Gholamreza Asadikaram; Majid Asiabanha; Ahmadreza Sayadi; Abdollah Jafarzadeh; Gholamhossein Hassanshahi
Volume 7, Issue 3 , September 2010, , Pages 186-192
Abstract
Background: Several cells of immune system such as regulatory T cells and macrophages secrete transforming growth factor-β (TGF-β) in response to different stimuli. This cytokine has inhibitory effect on immune system and diminished production of this cytokine is associated with autoimmune ...
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Background: Several cells of immune system such as regulatory T cells and macrophages secrete transforming growth factor-β (TGF-β) in response to different stimuli. This cytokine has inhibitory effect on immune system and diminished production of this cytokine is associated with autoimmune disorders. Objective: The aim of this study was to evaluate the influence of opium addiction on serum level of TGF-β in male and female diabetic and non-diabetic Wistar rats. Methods: This experimental study was performed on normal, opium addicted, diabetic and addicted-diabetic male and female rats. Serum level of TGF-β was measured by ELISA. Results: The results of our study indicated that the mean serum level of TGF-β in female addicted rats was significantly increased compared to control group (p<0.004). Conversely, in male addicted rats the mean serum level of TGF-β was lower compared with control (p<0.065). Conclusion: Our results suggest that opium and its derivatives have differential inductive effects on the cytokine expression in male and female rats.
Mohammad Taghi Goodarzi; Safyieh Ghahramany; Mohammad Hossien Mirmomeni
Volume 2, Issue 1 , March 2005, , Pages 36-42
Abstract
Background: Glycation of proteins is a non-enzymatic spontaneous process that occurs in diabetes mellitus and aging, altering the structure and function of proteins. IgG undergoes glycation leading to changes in its reactivity to antigen and fixation of complement. Objective: This study aimed ...
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Background: Glycation of proteins is a non-enzymatic spontaneous process that occurs in diabetes mellitus and aging, altering the structure and function of proteins. IgG undergoes glycation leading to changes in its reactivity to antigen and fixation of complement. Objective: This study aimed at revealing the effect of glycation on the interaction of IgG with anti-IgG using electroimmunoassay. Methods: Purified human IgG was glycated with different concentrations of glucose and different periods of treatment. Glycation was measured using thiobarbituric acid reaction. Glycated and non-glycated IgG were subjected to electroimmunoassay, and the height of the precipitated rings were measured and compared. Results: The results showed that IgG was glycated in vitro and the level of glycation was dependent on the glucose concentration and duration of treatment with glucose. The height of glycated IgG peaks formed in the electroimmunoassay was significantly lower than those of nonglycated IgG ( p < 0.01). Conclusion: The results indicated that in vitro glycation of IgG leads to structural changes altering its mobility in the electroimmunoassay. Moreover, it suggests that this alteration may cause the weakness of its interaction with anti-IgG. This phenomenon may play a role in the susceptibility of diabetic patients to infection.
