Biochemistry & Analytical Biochemistry

In vitro interaction of soluble and amyloid form of serum amyloid protein with amyloid P component to hepta 1-6 cells

International Conference on Biochemistry

October 10-12, 2016 Kuala Lumpur, Malaysia

Asokan Chinnasamy and Shagari A B

Sokoto State University, Nigeria

Posters & Accepted Abstracts: Biochem Anal Biochem

Abstract:

Hepta 1-6 cell binding study is 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. The interactions of Serum Amyloid A (SAA) and Serum Amyloid A protofibrils with Serum Amyloid P component [SAP (CaCl2)] to hepta 1-6 cells of the mouse are dealt with in detail to study the binding of SAA protofibrils in various conditions. The induced fluorescence, circular dichroism, FACScan and MTT assay results have shown the SAA and SAA fibrils binding with SAP (CaCl2) 0.12-1.2 nM and cell toxicity with the hepta 1-6 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. Already 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, SAA fibrils have more binding and cell cytotoxicity than SAA protein and has protective role with SAP (CaCl2).

Biography :

Email: asokan_74@hotmail.com