An apolipoprotein preferentially enriched in cholesteryl ester-rich very low density lipoproteins

Shore, B.; Shore, Virgie G.; Salel, Antone F.; Mason, Dean T.; Zelis, Robert

doi:10.1016/0006-291x(74)90882-1

Cited by 83 publications

(17 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These data indicate that the rat liver can synthesize and secrete lipoproteins having many of the characteristics of both the circulating B-VLDL of hypercholesterolemic animals (9-12) and the broad-beta lipoproteins of human dysbetalipoproteinemia (1,44). These include VLDL having increased cholesterol ester and decreased triacylglycerol levels and diminished apoC-II and apoC-III content.…”

Section: Discussionmentioning

confidence: 84%

“…These observations do not rule FIGuRE 3 Electrophoresis in agarose of serum and perfusate lipoproteins. (1) Normal rat serum; (2) VLDL secreted by perfused liver from normal animals; (3) VLDL secreted by perfused liver from hypercholesterolemic rats; (4) serum from hypercholesterolemic rats; (5) LDL secreted by perfused liver from hypercholesterolemic rats; (6) LDL isolated from the serum of hypercholesterolemic rats. Gels depicted in 3A and 3B were run at different times so that the mobility of the lipoproteins on the two gels are not directly comparable.…”

Section: Resultsmentioning

confidence: 99%

“…Primary familial dysbetalipoproteinemia (Type III hyperlipoproteinemia, broad-beta disease) is characterized by the presence ofvery low density lipoproteins (VLDL)' showing 8-mobility on electrophoresis, containing abnormally high amounts of both cholesterol and apolipoprotein (apo) E (arginine-rich protein), and a decreased proportion of apoC (1,2). Based on these properties and a number of metabolic studies, it has been suggested that the abnormal VLDL found in familial dysbetalipoproteinemia represents an accumulation of remnants of VLDL and chylomicron catabolism which have not been efficiently removed (2)(3)(4)(5)(6).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Secretion of Cholesterol-Rich Lipoproteins by Perfused Livers of Hypercholesterolemic Rats

Noël¹,

Wong²,

Dolphin³

et al. 1979

J. Clin. Invest.

102

View full text Add to dashboard Cite

A B S T R A C T Rats maintained on a high-fat diet supplemented with propylthiouracil develop a hypercholesterolemia, an increased serum level of apolipoprotein (apo) E, abnormal very low density lipoproteins (VLDL) and low density lipoproteins (LDL), and a fatty liver which contains cholesterol ester as its major lipid. The fatty liver secretes apoE into a recirculating perfusate at a significantly higher rate and produces cholesterol ester-rich, apoC-deficient VLDL with slower electrophoretic mobility than the triacylglycerol-rich VLDL produced by perfused normal livers. LDL

show abstract

Section: Discussionmentioning

confidence: 84%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Secretion of Cholesterol-Rich Lipoproteins by Perfused Livers of Hypercholesterolemic Rats

Noël¹,

Wong²,

Dolphin³

et al. 1979

J. Clin. Invest.

102

View full text Add to dashboard Cite

show abstract

“…ApoE is unusually rich in arginines (11% vs. 4.2% for all vertebrate proteins) (38), and has twice as many as apoA-I (34 of 299 vs. 17 of 242 residues). Indeed, the original name for apoE was arginine-rich protein (39). High levels of arginine are commonly found in proteins that bind phosphate or phosphate-rich ligands such as DNA or RNA, reflecting the highly favorable binding energy between arginine and phosphate.…”

Section: Models Of the Apoeanddppc Particle In Solutionmentioning

confidence: 99%

Apolipoprotein E•dipalmitoylphosphatidylcholine particles are ellipsoidal in solution

