Asokan Chinnasamy
Sokoto State University, Nigeria
Title: Interaction of soluble and Amyloid form of Serum Amyloid a protein to Neuro 2a Cells
Biography
Biography: Asokan Chinnasamy
Abstract
Accumulation of Serum amyloid A and fi brillar form is strongly associated with Chronic infl ammatory 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 Afi brils species are potent neurotoxins, however the molecular mechanism responsible for amyloid toxicity is still unknown. Th e interactions of Serum Amyloid a (SAA) and Serum Amyloid aprotofi brils with Neuro 2a cells of the mouse are dealt with in detail to study the binding of SAA protofi brils in various conditions. Th e FACScan and MTT assay results have shown the SAA and SAA fi brils binding and cell toxicity with the Neuro 2a cells with diff erent concentrations of Serum amyloid P component and Amyloid enhancing factor. Specifi cally, interaction of serum amyloid A fi brils 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 fi birillogenic property. In the present study, concluding the SAA fi brils more binding and cell cytotoxicity than SAA protein.