The construction of resveratrol-loaded protein–polysaccharide–tea saponin complex nanoparticles for controlling physicochemical stability and in vitro digestion

2020 ◽  
Vol 11 (11) ◽  
pp. 9973-9983
Author(s):  
Yang Wei ◽  
Chang Li ◽  
Lei Dai ◽  
Liang Zhang ◽  
Jinfang Liu ◽  
...  
Keyword(s):  
Propylene Glycol ◽  
Ternary Complex ◽  
In Vitro Digestion ◽  
The Novel ◽  
Tea Saponin ◽  
Physicochemical Stability ◽  
Propylene Glycol Alginate

The novel zein–propylene glycol alginate (PGA)–tea saponin (TS) ternary complex nanoparticles were fabricated to deliver resveratrol.

scholarly journals Anti-Colon Cancer Activity of Novel Peptides Isolated from In Vitro Digestion of Quinoa Protein in Caco-2 Cells

Foods ◽  
2022 ◽  
Vol 11 (2) ◽  
pp. 194
Author(s):  
Xin Fan ◽  
Huimin Guo ◽  
Cong Teng ◽  
Biao Zhang ◽  
Christophe Blecker ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Anticancer Activity ◽  
Protein Hydrolysate ◽  
Biological Activities ◽  
Quantitative Polymerase Chain Reaction ◽  
In Vitro Digestion ◽  
The Novel ◽  
Histone Deacetylase 1 ◽  
Liquid Chromatography Tandem Mass

Quinoa peptides are the bioactive components obtained from quinoa protein digestion, which have been proved to possess various biological activities. However, there are few studies on the anticancer activity of quinoa peptides, and the mechanism has not been clarified. In this study, the novel quinoa peptides were obtained from quinoa protein hydrolysate and identified by liquid chromatography–tandem mass spectrometry (LC–MS/MS). The anticancer activity of these peptides was predicted by PeptideRanker and evaluated using an antiproliferative assay in colon cancer Caco-2 cells. Combined with the result of histone deacetylase 1 (HDAC1) inhibitory activity assay, the highly anticancer activity peptides FHPFPR, NWFPLPR, and HYNPYFPG were screened and further investigated. Molecular docking was used to analyze the binding site between peptides and HDAC1, and results showed that three peptides were bound in the active pocket of HDAC1. Moreover, real-time quantitative polymerase chain reaction (RT-qPCR), and Western blot showed that the expression of HDAC1, NFκB, IL-6, IL-8, Bcl-2 was significantly decreased, whereas caspase3 expression showed a remarkable evaluation. In conclusion, quinoa peptides may have the potential to protect against cancer development by inhibiting HDAC1 activity and regulating the expression of the cancer-related genes, which indicates that these peptides could be explored as functional foods to alleviate colon cancer.

scholarly journals A novel Lnc408 maintains breast cancer stem cell stemness by recruiting SP3 to suppress CBY1 transcription and increasing nuclear β-catenin levels

2021 ◽  
Vol 12 (5) ◽  
Author(s):  
Siyang Wen ◽  
Yilu Qin ◽  
Rui Wang ◽  
Liping Yang ◽  
Huan Zeng ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Ternary Complex ◽  
Epithelial Mesenchymal Transition ◽  
The Novel ◽  
Mesenchymal Transition ◽  
Mammosphere Formation ◽  
Transcript Factor ◽  
Signaling Axis

AbstractTumor initiation, development, and relapse may be closely associated with cancer stem cells (CSCs). The complicated mechanisms underlying the maintenance of CSCs are keeping in illustration. Long noncoding RNAs (lncRNAs), due to their multifunction in various biological processes, have been indicated to play a crucial role in CSC renewal and stemness maintenance. Using lncRNA array, we identified a novel lncRNA (named lnc408) in epithelial–mesenchymal transition-related breast CSCs (BCSCs). The lnc408 is high expressed in BCSCs in vitro and in vivo. The enhanced lnc408 is critical to BCSC characteristics and tumorigenesis. Lnc408 can recruit transcript factor SP3 to CBY1 promoter to serve as an inhibitor in CBY1 transcription in BCSCs. The high expressed CBY1 in non-BCSC interacts with 14-3-3 and β-catenin to form a ternary complex, which leads a translocation of the ternary complex into cytoplasm from nucleus and degradation of β-catenin in phosphorylation-dependent pattern. The lnc408-mediated decrease of CBY1 in BCSCs impairs the formation of 14-3-3/β-catenin/CBY1 complex, and keeps β-catenin in nucleus to promote CSC-associated CD44, SOX2, Nanog, Klf4, and c-Myc expressions and contributes to mammosphere formation; however, restoration of CBY1 expression in tumor cells reduces BCSC and its enrichment, thus lnc408 plays an essential role in maintenance of BCSC stemness. In shortly, these findings highlight that the novel lnc408 functions as an oncogenic factor by recruiting SP3 to inhibit CBY1 expression and β-catenin accumulation in nucleus to maintain stemness properties of BCSCs. Lnc408–CBY1–β-catenin signaling axis might serve as a new diagnostic and therapeutic target for breast cancer.

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