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• W2281780141 abstract "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 A fibrils 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 A protofibrils 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. 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 glycation endproducts) 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." @default.
• W2281780141 created "2016-06-24" @default.
• W2281780141 creator A5029798236 @default.
• W2281780141 date "2015-09-26" @default.
• W2281780141 modified "2023-09-23" @default.
• W2281780141 title "IN-VITRO Interaction of Soluble and Amyloid Form of Serum Amyloid a Protein to NEURO 2A CELLS" @default.
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