Fine characterization of glucosylated human IgG by biochemical and biophysical methods

Arfat, Mir Yasir; Ashraf, Jalaluddin M.; Arif, Zarina; Moinuddin, Mohammed; Alam, Khursheed

doi:10.1016/j.ijbiomac.2014.05.069

Cited by 42 publications

(31 citation statements)

References 37 publications

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“…During diabetes, persistent hyperglycemia leads to nonenzymatic glycation of various proteins such as hemoglobin, proteins of erythrocyte membrane, insulin, human serum albumin (HSA), high and low density lipoproteins, IgG, IgM, collagen and histones. [ 3 4 ] Proteins are glycated, when glucose is chemically bound to amino groups of proteins without the help of enzyme, which causes many structural and conformational changes in protein, and proceeds to various micro-macro complications in diabetic patients. [ 5 ] A strong link between Amadori albumin and diabetes specific complications have been demonstrated by studies in humans,[ 6 ] animals[ 7 ] and cell culture.…”

Section: Introductionmentioning

confidence: 99%

Amadori albumin in diabetic nephropathy

Neelofar

Ahmad

2015

Indian J Endocr Metab

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Nonenzymatic glycation of macromolecules in diabetes mellitus (DM) is accelerated due to persistent hyperglycemia. Reducing sugar such as glucose reacts non enzymatically with free €-amino groups of proteins through series of reactions forming Schiff bases. These bases are converted into Amadori product and further into AGEs. Non enzymatic glycation has the potential to alter the biological, structural and functional properties of macromolecules both in vitro and in vivo. Studies have suggested that amadori as well as AGEs are involved in the micro-macro vascular complications in DM, but most studies have focused on the role of AGEs in vascular complications of diabetes. Recently putative AGE-induced patho-physiology has shifted attention from the possible role of amadori-modified proteins, the predominant form of the glycated proteins in the development of the diabetic complications. Human serum albumin (HSA), the most abundant protein in circulation contains 59 lysine and 23 arginine residues that could, in theory be involved in glycation. Albumin has dual nature, first as a marker of intermediate glycation and second as a causative agent of the damage of tissues. Among the blood proteins, hemoglobin and albumin are the most common proteins that are glycated. HSA with a shorter half life than RBC, appears to be an alternative marker of glycemic control as it can indicate blood glucose status over a short period (2-3 weeks) and being unaffected by RBCs life span and variant haemoglobin, anemia etc which however, affect HbA1c. On the other hand, Amadori albumin may accumulate in the body tissues of the diabetic patients and participate in secondary complications. Amadori-albumin has potential role in diabetic glomerulosclerosis due to long term hyperglycaemia and plays an important role in the pathogenesis of diabetic nephropathy. This review is an approach to compile both the nature of glycated albumin as a damaging agent of tissues and as an intermediate diagnostic marker and its potential role in diabetic nephropathy.

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Section: Introductionmentioning

confidence: 99%

Amadori albumin in diabetic nephropathy

Neelofar

Ahmad

2015

Indian J Endocr Metab

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“…DM results either due to lack of insulin or because of the presence of factors that oppose the action of insulin. It is well recognized that long-term exposure of macromolecules during hyperglycemia results in excessive nonenzymatic glycation and formation of advanced glycation end products (AGEs) [2][3][4][5][6]. Furthermore, chronic hyperglycemia may accelerate AGE formation in different tissues [7].…”

Section: Introductionmentioning

confidence: 99%

A clinical correlation of anti-DNA-AGE autoantibodies in type 2 diabetes mellitus with disease duration

Ashraf

Arfat

Arif³

et al. 2015

Cellular Immunology

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“…These amides I and amide II bands are also present in the GNP-TA-IgG bio-nanostructure at 1640 and 1549 cm −1 14. Thus, for the GNP-TA-IgG sample, the disappearance of the citrate ions attributed IR bands, corroborated with the appearance of the IgG amide bands confirms the successful functionalization of gold nanoparticles with the antibody.…”

Section: Resultsmentioning

confidence: 54%

Selective in vitro photothermal nano-therapy of MRSA infections mediated by IgG conjugated gold nanoparticles

Mocan

Matea

Tabaran

et al. 2016

Sci Rep

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There are serious systemic infections associated with methicillin-resistant Staphylococcus aureus (MRSA) and several other types of bacteria leading to the deaths of millions of people globally. This type of mortality is generally caused by the increasing number of antibiotic-resistant organisms, a consequence of evolution via natural selection. After the synthesis of gold nanoparticles (GNPs) by wet chemistry, bio-functionalization with IgG molecules was performed. Following administration of IgG-GNPs to MRSA cultures at various concentrations and various incubation time laser irradiation was performed. To assess the selectivity and specificity of the proposed treatment the following methods were used: flow cytometry, contrast phase microscopy, and by fluorescence microscopy. The results in our study indicate that following administration of IgG-GNPs biomolecule an extended and selective bacterial death occurs following laser irradiation in a dose dependent manner. Therefore, the new findings might impel studies on these antibacterial nanomaterials and their biological and medical applications.

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Fine characterization of glucosylated human IgG by biochemical and biophysical methods

Cited by 42 publications

References 37 publications

Amadori albumin in diabetic nephropathy

Amadori albumin in diabetic nephropathy

A clinical correlation of anti-DNA-AGE autoantibodies in type 2 diabetes mellitus with disease duration

Selective in vitro photothermal nano-therapy of MRSA infections mediated by IgG conjugated gold nanoparticles

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