Antibodies against Gluco-Oxidatively Modified Human Serum Albumin Detected in Diabetes-Associated Complications

Khan, Mohd Wajid Ali; Qadrie, Zulfkar Latief; Khan, Wahid Ali

doi:10.1159/000312639

Cited by 27 publications

(29 citation statements)

References 50 publications

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“…Glycated HSA causes autoantibody production and has been related to autoimmune disorder. Beside this, glycated HSA has been associated with nephropathy and HSA glycation has also been linked to changes in the binding of HSA to several drugs such as phenytoin, salicylate, ibuprofen, phenylbutazone and warfarin and small solutes in the body [19,20]. Glycation of HSA can generate thermodynamically more stable high-molecular weight aggregates having a remarkably increased beta-sheet structure than its non-glycated form.…”

mentioning

confidence: 99%

Papaverine increases human serum albumin glycation

Ahmadzadeh

2014

J Biol Phys

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Glycation is a non-enzymatic reaction that is initiated by the primary addition of sugars to amino groups of proteins. In the early phase of glycation, the synthesis of intermediates leads to formation of Amadori compounds. In the last phase, advanced glycation end products (AGE) are irreversibly formed following a complex cascade of reactions. It has recently been shown that glycation also affects diabetes-related complications and Alzheimer's disease. In this study, human serum albumin at a concentration of 10 mg/ml was incubated in PBS with 40 mM of glucose and in different concentrations of papaverine (25, 100, 250, 500 µM) for 42 days at 37 • C. HSA with no additives as well as with glucose 40 mM were incubated as a control and as a glycated sample, respectively. Following the incubation, the samples were prepared for circular dichroism, fluorescence and absorbance techniques. The results showed that in presence of papaverine and glucose, the glycation of HSA increased notably compared with the glycated sample. In conclusion, in this work, we showed that papaverine affects HSA and increases its glycation level.

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confidence: 99%

Papaverine increases human serum albumin glycation

Ahmadzadeh

2014

J Biol Phys

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“…White female New Zealand rabbits were immunized with N-HSA and G-HSA as previously described [30]. Briefly, rabbits (2 each for N-HSA and G-HSA) were immunized intramuscularly at multiple sites with 100 mg of antigen emulsified with an equal volume of Freund's complete adjuvant.…”

Section: Immunization Schedulementioning

confidence: 99%

Depression and Smoking Augment the Production of Circulating Autoantibodies against Glycated HSA in Rheumatoid Arthritis Patients

Alouffi

Sherwani

Al-Mogbel

et al. 2018

Int Arch Allergy Immunol

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Background: Depression and smoking contribute to the prognosis of autoimmune rheumatoid arthritis (RA). Advanced glycation end products (AGEs) are also detected in RA patients. This study correlates RA in patients with various levels of depression and a history of smoking through the detection of antibodies against AGEs of proteins. Methods: Sixty RA subjects were selected and divided into 4 groups based on their levels of depression and smoking habits. The division was as follows: group I consisted of RA patients classified as depressed (RA-D); group II consisted of RA patients with a history of smoking (RA-S); group III consisted of RA patients suffering from depression who were also smokers (RA-DS); and group IV consisted of patients with RA alone (RA-A), i.e., not depressed and non-smokers. In vitro human serum albumin (HSA) was modified by glucose, and the modifications were studied by biochemical and biophysical techniques. Glycated (G)-HSA was used as an antigen, and autoantibodies against G-HSA (G-HSA-Abs) were screened in serum samples of different groups of RA subjects. Oxidative stress levels in all patients and healthy individuals were analyzed by protein-bound carbonyl content estimations. Results: Significant biochemical and biophysical changes were detected in G-HSA when compared to native (N)-HSA. All patients and control subjects were screened for circulating G-HSA-Abs and N-HSA-Abs. From the cohort of different samples, serum autoantibodies from RA-DS showed a high recognition of G-HSA-Abs titres compared to RA-D or RA-S. RA-A exhibited the least binding of circulating G-HSA-Abs of all the groups. The oxidative stress marker, the carbonyl content also exhibited highest levels in RA-DS, followed by RA-D and RA-S. Band shift assay showed the highest titres of immunoglobulin G in the serum samples of RA-DS. Conclusions: Smoking and concomitant depression in RA subjects may lead to enhanced oxidative stress levels responsible for the gradual formation and/or exposing of cryptic epitopes on HSA that induce the production of G-HSA-Abs. Hence, we postulate that by reducing depression and corresponding oxidative stress, it may be possible to control or limit the severity of the precipitation of RA disease activity and improve prognosis.

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“…Elevated levels of autoantibodies against AGEs were observed in the sera of diabetic patients (7,8). Circulating autoantibodies showed higher recognition of gluco-oxidatively modified human serum albumin (HSA) in patients with diabetic complications (9). The autoantibodies form complexes with their antigens and are referred as circulating immune complexes (CICs), which were found to affect quantification of AGE antibody titer in vivo (10).…”

Section: Formation Of Advanced Glycation End Products (Ages)mentioning

confidence: 99%

Proteomic Insight Reveals Elevated Levels of Albumin in Circulating Immune Complexes in Diabetic Plasma

Bhat

Jagadeeshaprasad

Patil

et al. 2016

Molecular & Cellular Proteomics

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A Hyperglycemic condition in diabetes promotes formation of advanced glycation end products, which are known to elicit immune response and form complexes with immunoglobulins called circulating immune complexes. To investigate the involvement of advanced glycation end product (AGE)-modified proteins in the elicitation of an immune response, circulating immune complexes were isolated and proteins associated were identified and characterized. Label-free-based mass spectrometric analysis of circulating immune complexes in clinical plasma of prediabetic, newly diagnosed diabetes, and diabetic microalbuminurea revealed elevated levels of serum albumin in the circulating immune complexes, which were also observed to be AGE modified. Further, to examine the role of glycation, circulating immune complexes were analyzed in the streptozotocin-induced diabetic mice treated with or without aminoguanidine, a prototype glycation inhibitor. Mass spectrometric analysis of circulating immune complexes showed elevated levels of serum albumin in plasma from diabetic mice over that of control animals. Aminoguanidine-treated diabetic mice displayed decreased AGE modification of plasma albumin, accompanied by a reduced level of albumin in the circulating immune complexes. In addition, elevated levels of proinflammatory cytokines such as IL-1b, IL-2, and TNF-alpha were observed in diabetes, which were reduced with aminoguanidine treatment, suggesting the involvement of glycation in the immune response.

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Antibodies against Gluco-Oxidatively Modified Human Serum Albumin Detected in Diabetes-Associated Complications

Cited by 27 publications

References 50 publications

Papaverine increases human serum albumin glycation

Papaverine increases human serum albumin glycation

Depression and Smoking Augment the Production of Circulating Autoantibodies against Glycated HSA in Rheumatoid Arthritis Patients

Proteomic Insight Reveals Elevated Levels of Albumin in Circulating Immune Complexes in Diabetic Plasma

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