Reach Us +1-218-451-2974


Interaction Of Soluble And Amyloid Form Of Serum Amyloid Aprotein To BC3H1 Cells | 36483
ISSN: 2161-0460

Journal of Alzheimers Disease & Parkinsonism
Open Access

Like us on:

Our Group organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations
700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)
Recommended Conferences
Google scholar citation report
Citations : 2245

Journal of Alzheimers Disease & Parkinsonism received 2245 citations as per google scholar report

Journal of Alzheimers Disease & Parkinsonism peer review process verified at publons
Indexed In
  • Index Copernicus
  • Google Scholar
  • Sherpa Romeo
  • Open J Gate
  • Genamics JournalSeek
  • Academic Keys
  • JournalTOCs
  • China National Knowledge Infrastructure (CNKI)
  • Electronic Journals Library
  • RefSeek
  • Hamdard University
  • OCLC- WorldCat
  • SWB online catalog
  • Virtual Library of Biology (vifabio)
  • Publons
  • Geneva Foundation for Medical Education and Research
  • Euro Pub
Share This Page

Interaction of soluble and amyloid form of serum amyloid aprotein to BC3H1 cells

3rd International Conference on Alzheimers Disease & Dementia

Asokan Chinnasamy and Musthapa I

Sokoto State University, Nigeria

ScientificTracks Abstracts: J Alzheimers Dis Parkinsonism

DOI: 10.4172/2161-0460.C1.015

The BC3H1 smooth muscle cells of mice brain, the study was carried out membrane binding. This 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 BC3H1 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 BC3H1 cells with different concentrations of Serum amyloid P component and Amyloid enhancing factor. Specifically, cells were incubated with 1.25-6.25 μM SAA-FITC and SAA protofibrils-FITC assayed. The 50% viable BC3H1 cells at 4-6 μM with an LD50 of 3.5 μM. The 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. The 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. The present study concludes the SAA fibrils more binding and cell cytotoxicity than SAA protein.

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, Nigeria. He has published more than 36 papers in reputed journals and has been serving as an Editorial Board Member of reputed journals.

Email: [email protected]