Qingqing Gu

Nantong University, Tungchow, Jiangsu Sheng, China

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Publications (3)3.99 Total impact

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    ABSTRACT: Curcumin was reported to exhibit a wide range of pharmacological effects including antioxidant, anti-inflammatory, and antiproliferative activities and significantly prevent smooth muscle cells migration. In the present study, a novel kind of curcumin loaded nanoparticles (Cur-NP) has been prepared and characterized with the aim of inhibiting inflammation formation and accelerating the healing process of the stented arteries. Cur-NP was administrated intravenously after stent implantation twice a week and detailed tissue responses were evaluated. The results demonstrated that intravenous administration of Cur-NP after stent implantation accelerated endothelial cells restoration and endothelium function recovery and may potentially be an effective therapeutic alternative to reduce adverse events for currently available drug eluting stents.
    Preview · Article · Jul 2015
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    ABSTRACT: BACKGROUND: Cardiac troponin T (cTnT) is crucial in regulating the contraction of striated muscle and plays an important role in cardiomyopathy, which can lead to heart failure. Alternative splicing of exon 5 is developmentally regulated. Exon 5 is included in the embryonic cTnT but is excluded from the adult cTnT. Changes of cTnT isoform expression have been reported in hypothyroidism, cardiac hypertrophy of the left ventricle and, in some cases, heart failure. OBJECTIVE: To investigate the underlying mechanism of exon 5 alternative splicing and identify potential therapeutics for heart disease. METHODS: A cTnT minigene was constructed and a series of minigene constructions were generated with intron deletions from the full length of cTnT exons 3 to 6. RESULTS: Reverse-transcription polymerase chain reaction results demonstrated that the splicing silencers were located in intron 4 and 5. In addition, ASF/SF2, a member of the SR family of splicing factors, was found to promote the inclusion of cTnT exon 5 in a dose-dependent manner. Both dual-specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A) and cAMP-dependent kinase (PKA) phosphorylated the splicing factor SF2/ASF and inhibited the inclusion of cTnT exon 5. CONCLUSIONS: PKA and Dyrk1A induced changes in the alternative splicing of TNNT2 exon 5 via SF2/ASF, potentially uncovering new avenues for research into the molecular mechanism and aiding in the development of new therapeutics in cardiomyopathy.
    No preview · Article · Dec 2013 · Experimental and clinical cardiology
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    ABSTRACT: Ca(2+)/calmodulin-dependent protein kinase (CaMK) IIδ is predominantly expressed in the heart. There are three isoforms of CaMKIIδ resulting from the alternative splicing of exons 14, 15, and 16 of its pre-mRNA, which is regulated by the splicing factor SF2/ASF. Inclusion of exons 15 and 16 or of exon 14 generates δA or δB isoform. The exclusion of all three exons gives rise to δC isoform, which is selectively increased in pressure-overload-induced hypertrophy. Overexpression of either δB or δC induces hypertrophy and heart failure, suggesting their specific role in the pathogenesis of hypertrophy and heart failure. It is well known that the β-adrenergic-cyclic AMP-dependent protein kinase A (PKA) pathway is implicated in heart failure. To determine the role of PKA in the alternative splicing of CaMKIIδ, we constructed mini-CaMKIIδ genes and used these genes to investigate the regulation of the alternative splicing of CaMKIIδ by PKA in cultured cells. We found that PKA promoted the exclusion of exons 14, 15, and 16 of CaMKIIδ, resulting in an increase in δC isoform. PKA interacted with and phosphorylated SF2/ASF, and enhanced SF2/ASF's activity to promote the exclusion of exons 14, 15, and 16 of CaMKIIδ, leading to a further increase in the expression of δC isoform. These findings suggest that abnormality in β-adrenergic-PKA signaling may contribute to cardiomyopathy and heart failure through dysregulation in the alternative splicing of CaMKIIδ exons 14, 15, and 16 and up-regulation of CaMKIIδC.
    Preview · Article · Nov 2011 · PLoS ONE