Journal of Alzheimers Disease & Parkinsonism
Open Access

Abstract

Accumulation of Serum amyloid A and fibrillar form is strongly associated with Chronic inflammatory disease. Cell membrane binding study is especially important in relation to the activity of membrane proteins, because losing the activity of such systems will ultimately lead to malfunction or death of the cell. Serum amyloid Afibrils species are potent neurotoxins, however the molecular mechanism responsible for amyloid toxicity is still unknown. The interactions of Serum Amyloid a (SAA) and Serum Amyloid aprotofibrils with Neuro 2a cells of the mouse are dealt with in detail to study the binding of SAA protofibrils in various conditions. The FACScan and MTT assay results have shown the SAA and SAA fibrils binding and cell toxicity with the Neuro 2a cells with different concentrations of Serum amyloid P component and Amyloid enhancing factor. Specifically, interaction of serum amyloid A fibrils with a cell surface binding site/receptor might alter the local environment to cause cellular dysfunction and to be more favorable for amyloid formation. Previous study have shown RAGE (receptor for advanced glycationend products) a polyvalent receptor in the immunoglobulin super family has been implicated in binding with the isoform of SAA (SAA1.1) which has the highest fibirillogenic property. In the present study, concluding the SAA fibrils more binding and cell cytotoxicity than SAA protein.

Biography

Asokan Chinnasamy has completed his PhD at the age of 27 years from University of Madras and postdoctoral studies from Columbia University. USA. He is the Associate Professor, Department of Biochemistry, Sokoto State University, Sokoto. Nigeria. He has published more than 36 papers in reputed journals and has been serving as an editorial board member of repute.

Email: asokan_74@hotmail.com