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peer reviewedQuinoa is an excellent source of nutritional and bioactive components. Protein is considered a key nutritional advantage of quinoa grain, and many studies have highlighted the nutritional and physicochemical properties of quinoa protein. In addition, quinoa protein is a good precursor of bioactive peptides. This review focused on the biological properties of quinoa protein hydrolysate and peptides, and gave a summary of the preparation and functional test of quinoa protein hydrolysate and peptides. A combination of milling fractionation and solvent extraction is recommended for the efficient production of quinoa protein. The biological functionalities of quinoa protein hydrolysate, including antidiabetic, antihypertensive, anti-inflammatory, antioxidant activities, and so on, have been extensively investigated based on in vitro studies and limited animal models. Additionally, bioinformatics analysis, including proteolysis simulation, virtual screening, and molecular docking, provides an alternative or assistive approach for exploring the potential bioactivity of quinoa protein and peptides. Nevertheless, further research is required for industrial production of bioactive quinoa peptides, verification of health benefits in humans, and mechanism interpretation of observed effects

Functional properties and adipogenesis inhibitory activity of protein hydrolysates from quinoa ( Chenopodium quinoa

The functional properties and adipogenesis inhibitory activity of quinoa protein hydrolysates, prepared using papain, pepsin, and pancreatin for 0, 30, 60, 90, and 120 min, were studied. For these three kinds of proteases, the solubility of the hydrolysates significantly increased with the increasing DH in pH range of 3–8, while the EAI and ESI of these hydrolysates significantly decreased during hydrolysis. The anti‐inflammatory activity of these protein hydrolysates was measured. All of these protein hydrolysates showed high anti‐inflammatory activity. However, there was no significant difference in anti‐inflammatory activity between protein hydrolysates and total protein from quinoa. These protein hydrolysates also inhibited lipid accumulation during differentiation within the range of concentrations of 0–1,600 μg/ml, which exerted no cytotoxicity toward 3T3‐L1 cells. The protein hydrolysates from quinoa prepared using pepsin for 120 min (PEP‐120) had the highest activity with an IC50 value of 786.58 μg/ml. Moreover, LC‐MS/MS analysis of PEP‐120 showed that five main bioactive peptides, which have been demonstrated to have ACE inhibitor, antioxidant, and antithrombotic activities, were present in PEP‐120. In addition, gene expression and Western blot analysis revealed that PEP‐120 suppressed the 3T3‐L1 cell differentiation through the peroxisome proliferator‐activated receptor γ (PPARγ) pathway

Expression of Bioactive Lunasin Peptide in Transgenic Rice Grains for the Application in Functional Food

Lunasin, a bioactive peptide initially isolated from soybean, has anticancer, anti-inflammatory, and antioxidant activity. Due its great application value, lunasin seems to be a candidate gene in improving the nutritional value of crops. In this study, lunasin was inserted into the rice genome to evaluate whether it was feasible to express lunasin using the rice expression system and improve the bioactivity of protein in rice for our needs. We generatedlunasin-overexpressing rice lines, and chose three independent transgenic rice lines for further study. The lunasin content in trans-lunasin rice detected by UPLC-MS/MS was 1.01 × 10−3 g·kg−1 dry rice flour with grease removal in the lunasin extracts. The antioxidant efficacy of LET (lunasin-enriched fraction from trans-lunasin rice) and PEW (peptide-enriched fraction from wild type rice) was compared. Due to the presence of lunasin, LET showed higher (p < 0.05) antioxidant activity than PEW. LET exhibited high DPPH radical scavenging activity (IC50 value, 8 g·L−1), strong ABTS+ radical scavenging activity (IC50 value, 1.18 g·L−1), and great oxygen radical scavenging activity (170 μmol·L−1 Trolox equivalents when the concentration reached 4 g·L−1). Moreover, LET presented significantly higher (p < 0.05) anti-inflammatory activity on macrophage cells, and the NO production and the release of pro-inflammatory cytokines (IL-6, MCP1, and TNF-α) were significantly inhibited by LET. However, because of the low purity, LET showed weaker antioxidant and anti-inflammatory activity when compared to the Lunasin standard. These results suggested that it is feasible to use the rice expression system to express the exogenous lunasin in rice, and lunasin-overexpressing rice seems to be a candidate resource for application in functional food. Rice rich in lunasin is beneficial for human health, and could be used as a functional food in the diets of cancer and obese patients in the future

