In Vitro antioxidative activity of pumpkin seed (Cucurbita pepo) protein isolate and itsIn Vivo effect on alanine transaminase and aspartate transaminase in acetaminophen-induced liver injury in low protein fed rats

2006 ◽  
Vol 20 (9) ◽  
pp. 780-783 ◽  
Author(s):  
C. Z. Nkosi ◽  
A. R. Opoku ◽  
S. E. Terblanche
Keyword(s):  
Liver Injury ◽  
Cucurbita Pepo ◽  
Antioxidative Activity ◽  
Protein Isolate ◽  
Alanine Transaminase ◽  
Aspartate Transaminase ◽  
Pumpkin Seed ◽  
Low Protein

Anti-hepatotoxic effects of 3,4-methylenedioxyphenol and N-acetylcysteine in acutely acetaminophen-overdosed mice

2011 ◽  
Vol 30 (10) ◽  
pp. 1609-1615 ◽  
Author(s):  
Victor Raj Mohan Chandrasekaran ◽  
Se-Ping Chien ◽  
Dur-Zong Hsu ◽  
Ming-Yie Liu
Keyword(s):  
Lipid Peroxidation ◽  
Liver Injury ◽  
Protective Effect ◽  
Liver Damage ◽  
Alanine Transaminase ◽  
Aspartate Transaminase ◽  
Hepatic Glutathione ◽  
Hepatotoxic Effect

3,4-Methylenedioxyphenol (sesamol) is effective against acetaminophen-induced liver injury in rats. Whether sesamol’s anti-hepatotoxic effect is comparable to that of N-acetylcysteine has never been studied. We investigated the anti-hepatotoxic effects of sesamol and N-acetylcysteine on acetaminophen-induced hepatotoxicity in mice. Equimolar doses (1 mmol/kg) of sesamol and N-acetylcysteine significantly inhibited acetaminophen (300 mg/kg)-increased serum aspartate transaminase and alanine transaminase levels 6 h post-administration. Sesamol and N-acetylcysteine maintained hepatic glutathione levels and inhibited lipid peroxidation. Moreover, the combination of sesamol and N-acetylcysteine antagonistically inhibited sesamol’s protection against acetaminophen-induced liver injury. We conclude that the protective effect of sesamol against acetaminophen-induced liver damage is comparable to that of N-acetylcysteine by maintaining glutathione levels and inhibiting lipid peroxidation in mice.

scholarly journals CXCL6 promotes human hepatocyte proliferation through the CXCR1–NFκB pathway and inhibits collagen I secretion by hepatic stellate cells

2016 ◽  
Vol 94 (3) ◽  
pp. 229-235 ◽  
Author(s):  
Zhenghong Li ◽  
Qidi Zhang ◽  
Qingqing Zhang ◽  
Mingyi Xu ◽  
Ying Qu ◽  
...  
Keyword(s):  
Hepatic Stellate Cells ◽  
Stellate Cells ◽  
Alanine Transaminase ◽  
Collagen I ◽  
Hepatocyte Proliferation ◽  
Aspartate Transaminase ◽  
Nfκb Pathway ◽  
L02 Cells

Hepatocyte proliferation and collagen I (COLI) secretion are important processes during liver regeneration. This study aimed to investigate the role of CXCL6 in hepatocyte proliferation and COLI secretion. Serum CXCL6 levels in patients with chronic hepatitis B (CHB) were examined and the effects of CXCL6 on the proliferation of L02 hepatocytes and the secretion of COLI from LX2 human hepatic stellate cells were evaluated. We found that serum CXCL6 levels increased gradually with disease progression of CHB, and there was positive correlation between serum CXCL6 level and alanine transaminase (ALT) and aspartate transaminase (AST). In vitro, CXCL6 promoted L02 proliferation but this was blocked upon CXCR1 knockdown. The level of phospho-IκBα was upregulated by CXCL6 but downregulated by CXCR1 siRNA in L02 cells. CXCL6 inhibited the secretion of COLI by LX2 cells, dependent on CXCR1 and CXCR2. Taken together, these data suggest that increased expression of CXCL6 during CHB could promote hepatocyte proliferation through the CXCR1–NFκB pathway and inhibit the secretion of COLI by hepatic stellate cells.

scholarly journals Functional properties of pumpkin (Cucurbita pepo) seed protein isolate and hydrolysate

2016 ◽  
Vol 81 (1) ◽  
pp. 35-46 ◽  
Author(s):  
Sandra Bucko ◽  
Jaroslav Katona ◽  
Ljiljana Popovic ◽  
Zuzana Vastag ◽  
Lidija Petrovic
Keyword(s):  
Ionic Strength ◽  
Cucurbita Pepo ◽  
Seed Protein ◽  
Protein Hydrolysate ◽  
Protein Isolate ◽  
Emulsifying Properties ◽  
Protein Solution ◽  
Pumpkin Seed ◽  
Solution Interface ◽  
Oil In Water

