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By M. Ola

ISBN-10: 9535100440

ISBN-13: 9789535100447

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2007). Biochemical, spectral, electrophoretic, circular dichroism spectropolarimetric, and thermodynamic analyses confirmed that the structure and stability of HSA is significantly affected by glucose induced modification. , 2010). Ex vivo designed gluco-oxidative modified human serum albumin (RGHSA) were used as an antigen and the titres of antibodies against (RG-HSA-Abs) it were screened in both types of diabetic patients, as well as screening was also done in diabetic patients with complications like retinopathy, nephropathy and artherosclerosis (Table 1).

Schematic presentation of potential pathway leading to AGE formation. The abbreviations given above are represented as, GLO=glyoxal; MG=methylglyoxal; 3-DG=3deoxyglucosone; CML=carboxymethyl-lysine (Turk, 2001). , 2004). Some of the major AGEs are carboxymethyl lysine (CML) and pentosidine and also include many reactive intermediates or AGE-precursors such as 1- or 3deoxyglucosone, methylglyoxal (MG) and their derivatives. , 2004; Vlassara 2001). , 2002). , 1998). Retinal organ cultures show an increased glyoxal induced CML formation in association with increased apoptosis and cell death, restored by anti-AGE agents and antioxidants (Mamputu & Renier 2002).

At this stage, glycation becomes an autonomic process, which significantly accelerates the progress of the complication (Turk 2001). Immunoglobins are glycated differently according to their class. The glycation of immunoglobulin-M is twofold greater than that of immunoglobulin G, and can be related to Gluco-Oxidation of Proteins in Etiology of Diabetic Retinopathy 35 the difference in amino acid composition. Albumin can be glycated at multiple sites. , 1997). , 1978). , 1987; Bryszewska & Szosland 1988).

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Diabetic Retinopathy by M. Ola

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