Recombinant Human Apolipoprotein C-II (APOC2)

1. Results from this exploratory analysis suggest that regulatory element methylation levels within the larger TOMM40-APOE-APOC2 gene region correlate with AD-related biomarkers and TOMM40 or APOE gene expression in AD. PMID: 29371683
2. Triglyceride-raising variant alleles of the APOC2 encoding apo C-II, associated with clinical Cardiovascular endpoints. PMID: 28534127
3. The results demonstrate the important role of both intra- and inter-subunit charge interactions in stabilizing apoC-II amyloid fibrils, a process that may be a key factor in determining the general ability of proteins to form amyloid fibrils. PMID: 28229588
4. The results highlight the importance of charge-pair interactions within the apoC-II fibril core PMID: 26196342
5. Conformational rearrangement of apoC-II at lipoprotein surfaces promotes interaction with LPL. PMID: 26026161
6. Large deletion in APOC2 caused by Alu-Alu homologous recombination is associated with with apolipoprotein C-II deficiency. PMID: 25172036
7. No APOC2 mutations were identified in a cohort of patients with diabetic lipemia. PMID: 25131724
8. STAT1 bound on multienhancer 2 cooperates with RXRalpha located on apoCII promoter and upregulates apoCII expression only in macrophages. PMID: 22808166
9. Mutations in GPIHBP1 are rare but the associated clinical phenotype of hypertriglyceridaemia is severe PMID: 22239554
10. These results support a predictive change in the ratio of plasma ApoCIII to ApoCII in pregnancies complicated by severe preeclampsia. PMID: 21321243
11. Substoichiometric concentrations of cyc[60-70] significantly delayed fibril formation by the fibrillogenic, linear peptides apoC-II[60-70] and apoC-II[56-76]. PMID: 22244853
12. Activation of apoC-II fibrils by submicellar lipid (NBD-lyso-12-phosphocholine) is catalytic with release of monomer- and tetramer-bound lipid accompanying fibril elongation and growth. PMID: 21985034
13. Physiological shear flow conditions and conditions experienced during apoC-II manufacturing exert significant effects on apoC-II conformation, leading to protein misfolding, aggregation, and amyloid fibril formation. PMID: 21476595
14. Includes the observation of APOC4-APOC2 read-through transcription PMID: 8530039
15. Our structural model for apoC-II fibrils suggests that apoC-II monomers fold and self-assemble to form a stable cross-beta-scaffold containing relatively unstructured connecting loops. PMID: 21146539
16. Results describe the functional role of the secondary structure in the lipoprotein lipase-binding portion of apolipoprotein CII. PMID: 20042600
17. Human apolipoprotein C-II (apoC-II) slowly forms amyloid fibers in lipid-free solutions at physiological pH and salt concentrations PMID: 11751863
18. During amyloidosis under oxidizing conditions, cysteine-containing apolipoprotein C-II (apoC-II) derivatives form fibrils more rapidly and become extensively tangled compared to wild-type apoC-II. PMID: 12450397
19. Three categories of global constraints, together with the local classical NMR constraints, define the 3D structure of the apoCII-SDS micelle complex and give important clues toward a possible mechanism for the activation of lipoprotein lipase by apoCII. PMID: 12590574
20. regions of lipoprotein lipase that are responsive to activation by apoC-II PMID: 12682050
21. Hydrolysis activated by APOC2 was faster compared with the LPL-mediated lipolysis of emulsion triolein. The binding density of APOC2 was less for small emulsion surfaces than for large ones. PMID: 12782148
22. Different levels of secreted apoC-II had little effect on LDL and HDL protein degradation by HepG2 cells. Compared to controls, cells under-expressing apoC-II showed a 160% higher capacity to selectively take up HDL-CE. PMID: 15778093
23. Results show that purified human HDL and recombinant apolipoprotein A-I lipid particles bind directly to amyloid beta and apolipoprotein C-II amyloid fibrils. PMID: 16432277
24. No relationship was found between ApoCII polymorphism and coronary disease in the Chinese Han population. PMID: 16459141
25. Decrease of LPL activity in the heart, along with the inhibitory effects of excess apolipoprotein C-II, may contribute to the hypertriglyceridemia observed in apolipoprotein c-ii transgenic mice. PMID: 17018885
26. Taken together these data demonstrate an interaction between antichymotrypsin and apolipoprotein C-II that accelerates fibrillogenesis and indicates a specific role for accessory proteins in protein aggregation. PMID: 17174330
27. These results suggested that T-->A substitution at position -190 in the apoC-II gene promoter only partly affected transcriptional activity of the apoC-II promoter, leading to decrease of apoC-II expression in quantity. PMID: 17222387
28. The ozone oxidation product of cholesterol, 3beta-hydroxy-5-oxo-5,6-secocholestan-6-al, rapidly promotes human apolipoprotein (apo) C-II amyloid fibril formation in vitro. PMID: 17429947
29. Both common and rare DNA variants of APOC2 gene were found in 10% patients with severe hypertriglyceridemia PMID: 17717288
30. Phospholipid interaction induces molecular-level polymorphism in APOC2 amyloid fibrils via alternative assembly pathways. PMID: 18005990
31. The concentration-dependent kinetics of apolipoprotein C-II amyloid fibril formation and correlated this with the final size distribution of the fibrils determined by sedimentation velocity experiments, is studied. PMID: 18206908
32. lipids promote on-pathway intermediates of apoC-II fibril assembly and the accumulation of a discrete tetrameric intermediate depends on the molecular state of the lipid PMID: 18852267
33. No significant differences were found between the acute hypertriglyceridaemic pancreatitis cases and controls with severe hypertriglyceridaemia in terms of LPL activity and mass, hepatic lipase activity, CII and CIII mass, or apo E polymorphisms. PMID: 19534808

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HGNC: 609

OMIM: 207750

KEGG: hsa:344

STRING: 9606.ENSP00000466775

UniGene: Hs.75615