release of less than 15% of the vesicle contents in 20 min, indicating that the enzyme did not disrupt the structure of the lipid. In contrast, greater than 80% of the vesicle contents were released with the addition of apolipoprotein A-I to an identical vesicle preparation. The temperature dependence of the fluorescence polarization of 1,6-diphenyl-1,3,5-hexatriene incorporated into C14-ether-PC vesicles was not significantly altered by the addition of LpL. When LpL is added to vesicles, the bilayer structure of the vesicles is not disrupted as observed by freeze-fracture electron microscopy. However, at low ionic strength (0.1-0.25 M NaCl) significant aggregation of intact vesicles is observed by light scattering and electron microscopy. Vesicle aggregation is prevented and reversed by 1 M NaCl and by heparin. These data demonstrate that LpL binds to the surface of a lipid interface, without dramatic changes in lipid bilayer or protein structure.

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Section: Resultssupporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

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Interaction of lipoprotein lipase with phospholipid vesicles: effect on protein and lipid structure

McLean¹,

Larsen²,

Jackson³

1986

Biochemistry

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“…Statistical association does not mean biological causality and no insights on the possible causal mechanisms linking ApoC-III and coagulation can be inferred. It could be argued that apolipoproteins could remodel the phospholipid distribution in cellular membranes, 46,47 which in turn influences TF-FVIIa activity at the cell surface. [48][49][50] However, our work does not provide any proof about the molecular mechanisms potentially linking ApoC-III and TF-FVIIa interaction.…”

Section: Discussionmentioning

confidence: 99%

Apolipoprotein C-III Strongly Correlates with Activated Factor VII–Anti-Thrombin Complex: An Additional Link between Plasma Lipids and Coagulation

et al. 2019

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Activated factor VII–anti-thrombin (FVIIa-AT) complex is a potential biomarker of pro-thrombotic diathesis reflecting FVIIa–tissue factor (TF) interaction and has been associated with mortality in patients with coronary artery disease (CAD). Previous data indicated plasma lipids as predictors of FVIIa-AT variability, and plasma lipoproteins as potential stimulators of the coagulation cascade. Our aim was to evaluate the relationships between FVIIa-AT plasma concentration and a broad apolipoprotein profile (including ApoA-I, ApoB, ApoC-III and ApoE). Within the framework of the observational Verona Heart Study, we selected 666 subjects (131 CAD-free and 535 CAD, 75.4% males, mean age: 61.1 ± 10.9 years) not taking anticoagulant drugs and for whom plasma samples were available for both FVIIa-AT assay and a complete lipid profile. Plasma concentration of FVIIa-AT levels significantly and directly correlated with total and high-density lipoprotein cholesterol, triglycerides, ApoA-I, ApoC-III and ApoE levels. ApoC-III showed the strongest correlation (R = 0.235, p = 7.7 × 10−10), confirmed in all the sub-group analyses (males/females and CAD/CAD-free). Only ApoC-III remained associated with FVIIa-AT plasma concentration, even after adjustment for sex, age, CAD diagnosis, body mass index, renal function, smoking status, lipid-lowering therapies and FVIIa levels. The APOC3 gene locus-tagging polymorphism rs964184, previously linked with cardiovascular risk and plasma lipids by genome-wide association studies, was associated with both ApoC-III and FVIIa-AT plasma concentration. Our results indicate a strong association between ApoC-III and FVIIa-AT levels, thereby suggesting that an increased ApoC-III concentration may identify subjects with a pro-thrombotic diathesis characterized by an enhanced TF-FVIIa interaction and activity.

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“…Calcium titrations were conducted on 1 µ felodipine and 2 µ protein as described in Figure 2. Fluorescence polarization measurements were conducted as previously described (Cardin et al, 1982). Excitation was at 365 nm, and emission was monitored at 445 nm.…”

Section: Resultsmentioning

confidence: 99%

Localization of felodipine (dihydropyridine) binding site on calmodulin

Jd¹,

La²,

Thulin³

et al. 1986

Biochemistry

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The fluorescent dihydropyridine calcium antagonist drug felodipine binds to calmodulin (CaM) in a Ca2+-dependent manner. Its binding can be regulated by the interaction of CaM antagonist drugs through allosteric mechanisms [Mills, J.S., & Johnson, J.D. (1985) Biochemistry 24, 4897]. Here, we have examined the binding of a nonspecific hydrophobic fluorescent probe molecule TNS (toluidinylnaphthalenesulfonate) and of felodipine to CAM and several of its proteolytic fragments. While TNS interacts with sites on both the amino-terminal half of the protein [proteolytic fragment TR1C (1-77)] and carboxy-terminal half [proteolytic fragment TR2C (78-148)], felodipine binding shows more selectivity. It binds in a Ca2+-dependent manner to the proteolytic fragments TM1 (1-106) and TR2E (1-90) but exhibits only weak affinity for TR1C (1-77) and TR2C (78-148). Furthermore, felodipine exhibits selectivity over TNS and trifluoperazine (TFP) in blocking the tryptic cleavage between residues 77 and 78. These studies indicate a selective binding of felodipine to a hydrophobic site existing in residues 1-90 and suggest that productive binding requires amino acids in the region 78-90. Although the felodipine binding site is preserved in fragment 1-106, the allosteric interactions between the prenylamine and the felodipine binding sites that are observed with intact CaM are not observed in this fragment. Rather, prenylamine simply displaces felodipine from its binding site on this fragment. Our results are consistent with calmodulin containing not less than two allosterically related hydrophobic drug binding sites. One of these sites (felodipine) appears to be localized in region 1-90 and the other one in region 78-148.

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Effects of human plasma apolipoproteins C‐I, C‐II and C‐III on the phase‐transition of sonicated vesicles of dipalmitoylphosphatidylcholine

Cited by 10 publications

References 12 publications

Interaction of lipoprotein lipase with phospholipid vesicles: effect on protein and lipid structure

Interaction of lipoprotein lipase with phospholipid vesicles: effect on protein and lipid structure

Apolipoprotein C-III Strongly Correlates with Activated Factor VII–Anti-Thrombin Complex: An Additional Link between Plasma Lipids and Coagulation

Localization of felodipine (dihydropyridine) binding site on calmodulin

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