期刊
CLINICA CHIMICA ACTA
卷 413, 期 1-2, 页码 246-250出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.cca.2011.09.045
关键词
Apolipoprotein A5; Triglyceride; Mutagenesis; Lipoprotein lipase; Mutant
资金
- National Science Council of Taiwan [NSC 96-2320-B-002-038-MY3, NSC 98-2320-B-002-019-MY3]
Background: Apolipoprotein A5 (APOA5) over-expression enhances lipolysis of triglyceride (TG) through stimulation of lipoprotein lipase (LPL) activity; however, an APOA5 G185C variant was found associated with hypertriglyceridemia. The aim of this study was, therefore, to explore the importance of APOA5 185GG in the activation of LPL Methods: A fragment containing mature human APOA5 cDNA was obtained by RT-PCR and subcloned into pET-15b vector. Site-directed mutagenesis was performed to generate 19 variants. Recombinant human APOA5 wild type and variants were produced in Escherichia coli, and then activation of LPL was measured. Results: Activity of APOA5 variants on LPL-mediated 1,2-dimyristoyl-sn-glycero-3-phosphocholine hydrolysis was reduced by 17 to 74% in comparison to wild type APOA5 (P<0.0001). All variants also showed reduced activation (P<0.0001) of LPL-mediated hydrolysis of very low-density lipoprotein (VLDL); activation abilities of APOA5 variants ranged from 31 to 81% of wild-type APOA5. Conclusions: APOA5 residue 185G is very important in LPL-mediated VLDL hydrolysis, and any mutation at this residue will decrease LPL activation and concomitant TG modulation. (C) 2011 Elsevier B.V. All rights reserved.
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