THE EFFECT OF BETA-AMYLOID PEPTIDES AND MAIN STRESS PROTEIN HSP70 ON HUMAN SH-SY5Y NEUROBLASTOMA PROTEOME
Accumulation and aggregation of β-amyloids are major molecular events underlying the progression of Alzheimer’s disease. In the neural cells, recombinant Hsp70 ameliorates the toxic effect of Aβ and its isomeric forms. Here we describe the proteome of neuroblastoma cell line after incubation with amyloid peptides Aβ42, isomerised Asp7 (‘‘isoAβ42’’) alone and in presence human recombinant heat shock protein 70 (HSP70). Incubation of SH-SY5Y cell culture with the synthetic Aβ-peptides lead to a decrease in the levels of several cytoskeleton proteins (e.g. ACTN1, VIME, TPM3) and several chaperonines involved in the folding of actin and tubulin (TCPQ, TCPG, TCPE, TCPB). These changes are accompanied by an increase in the expression of calmoduline and the proteins involved in the folding in endoplasmic reticulum and in endoplasmic cell stress response. In presence of exogenous HSP70, expression of several chaperones and a few other proteins, including endogenous HSP70, was increased. A combination of recombinant HSP70 with Aβ-peptides resulted in the reduction of apoptosis and the levels of tubulin phosphorylation as compared to the treatment with Aβ-peptides only.