Chicoric acid has been widely used in food, medicine, animal husbandry, and other commercial products because of its significant pharmacological activities. However, the shortage of chicoric acid limits its further development and utilization. Currently, Echinacea purpurea (L.) Moench serves as the primary natural resource of chicoric acid, while other sources of it are poorly known. Extracting chicoric acid from plants is the most common approach. Meanwhile, chicoric acid levels vary in different plants as well as in the same plant from different areas and different medicinal parts, and different extraction methods. We comprehensively reviewed the information regarding the sources of chicoric acid from plant extracts, its chemical synthesis, biosynthesis, and bioactive effects.
Echinacea purpurea (EP) is a common medicinal material for extracting anti-RSV components. However, up to now, there has been no effective and simple method to comprehensively reflect the quality of EP. In our current study, the quality of Echinacea purpurea (L.) Moench samples from six different cultivation locations in China was evaluated by establishing a high-performance liquid chromatography (HPLC) fingerprint, combining chemical pattern recognition and multi-component determination. In this study, the chemical fingerprints of 15 common peaks were obtained using the similarity evaluation system of the chromatographic fingerprints of traditional Chinese medicine (2012A Edition). Among the 15 components, three phenolic acids (caftaric acid, chlorogenic acid and cichoric acid) were identified and determined. The similarity of fingerprints of 16 batches of Echinacea purpurea (L.) Moench samples ranged from 0.905 to 0.998. The similarity between fingerprints of five batches of commercially available Echinacea pupurea (L.) Moench and the standard fingerprint ”R” ranged from 0.980 to 0.997, which proved the successful establishment of the fingerprint. PCA and HCA were performed with the relative peak areas of 15 common peaks (peak 3 as the reference peak) as variables. Anhui and Shaanxi can be successfully distinguished from the other four cultivation areas. In addition, the index components of caftaric acid, chlorogenic acid and cichoric acid were in the range of 1.77–8.60 mg/g, 0.02–0.20 mg/g and 2.27–15.87 mg/g. The results of multi-component index content determination show that the contents of the Shandong cultivation area were higher, followed by Gansu, Henan and Hebei, and the lowest were Anhui and Shaanxi. The results are consistent with PCA and HCA, which proved that the quality of Echinacea purpurea (L.) Moench from different origins was different. HPLC fingerprint combined with chemical pattern recognition and multi-component content determination was a reliable, comprehensive and prospective method for evaluating the quality of Echinacea purpurea (L.) Moench. This method provides a scientific basis for the quality control and evaluation of Echinacea purpurea (L.) Moench.
Quiescent state of lymphocyte is a critical mechanism for immunity homeostasis. Until recently it has been recognized that quiescent state is not a passive default mode which also needs many signal molecular and transcriptional factors involvement. However, the mechanism of T cell quiescence remains incompletely understood. In quiescent cell, KLF3 is a highly expressed transcriptional factor, but once T lymphocyte is activated, KLF3 expression is reduced to an undetectable level. The Src homology 2 domain tyrosine phosphatase (SHP-1) is mainly expressed in hematopoietic cells and has been known to plays a negative effect on T cell activation. SHP-1 mutant mice (SHP-1me/me) exhibits multiple hematopoietic cells proliferation disorder and systemic inflammation. Compare to SHP-1me/me mice, KLF3 knock-out mice shows a myeloproliferative disorder and systematic inflammatory responses likewise. Accumulating evidence indicates KLF3 is a crucial transcription factor in T cell quiescent. Based on similarity between SHP-1me/me mice and KLF3 knock-out mice, we explore whether KLF3 cooperate with SHP-1 to maintain cell quiescence. SHP-1 consists two promoter regions that one locates upstream of exon1, mainly expressed in epithelial cell and the other one locates in intron 1 which mainly serves for hematopoietic cell. According to literature, the core promoter element which plays a critical role in SHP-1 gene regulation locates upstream 120bp of transcriptional site. Two cacc boxes (5'---caccc----3') were found among the core promoter elements. We constructed a reporter gene vector named pGL3-SHP1-luci1 which consist two cacc boxes. We also constructed another three vectors based on pGL3-SHP1-luci1. (figure1 left). We process dual-luciferase assay at 72h post transfection (figure1 right). when the proximal cacc box is mutated, the promoter activity is 1.7 times as high as the promoter activity of normal promoter sequence (luci1 vector) (p<0.05). The transcription factor KLF3 functions as a repressor to interact with SHP-1 P2 promoter. We prepare two dioxin-labelled probes based on cacc box motif to verify the binding activities between KLF3 and SHP-1. The probe I is consist of the distal cacc box and the probe II possesses the proximal cacc box. Two specific bands (A,B)were observed when probe target I or target II was adding into DNA-protein mixture (Figure2, lane2, 5). This band specifically disappeared by the addition of excess unlabeled target as a competitor (Figure2, lane 3, 6) which indicates probe can be a target of nuclear proteins from Jurkat cell. To verify KLF3 is the transcription factor involving in the interaction with labelled-probe, we added anti-KLF3 antibody to the EMSA binding reaction. The results show band A disappeared in the presence of target I and it became weaker in the presence of target II, but band B were still present after addition of anti-KLF3 antibody to the mixture (Figure2, lane4, 8). The band A, but not band B, disappeared or become weaken in the presence of anti-KLF3 antibody, indicates KLF3 interacts with SHP-1 P2 promoter. To test the ability of KLF3 binding to SHP-1 promoter 2 (P2) in vivo, we performed chromatin immunoprecipitation (ChIP) analysis using antibodies for KLF3 and compared it with the IgG-negative control. We design one promoter primer targeting a region from -135bp to 53bp which contains a potential KLF3 binding site and one SHP-1 exon15 promoter as a control for antibody enriched DNA analysis. By promoter primer or exon15 primer, specific DNA bands were observed in input. However, only anti-KLF3 enriched DNA can amplify a specific band with promoter primer. By contrast, the IgG negative control enriched DNA fail to amplify positive bands with promoter primer. And for the exon15 primer, it hardly amplified positive bands neither from anti-KLF3-enriched DNA nor from IgG negative control-enriched DNA (figure3). These data demonstrates that KLF3 proteins directly regulate SHP-1 expression. Our study suggests KLF3, as the candidate of programing T cell quiescence, can regulate SHP-1 to maintain quiescent phenotype. Figure 1. Figure 1. Figure 2. Figure 2. Figure 3. Figure 3. Disclosures No relevant conflicts of interest to declare.
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