Peters‐Libeu

Newhouse

Hall

et al. 2007

Journal of Lipid Research

View full text Add to dashboard Cite

Apolipoprotein E (apoE) is a major protein component of cholesterol-transporting lipoprotein particles in the central nervous system and in plasma. Polymorphisms of apoE are associated with cardiovascular disease and with a predisposition to Alzheimer's disease and other forms of neurodegeneration. For full biological activity, apoE must be bound to a lipoprotein particle. Complexes of apoE and phospholipid mimic many of these activities. In contrast to a widely accepted discoidal model of apoA-I bound to dimyristoylphosphatidylcholine, which is based on solution studies, an X-ray diffraction study of apoE bound to dipalmitoylphosphatidylcholine (DPPC) indicated that apoE&DPPC particles are quasi-spheroidal and that the packing of the phospholipid core is similar to a micelle. Using small-angle X-ray scattering, we show that apoE&DPPC particles in solution are ellipsoidal and that the shape of the phospholipid core is compatible with a twisted-bilayer model. The proposed model is consistent with the results of mass spectrometric analysis of products of limited proteolysis. These revealed that the nonlipid-bound regions of apoE in the particle are consistent with an a-helical hairpin.-Peters-Libeu, C. A., Y. Newhouse, S. C. Hall, H. E. Witkowska, and K. H. Weisgraber. Apolipoprotein E&dipalmitoylphosphatidylcholine particles are ellipsoidal in solution. J. Lipid Res.

show abstract

“…The Journal of Clinical Investigation Volume 57 March 1976-714721 714 hypothyroidism (13), type III hyperlipoproteinemia (14), and in obstructive jaundice (15).…”

Section: Introductionmentioning

confidence: 99%

Serum lipoproteins and apolipoproteins in rats with streptozotocin-induced diabetes.

Bar‐On¹,

Roheim²,

Eder³

1976

J. Clin. Invest.

134

View full text Add to dashboard Cite

A B STRA CT The lipoproteins of rats fed a high sucrose diet and made diabetic by administration of 45 mg/kg of streptozotocin were studied. All lipoprotein classes were found to be present in increased concentrations. The apolipoprotein composition of the various lipoprotein fractions was studied by polyacrylamide-gel electrophoresis in the presence of 8 M urea, isoelectric focusing in the presence of 8 M urea, and sodium dodecyl sulfate gel electrophoresis in polyacrylamide gels. In the very low density lipoproteins (VLDL) of diabetic rats, there was a marked alteration in the relative amounts of C proteins by polyacrylamide-gel electrophoresis, and this was found by isoelectric focusing to be primarily a relative increase in C-III-3 apoprotein and a decrease in C-III-0. In addition, in the diabetic rats, the VLDL contained a protein of mol wt 46,000, the A-IV protein, which normally is only present in the high density lipoproteins. In the high density lipoproteins, (HDL) the same alterations in pattern of the C proteins seen in the VLDL were present. Furthermore, the arginine-rich and A-IV protein normally present in HDL could not be detected in the HDL, although the other apolipoproteins are present.Apolipoprotein concentrations were determined by quantitative immunoelectrophoresis. It was found that in the diabetic rats there was an increase in the total amount of apo-B in the plasma, with the increment divided proportionately between the VLDL and the low density lipoprotein (LDL). The total apo-C concentration of plasma increased minimally. The A-IV concentration of plasma increased by 27%; it decreased markedly in the HDL, but appeared in increased amounts in both VLDL and in the d > 1.21 fraction. The arginine-rich protein decreased

show abstract

An apolipoprotein preferentially enriched in cholesteryl ester-rich very low density lipoproteins

Cited by 83 publications

References 11 publications

Secretion of Cholesterol-Rich Lipoproteins by Perfused Livers of Hypercholesterolemic Rats

Secretion of Cholesterol-Rich Lipoproteins by Perfused Livers of Hypercholesterolemic Rats

Apolipoprotein E•dipalmitoylphosphatidylcholine particles are ellipsoidal in solution

Serum lipoproteins and apolipoproteins in rats with streptozotocin-induced diabetes.

Contact Info

Product

Resources

About