Pumpkin seed protein isolate (PSPI) was enzymatically hydrolysed by pepsin to obtain pumpkin seed protein hydrolysate, PSPH. Investigation on solubility, interfacial and emulsifying properties of both PSPI and PSPH was conducted under different conditions of pH (3-8) and ionic strength (0-1 mol/dm3 NaCl). PSPI had the lowest solubility, i.e. isoelectric point (pI), at pH 5. PSPH had higher solubility than PSPI over whole range of pH and ionic strengths tested. Decrease in surface and interfacial tension evidenced that both PSPI and PSPH adsorb at air/protein solution and oil/protein solution interface. Emulsions (20 % oil in water) stabilized by 1 g/100cm3 PSPI or PSPH solution were prepared at pH 3, 5 and 8 and ionic strength of 0 and 0.5 mol/dm3 NaCl. PSPH stabilized emulsions from coalescence at all pH and ionic strengths tested. PSPI was able to stabilize emulsions at pH 3 and 0 mol/dm3 NaCl, and at pH 8 regardless of ionic strength, while emulsions at pH 5 and both 0 and 0.5 mol/dm3 NaCl and at pH 3 when ionic strength was increased separated to oil and serum layer immediately after preparation. All emulsions were susceptible to creaming instability.

scholarly journals An investigation on the influence of pH and ionic strength on the adsorption and interfacial dilatational properties at the oil-water interface of pumpkin (Cucurbita pepo) seed protein hydrolysate

2018 ◽  
Vol 83 (7-8) ◽  
pp. 847-861
Author(s):  
Sandra Bucko ◽  
Jaroslav Katona ◽  
Lidija Petrovic ◽  
Jelena Milinkovic ◽  
Jadranka Fraj ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Rate Constant ◽  
Cucurbita Pepo ◽  
Seed Protein ◽  
Protein Hydrolysate ◽  
Protein Isolate ◽  
Pumpkin Seed ◽  
Interfacial Pressure ◽  
Oscillation Frequencies ◽  
Influence Of Ph

Pumpkin (Cucurbita pepo) seed protein hydrolysate (PSPH) was obtained by enzymatic hydrolysis of pumpkin seed protein isolate using pepsin. Influence of pH (3, 5 and 8) and ionic strength, Ic (0?1 mol dm-3), on the adsorption kinetics of PSPH (diffusion rate constant, kdiff, and adsorption rate constant, kads), interfacial pressure (?) and interfacial dilatational properties (dilatational elasticity, E?, and viscosity, E?) of the oil?PSPH solution interfaces was investigated at different PSPH concentrations (c = 0.0014?14 g dm-3). It was found that PSPH adsorbs to the interface at c ? 0.0014 g dm-3, regardless of pH and ionic strength, as evidenced by the increase in interfacial pressure. The kdiff and kads value were found to be the highest at pH 3 and the lowest at pH 5 at the corresponding concentrations. The dilatational properties of the interfaces, which were investigated at different oscillation frequencies, ?, 0.01?0.2 Hz, showed that the E? of the oil?PSPH solution interfaces is much higher than its E?. Moreover, E? increases with increasing PSPH concentration at pH 5 and 8, and with increasing Ic, regardless of the pH, while E? changes only minimally.

Chemical and Nutritional Evaluation of Pumpkin (Cucurbita pepo) Seed Proteins

2019 ◽  
pp. 1-11 ◽  
Author(s):  
Adanma C. Innocent-Ukachi
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Chemical Properties ◽  
Seed Proteins ◽  
Protein Digestibility ◽  
Amino Acid Profile ◽  
Protein Isolate ◽  
Pumpkin Seed ◽  
Chemical Score

Chemical and nutritional properties of pumpkin (Curcubita pepo) seed proteins were studied. The seed was processed into defatted flour (CPF) which was further processed into Curcubita protein concentrate (CPC) and Curcubita protein isolate (CPI) by alkaline water/isoelectric precipitation. Chemical properties of the protein products were determined using standard methods of analysis. The amino acid profile was determined by an automated Technicon® liquid chromatography system. Protein digestibility was assessed in-vitro (IVPD) using trypsin-pepsin enzyme method while biological values were determined on the basis of their amino acid profile. Protein efficiency ratio (PER) was estimated according to a standard proposed regression equation. The seed proteins demonstrated high levels of crude protein (CPC=69.98% and CPI=74.15%), vitamin C (CPC=43.46 and CPI=52.36 mg/ml) and vitamin A (CPC=100.56 and CPI= 63.43 I.U/g) with low levels of thiamin and riboflavin. Both proteins showed low and similar (p>0.05) levels of sodium (0.14-0.18%), calcium (0.86-1.02%), magnesium (0.53-0.58%) and phosphorus (0.09-0.11%). Percentage ratios of essential to total amino acids obtained for CPC and CPI (44.24% and 45.50%, respectively) were greater than 36% which is considered adequate for an ideal protein. Protein biological values obtained for CPC and CPI respectively were: 95% and 53% (chemical score), 2.80 and 1.56 (PER} and 70.10% and 51.28% (essential amino acid index). CPC showed a better digestibility than CPI with IVPD value of 56.88%. Threonine and lysine were the most limiting amino acids in both protein products. All anti-nutrients evaluated were low and below allowable limits. In conclusion pumpkin seed proteins showed good biological values and could be used to improve the quality of other plant proteins or as a possible replacement for animal proteins in conventional foods.

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