Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 3 de 3
Filter
Add more filters










Database
Language
Publication year range
1.
Heliyon ; 9(7): e17908, 2023 Jul.
Article in English | MEDLINE | ID: mdl-37483732

ABSTRACT

Renal fibrosis (RF) is a common pathological feature of chronic kidney disease (CKD), which remains a major public health problem. As now, there is still lack of chemical or biological drugs to reverse RF. Shen-shuai-yi Recipe (SSYR) is a classical Chinese herbal formula for the treatment of CKD. However, the effects and mechanisms of SSYR in treating RF are still not clear. In this study, the active constituents SSYR for treating RF were explored by UHPLC-Q-Orbitrap HRMS. Bioinformatics analyses were employed to analyze the key pharmacological targets and the core active constituents of SSYR in the treatment of RF. In experimental validation, vehicle or SSYR at doses of 2.12 g/kg/d and 4.25 g/kg/d were given by orally to unilateral ureteric obstruction (UUO) mice. 13 days after treatment, we detected the severity of renal fibrosis, extracellular collagen deposition and pre-fibrotic signaling pathways. Bioinformatics analysis suggested that signal transducer and activator of transcription 3 (STAT3) was the core target and lenticin, luteolin-7-O-rutinoside, hesperidin, kaempferol-3-O-rutinoside, and 3,5,6,7,8,3',4'-heptamethoxyflavone were the key constituents in SSYR for treating RF. SSYR significantly reduced the expressions of fibronectin (FN), α-smooth muscle actin (α-SMA), collagen-I and alleviated renal interstitial collagen deposition in UUO kidneys. In mechanism, SSYR potently blocked the phosphorylation of STAT3 and Smad3 and suppressed the expression of connective tissue growth factor (CTGF). Collectively, SSYR can ameliorate RF via inhibiting the phosphorylation of STAT3 and its downstream and reducing the collagen deposition, suggesting that SSYR can be developed as a novel medicine for treating RF.

2.
J Colloid Interface Sci ; 466: 56-61, 2016 Mar 15.
Article in English | MEDLINE | ID: mdl-26706486

ABSTRACT

Titanium dioxide (TiO2)/fullerene hybrid nanocomposite was facilely fabricated by mixing TiO2 and poly-carboxylic acid functionalized fullerene under an ultrasonication-evaporation method. It was found that the TiO2/fullerene composite could serve as an efficient and reusable photocatalyst for degradation of rhodamine B dye under visible light (λ>400 nm). The as-prepared photocatalyst was characterized by X-ray diffraction (XRD), transmission electron microscopy (TEM) and diffuse reflection spectroscopy (DRS). The degradation experiments revealed that the photocatalytic activity strongly depends on the contents of fullerene from 0.5% to 3% mass ratio. The incorporation of fullerene into TiO2 efficiently extended the absorption spectrum of photocatalyst to visible light region, enhanced the adsorption capacity and degradation efficiency, resulting from a synergistic effect of fullerene and TiO2. The trapping experiments demonstrated that both the photo-generated hole (h(+)) and the reactive oxygen species such as superoxide anion radical (˙O2(-)) were involved in the photocatalytic reaction.

3.
J Exp Bot ; 61(15): 4249-61, 2010 Oct.
Article in English | MEDLINE | ID: mdl-20643810

ABSTRACT

In rice, the class I small heat shock protein (sHSP-CI) genes were found to be selectively induced by L-azetidine-2-carboxylic acid (AZC) on chromosome 3 but not chromosome 1. Here it is shown that a novel cis-responsive element contributed to the differential regulation. By serial deletion and computational analysis, a 9 bp putative AZC-responsive element (AZRE), GTCCTGGAC, located between nucleotides -186 and -178 relative to the transcription initiation site of Oshsp17.3 was revealed. Deletion of this putative AZRE from the promoter abolished its ability to be induced by AZC. Moreover, electrophoretic mobility shift assay (EMSA) revealed that the AZRE interacted specifically with nuclear proteins from AZC-treated rice seedlings. Two AZRE-protein complexes were detected by EMSA, one of which could be competed out by a canonical heat shock element (HSE). Deletion of the AZRE also affected the HS response. Furthermore, transient co-expression of the heat shock factor OsHsfA4b with the AZRE in the promoter of Oshsp17.3 was effective. The requirement for the putative AZRE for AZC and HS responses in transgenic Arabidopsis was also shown. Thus, AZRE represents an alternative form of heat HSE, and its interaction with canonical HSEs through heat shock factors may be required to respond to HS and AZC.


Subject(s)
Azetidinecarboxylic Acid/pharmacology , Base Pairing/genetics , Chromosomes, Plant/genetics , Heat-Shock Proteins, Small/genetics , Heat-Shock Response/drug effects , Oryza/genetics , Promoter Regions, Genetic , Arabidopsis/drug effects , Arabidopsis/genetics , Base Sequence , Electrophoretic Mobility Shift Assay , Gene Expression Regulation, Plant/drug effects , Genes, Plant/genetics , Heat-Shock Proteins, Small/metabolism , Heat-Shock Response/genetics , Molecular Sequence Data , Nuclear Proteins/metabolism , Oryza/drug effects , Plant Proteins/genetics , Plant Proteins/metabolism , Plants, Genetically Modified , Protein Binding/drug effects , Protein Biosynthesis/drug effects , Protein Synthesis Inhibitors/pharmacology , Response Elements/genetics , Sequence Alignment , Sequence Deletion , Stress, Physiological/drug effects , Stress, Physiological/genetics
SELECTION OF CITATIONS
SEARCH DETAIL
...