Marital adjustment and depressive symptoms among Chinese perinatal women: a prospective, longitudinal cross-lagged study

Objectives The objective was to assess the prevalence of perinatal depressive symptoms and determine the trajectories of marital adjustment and depressive symptoms and their reciprocal relationships among Chinese perinatal women.Design This was a prospective, longitudinal cross-lagged study.Setting The study was conducted at the outpatient department of the largest women’s and children’s hospital in China, which is located in Chengdu, Sichuan Province.Participants Four hundred and sixty-three mothers were conveniently sampled.Main outcome measures The Dyadic Adjustment Scale and the Chinese version of the Edinburgh Postnatal Depression Scale were used to evaluate marital adjustment and depressive symptoms, respectively, at three time points: the first trimester of pregnancy (T1), the third trimester of pregnancy (T2) and 6 weeks after childbirth (T3). Descriptive statistics were used to assess the prevalence of perinatal depressive symptoms, and repeated-measures analysis of variance (ANOVA) was used to determine the trajectories of marital adjustment and depressive symptoms among the participants. A cross-lagged model was used to explore the reciprocal relationship between marital adjustment and depressive symptoms.Results The prevalence of perinatal depressive symptoms among our participants ranged from 21.2% to 24.0%. Repeated-measures ANOVA showed that during the perinatal period there was a significant tendency towards worse marital adjustment (F=33.031, p=0.000) and a slight but not significant reduction in depressive symptoms (F=1.883, p=0.153) among the participants. The cross-lagged model showed that maternal marital adjustment at T1 significantly and negatively predicted depressive symptoms at T2 (β=−0.165, p<0.001), and that depressive symptoms at T2 significantly and negatively predicted marital adjustment at T3 (β=−0.135, p<0.001). However, the predictive effects of depressive symptoms at T1 on marital adjustment at T2 and that of marital adjustment at T2 on depressive symptoms at T3 were not significant.Conclusion The prevalence of perinatal depressive symptoms ranged from 21.2% to 24.0% among the participants. During the perinatal period, the marital adjustment of women tended to be worse; however, there was no significant change in depressive symptoms. This study showed that better marital adjustment at T1 was a protective factor against maternal depressive symptoms at T2, and a higher level of depressive symptoms at T2 was a risk factor for worse marital adjustment at T3

Functional properties and adipogenesis inhibitory activity of protein hydrolysates from quinoa (Chenopodium quinoa Willd.)

The functional properties and adipogenesis inhibitory activity of quinoa protein hydrolysates, prepared using papain, pepsin, and pancreatin for 0, 30, 60, 90, and 120 min, were studied. For these three kinds of proteases, the solubility of the hydrolysates significantly increased with the increasing DH in pH range of 3–8, while the EAI and ESI of these hydrolysates significantly decreased during hydrolysis. The anti‐inflammatory activity of these protein hydrolysates was measured. All of these protein hydrolysates showed high anti‐inflammatory activity. However, there was no significant difference in anti‐inflammatory activity between protein hydrolysates and total protein from quinoa. These protein hydrolysates also inhibited lipid accumulation during differentiation within the range of concentrations of 0–1,600 μg/ml, which exerted no cytotoxicity toward 3T3‐L1 cells. The protein hydrolysates from quinoa prepared using pepsin for 120 min (PEP‐120) had the highest activity with an IC50 value of 786.58 μg/ml. Moreover, LC‐MS/MS analysis of PEP‐120 showed that five main bioactive peptides, which have been demonstrated to have ACE inhibitor, antioxidant, and antithrombotic activities, were present in PEP‐120. In addition, gene expression and Western blot analysis revealed that PEP‐120 suppressed the 3T3‐L1 cell differentiation through the peroxisome proliferator‐activated receptor γ (PPARγ) pathway

Exosome-mediated transfer of lncRNA PART1 induces gefitinib resistance in esophageal squamous cell carcinoma via functioning as a competing endogenous RNA

