Journal of Clinical and Cellular Immunology
Open Access
ISSN: 2155-9899
+44 1223 790975
ISSN: 2155-9899
+44 1223 790975
Ishrat Jahan Saifi
Aligarh Muslim University, India
Posters & Accepted Abstracts: J Clin Cell Immunol
Diabetes mellitus is a group of disease characterized by high level of blood glucose, resulting due to insulin production, insulin action or both. As diabetes mellitus (DM) becomes epidemic its prevalence increases day by day, so there is a need to find out the actual cause of DM. Existing literature and research describe that glycation of protein is very important as well as a harmful process, which may lead to development of DM in human body. Human Serum Albumin (HSA) is the most abundant protein in blood and it is highly prone to glycation by the reducing sugars. 2-deoxy- D-ribose (dRib) is a highly reactive reducing sugar which is produced in cells as a product of the enzyme thymidine phosphorylase. It is generated during the degradation of DNA in human body. It may cause glycation in HSA rapidly and is involved in the development of DM. In present study, we did an invitro glycation of HSA with 2- deoxy-D-ribose and found that dRib glycated HSA rapidly within 24 hours at certain concentration. UVSpectroscopy, Flourescence spectroscopy, Fourier transform infrared spectroscopy (FTIR) and Circular Dichroism (CD) technique have been done to determine the structural changes in HSA upon glycation. dRib modified HSA was also used to detect the autoantibodies in diabetes patients. Enhanced binding of dRib modified HSA with autoantibodies was observed compared to the native HSA. Thus it may be concluded that dRib is a potent enough to cause structural changes as well as generation of neoepitopes on the protein which may induce autoantibodies in diabetic patients and might play a role in the onset and progression of diabetes.
Email: ishratjahan19feb@gmail.com