Apolipoprotein C-III(Lys58----Glu). Identification of an apolipoprotein C-III variant in a family with hyperalphalipoproteinemia.

Eckardstein, A. Van; Holz, Harald; Sandkamp, M.; Weng, Wei; Funke, Harald; Assmann, Gerd

doi:10.1172/jci115190

Cited by 80 publications

(48 citation statements)

References 67 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In two following studies, the same group showed that two naturally occurring human mutations of apoC-III, A23T and K58E, were unable to promote triglyceride incorporation during VLDL assembly (73,74). Plasma concentrations of triglycerides and apoC-III are lower in carriers of the A23T or K58E mutations (62,63). Interestingly, recombinant A23T was reported to be as effective as wild-type apoC-III in inhibiting LPL activity (63).…”

Section: Discussionmentioning

confidence: 99%

Apolipoproteins C-I and C-III Inhibit Lipoprotein Lipase Activity by Displacement of the Enzyme from Lipid Droplets

Larsson

Vorrsjö

Talmud

et al. 2013

Journal of Biological Chemistry

147

128

View full text Add to dashboard Cite

Background: Apolipoproteins (apo) C-I and C-III regulate plasma triglyceride metabolism by inhibition of lipoprotein lipase (LPL) activity. Results: ApoC-I or apoC-III prevents LPL from binding to lipid droplets. This results in inhibition of LPL. Conclusion: Inhibition of LPL activity by apoC-I and apoC-III is due to displacement of LPL from lipid droplets. Significance: Our proposed mechanism explains several effects of these apolipoproteins on lipoprotein metabolism.

show abstract

Section: Discussionmentioning

confidence: 99%

Apolipoproteins C-I and C-III Inhibit Lipoprotein Lipase Activity by Displacement of the Enzyme from Lipid Droplets

Larsson

Vorrsjö

Talmud

et al. 2013

Journal of Biological Chemistry

147

128

View full text Add to dashboard Cite

show abstract

“…Three polymorphisms have been described for apoC-III (33,34 ). The observed charge heterogeneity could also result from causes such as phosphorylation, acetylation, and sulfation of the protein.…”

Section: Discussionmentioning

confidence: 99%

Apolipoprotein C-III Isofocusing in the Diagnosis of Genetic Defects in O-Glycan Biosynthesis

Wopereis

Grünewald

Morava³

et al. 2003

Clinical Chemistry

131

View full text Add to dashboard Cite

Background: Defects in the biosynthesis of N-glycans may be found by isoelectric focusing (IEF) of plasma transferrin. No test is available to demonstrate O-glycan biosynthesis defects. Methods: We used isoforms of apolipoprotein C-III (apoC-III) as a marker for the biosynthesis of core 1 mucin type O-glycans. Plasma samples from patients with primary defects and secondary alterations in Nglycan biosynthesis were studied by apoC-III isofocusing. Results: Age-related reference values for apoC-III were determined. Plasma samples from patients with the primary congenital disorders of glycosylation (CDG) types Ia-Ic, Ie, If, IIa, and IId all showed a normal apoC-III isofocusing profile. Plasma from two patients with CDG type IIx were tested: one showed a normal apoC-III distribution, whereas the other showed a hypoglycosylation profile. In plasma from patients with hemolytic uremic syndrome (HUS), a hypoglycosylation profile was obtained. Conclusions: IEF of apoC-III is a rapid and simple technique that may be used as a screening assay for

show abstract

“…74,75 Some missense mutations in APOC3 encode for structural apoC-III mutants, which show reduced abundance in HDL and cause a similar lipoprotein phenotype as the nonsense mutations. 76 It may hence be that the genetically determined lack of apoC-III in HDL improves the functionality and antiatherogenicity of HDL.…”

Section: Apolipoprotein C-iiimentioning

confidence: 99%

Dysfunctional high-density lipoproteins in coronary heart disease: implications for diagnostics and therapy

Annema

Eckardstein

2016

Translational Research

View full text Add to dashboard Cite

Low plasma levels of high-density lipoprotein (HDL) cholesterol are associated with increased risks of coronary heart disease. HDL mediates cholesterol efflux from macrophages for reverse transport to the liver and elicits many anti-inflammatory and anti-oxidative activities which are potentially antiatherogenic. Nevertheless, HDL has not been successfully targeted by drugs for prevention or treatment of cardiovascular diseases. One potential reason is the targeting of HDL cholesterol which does not capture the structural and functional complexity of HDL particles. Hundreds of lipid species and dozens of proteins as well as several microRNAs have been identified in HDL. This physiological heterogeneity is further increased in pathologic conditions due to additional quantitative and qualitative molecular changes of HDL components which have been associated with both loss of physiological function and gain of pathologic dysfunction. This structural and functional complexity of HDL has prevented clear assignments of molecules to the functions of normal HDL and dysfunctions of pathologic HDL. Systematic analyses of structure-function relationships of HDL-associated molecules and their modifications are needed to test the different components and functions of HDL for their relative contribution in the pathogenesis of atherosclerosis. The derived biomarkers and targets may eventually help to exploit HDL for treatment and diagnostics of cardiovascular diseases.

show abstract

Apolipoprotein C-III(Lys58----Glu). Identification of an apolipoprotein C-III variant in a family with hyperalphalipoproteinemia.

Cited by 80 publications

References 67 publications

Apolipoproteins C-I and C-III Inhibit Lipoprotein Lipase Activity by Displacement of the Enzyme from Lipid Droplets

Apolipoproteins C-I and C-III Inhibit Lipoprotein Lipase Activity by Displacement of the Enzyme from Lipid Droplets

Apolipoprotein C-III Isofocusing in the Diagnosis of Genetic Defects in O-Glycan Biosynthesis

Dysfunctional high-density lipoproteins in coronary heart disease: implications for diagnostics and therapy

Contact Info

Product

Resources

About