Abstract Background Currently, resistance to tyrosine kinase inhibitors, such as gefitinib, has become a major obstacle in improving the clinical outcome of patients with metastatic and advanced-stage esophageal squamous cell carcinoma (ESCC). While cell behavior can be modulated by long non-coding RNAs (lncRNAs), the roles of lncRNAs within extracellular vesicles (exosomes) are largely unknown. Therefore, we investigated the involvement and regulatory functions of potential lncRNAs enclosed in exosomes during formation of chemoresistance in human ESCC. Methods Gefitinib-resistant cell lines were established by continuously grafting TE1 and KYSE-450 cells into gefitinib-containing culture medium. LncRNA microarray assay followed by RT-qPCR were used to verify the differential expression of lncRNA Prostate Androgen-Regulated Transcript 1 (PART1) between gefitinib resistant and parental cell lines. RNA fluorescence in situ hybridization (FISH) was used to investigate whether extracellular PART1 could be incorporated into exosomes and transmitted to recipient cells. Subsequently, a series of in vitro assays and a xenograft tumor model were used to observe the functions of lncRNA PART1 in ESCC cells. A signal transduction reporter array, bioinformatics analysis, western blotting, and immunofluorescence were carried out to verify the regulation of PART1 and its downstream Bcl-2 signaling pathway. Results lncRNA PART1 was upregulated in gefitinib-resistant cells when compared to parental ESCC cells. It was found that STAT1 can bind to the promoter region of lncRNA PART1, resulting in its activation. Knockdown of lncRNA PART1 potently promoted the gefitinib-induced cell death, while elevated PART1 promoted gefitinib resistance by competitively binding to miR-129 to facilitate Bcl-2 expression in ESCC cells. In addition, extracellular PART1 could be incorporated into exosomes and transmitted to sensitive cells, thus disseminating gefitinib resistance. Clinically, high levels of serum lncRNA PART1 in exosome were associated with poor response to gefitinib treatment in ESCC patients. Conclusions LncRNA PART1 promotes gefitinib resistance by regulating miR-129/Bcl-2 pathway, and may serve as a therapeutic target for ESCC patients

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Despite the well-established role of quinoa protein as the source of antihypertensive peptides through in vitro enzymolysis, there is little evidence supporting the in vivo antihypertensive effect of intact quinoa protein. In this study, in vivo study on spontaneously hypertensive rats (SHRs) was conducted by administering quinoa protein for five weeks. Gastrointestinal content identification indicated that many promising precursors of bioactive peptides were released from quinoa protein under gastrointestinal processing. Quinoa protein administration on SHRs resulted in a significant decrease in blood pressure, a significant increase in alpha diversity, and microbial structure alternation towards that in non-hypertension rats. Furthermore, blood pressure was highly negatively correlated with the elevated abundance of genera in quinoa protein-treated SHRs, such as Turicibacter and Allobaculum. Interestingly, the fecal microbiota in quinoa protein-treated SHRs shared more features in the composition of genera with non-hypertension rats than that of the captopril-treated group. These results indicate that quinoa protein may serve as a potential candidate to lower blood pressure and ameliorate hypertension-related gut dysbiosis

Antihypertensive effect of quinoa protein under simulated gastrointestinal digestion and peptide characterization.

BACKGROUND: Quinoa protein is a potential source of bioactive peptides. Although some studies have demonstrated its angiotensin converting enzyme (ACE) inhibitory properties, research into its in vivo effect on blood-pressure regulation and peptide characterization remains limited. RESULTS: Quinoa protein hydrolyzate (QPH) was prepared by simulated gastrointestinal digestion. QPH lowered the systolic blood pressure (SBP) and diastolic blood pressure (DBP) in spontaneously hypertensive model rats (SHRs) from 2 h to10 h after oral administration, effectively controlling blood pressure in these SHRs. An in vitro study showed that QPH is capable of inhibiting ACE activity. This was attributed to the activity of a number of low-molecular-weight peptides. With relatively high scores predicted by PeptideRanker, three promising bioactive peptides, FHPFPR, NWFPLPR, and NIFRPF, were further studied and their ACE-inhibition effects were confirmed with IC(50) values of 34.92, 16.77, and 32.40 μM, respectively. A molecular docking study provided insights into the binding of ACE with peptides, and revealed that the presence of specific amino acids in the peptide sequence (Pro, Phe, and Arg at the C-terminal, and Asn at the N-terminal) could contribute to the interaction between ACE and peptides. CONCLUSION: These results demonstrated the potential of QPH for the management of hypertension, which indicates that it could be a good candidate for inclusion in functional foods to control high blood pressure. © 2020 Society of Chemical Industry