Effects of Succinate-Containing Preparation on Characteristics of Rat Erythrocytes in Exhaustive Swimming with a Load

Author(s):  
N. P. Mongalev ◽  
L. Yu. Rubtsova ◽  
N. A. Vakhnina ◽  
V. D. Shadrina ◽  
O. N. Chupakhin ◽  
...  
Keyword(s):  
1972 ◽  
Vol 247 (13) ◽  
pp. 4299-4304
Author(s):  
Adriana L. Goldemberg ◽  
Ricardo N. Farías ◽  
Raul E. Trucco
Keyword(s):  

1992 ◽  
Vol 284 (1) ◽  
pp. 169-176 ◽  
Author(s):  
T R Hughes ◽  
S J Piddlesden ◽  
J D Williams ◽  
R A Harrison ◽  
B P Morgan

The membrane attack complex (MAC) of complement in humans is regulated by several membrane-bound proteins; however, no such proteins have so far been described in other species. Here we report the isolation and characterization of a rat erythrocyte membrane glycoprotein of molecular mass 21 kDa which inserts into cell membranes and is a potent inhibitor of the rat MAC. This protein, here called rat inhibitory protein (RIP), was first partially purified by column chromatography from a butanol extract of rat erythrocyte membranes. Monoclonal antibodies (Mabs) were raised against RIP and used for its affinity purification. Affinity-purified RIP was shown to inhibit in a dose-dependent manner the cobra venom factor (CVF)-mediated ‘reactive’ lysis of guinea pig erythrocytes by rat complement. Conversely, the anti-RIP MAbs 6D1 and TH9 were shown to markedly enhance the CVF-mediated lysis of rat erythrocytes by rat complement. RIP acted late in the assembly of the MAC (at or after the C5b-8 stage) and was releasable from the membranes of rat erythrocytes by phosphatidylinositol-specific phospholipase C. These features, together with its size, deglycosylation pattern and N-terminal amino acid sequence, lead us to conclude that RIP is the rat homologue of the human MAC-inhibitory protein CD59 antigen.


1990 ◽  
Vol 5 (4) ◽  
pp. 221-227 ◽  
Author(s):  
Mohammed Y. H. Farooqui ◽  
Mohammad M. Mumtaz ◽  
Burhan I. Ghanayem ◽  
Ahmed E. Ahmed

2013 ◽  
Vol 64 (4) ◽  
pp. 553-559 ◽  
Author(s):  
Seyed Fazel Nabavi ◽  
Solomon Habtemariam ◽  
Antoni Sureda ◽  
Akbar Hajizadeh Moghaddam ◽  
Maria Daglia ◽  
...  

Abstract Gallic acid has been identified as an antioxidant component of the edible and medicinal plant Peltiphyllum peltatum. The present study examined its potential protective role against sodium fluoride (NaF)-induced oxidative stress in rat erythrocytes. Oxidative stress was induced by NaF administration through drinking water (1030.675 mg m-3 for one week). Gallic acid at 10 mg kg-1 and 20 mg kg-1 and vitamin C for positive controls (10 mg kg-1) were administered daily intraperitoneally for one week prior to NaF administration. Thiobarbituric acid reactive substances, antioxidant enzyme activities (superoxide dismutase and catalase), and the level of reduced glutathione were evaluated in rat erythrocytes. Lipid peroxidation in NaF-exposed rats significantly increased (by 88.8 %) when compared to the control group (p<0.05). Pre-treatment with gallic acid suppressed lipid peroxidation in erythrocytes in a dose-dependent manner. Catalase and superoxide dismutase enzyme activities and glutathione levels were reduced by NaF intoxication by 54.4 %, 63.69 %, and 42 % (p<0.001; vs. untreated control group), respectively. Pre-treatment with gallic acid or vitamin C significantly attenuated the deleterious effects. Gallic acid isolated from Peltiphyllum peltatum and vitamin C mitigated the NaF-induced oxidative stress in rat erythrocytes.


1994 ◽  
Vol 47 (2) ◽  
pp. 309-316 ◽  
Author(s):  
Jeannette Vásquez-Vivar ◽  
Ohara Augusto

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