Akademik Veri Yönetim Sistemi
Turkish Journal of Biochemistry, cilt.36, sa.4, ss.350-355, 2011 (SCI-Expanded)
Aim: Amyloid is an extracellular insoluble protein aggregate which accumulates in several tissues in various clinical conditions. The co-localization of ASC, a key molecule in both apoptotic and inflammatory processes, with AA type amyloid fibrils has previously been demonstrated by our group. The aim of this study was to determine whether the distribution of ASC is altered around Aβ deposits and senile plaques in post-mortem brain samples of Alzheimer's disease patients. Material and Methods: Immunohistochemical and immunofluorescence staining of paraffin-embedded tissues from post-mortem brain samples of 12 Alzheimer's disease patients were performed using anti-ASC and anti-Aβ antibodies. Then we investigated possible ASC- Aβ co-localization in an in-vitro system using COS-7 cells. Results: Immunohistochemical staining of paraffin-embedded tissues revealed co-localization of ASC protein with Aβ peptide in senile plaques. We further demonstrated the interaction between ASC and Aβ in ASC-YFP and amyloid precursor protein co-transfected COS-7 cells which also showed that specks are located near the intracellular Aβ deposits. Conclusion: We hypothesize that expression of ASC may be important in the pathogenesis of Aβ amyloid formation and in senile plaque development in predisposed tissues. Further functional studies are required to explore the link between ASC and Aβ amyloid formation. Key Words: ASC, Aβ, APP, Alzheimer's disease, inflammation, COS-7 cell line. © TurkJBiochem.com.