Stimulating Effect of the Water-Soluble Fraction from Brown Algae Fucus vesiculosus Extract on Cell Proliferation in the Tissue Culture of Young and Old Rats

2020 ◽  
Vol 10 (3) ◽  
pp. 282-286
Author(s):  
N. I. Chalisova ◽  
G. A. Rizhak ◽  
M. A. Zayitseva ◽  
M. L. Alexandrova ◽  
A. A. Krasnova ◽  
...  
Open Medicine ◽  
2016 ◽  
Vol 11 (1) ◽  
pp. 183-189 ◽  
Author(s):  
Yosuke Nakazawa ◽  
Mikako Oka ◽  
Hiroomi Tamura ◽  
Makoto Takehana

AbstractBackground. Chaperone activity of α-crystallin in the lens works to prevent protein aggregation and is important to maintain the lens transparency. This study evaluated the effect of hesperetin on lens chaperone activity in selenite-induced cataracts. Methodology. Thirteen-day-old rats were divided into four groups. Animals were given hesperetin (groups G2 and G4) or vehicle (G1 and G3) on Days 0, 1, and 2. Rats in G3 and G4 were administered selenite subcutaneously 4 hours after the first hesperetin injection. On Days 2, 4, and 6, cataract grades were evaluated using slit-lamp biomicroscopy. The amount of a-crystallin and chaperone activity in water-soluble fraction were measured after animals sacrificed. Results. G3 on day 4 had developed significant cataract, as an average cataract grading of 4.6 ± 0.2. In contrast, G4 had less severe central opacities and lower stage cataracts than G3, as an average cataract grading of 2.4 ± 0.4. The a-crystallin levels in G3 lenses were lower than in G1, but the same as G4. Additionally, chaperone activity was weaker in G3 lenses than G1, but the same as in G4. Conclusions. Our results suggest that hesperetin can prevent the decreasing lens chaperone activity and a-crystallin water solubility by administered of selenite.


2014 ◽  
Vol 91 (5) ◽  
pp. 473-481 ◽  
Author(s):  
Guiai Jiao ◽  
Xiangjin Wei ◽  
Gaoneng Shao ◽  
Lihong Xie ◽  
Zhonghua Sheng ◽  
...  

1957 ◽  
Vol 35 (4) ◽  
pp. 241-250 ◽  
Author(s):  
W. G. Martin ◽  
J. E. Vandegaer ◽  
W. H. Cook

Livetin, the major water-soluble protein of hen egg yolk, was found to contain three major components having mobilities of −6.3, −3.8, and −2.1 cm.2 sec.−1 volt−1 at pH 8, µ 0.1, and these have been designated α-, β-, and γ-livetin respectively. The α- and β-livetins were separated and purified electrophoretically after removal of γ-livetin by precipitation from 37% saturated ammonium sulphate or 20% isopropanol. The α-, β-, and mixed livetins resembled pseudoglobulins in solubility but γ-livetin was unstable and this loss of solubility has, so far, prevented its characterization. Molecular weights determined by light scattering, osmotic pressure, and Archibald sedimentation procedure yielded respectively: 8.7, 7.8, and 6.7 × 104 for α-livetin, and 4.8, 5.0, and4.5 × 104 for β-livetin. Under suitable conditions of sedimentation and electrophoresis, egg yolk has been shown to contain three components having the same behavior as the three livetins of the water-soluble fraction.


Chemosphere ◽  
2010 ◽  
Vol 78 (11) ◽  
pp. 1301-1312 ◽  
Author(s):  
S.M. Rodrigues ◽  
B. Henriques ◽  
J. Coimbra ◽  
E. Ferreira da Silva ◽  
M.E. Pereira ◽  
...  

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