Previous work from our laboratory has demonstrated that TGinduced apoptosis as well as apoptosis resistance induced by EGF in DU145 cells are mechanisms dependent of intracellular Ca2+ signalling. We have observed that PHE treatment has no affect on the intracellular Ca2+ concentration. This observation strongly suggests that resistance to TG-induced apoptosis in DU145 by PHE does not involve the Ca2+ signalling pathway. a1A-AR signalling is complex and various lines of evidence demonstrate that a1A-AR stimulation can activate a variety of signalling pathways depending on cell type, receptor expression and agonist concentration. It has been previously described, in cardiomyocytes, that a1A-AR activate ERK-related survival pathways. We have revealed, for the first time, the involvement of the ERK1/2 MAPK pathway in the apoptosis resistance function of the a1A-AR in DU145 androgenindependent prostate cancer cells. Interestingly, it has been demonstrated that human prostate biopsies have increased levels of activated ERKs in malignant tissues as compared to those in benign specimens. In conclusion, we demonstrate that caveolae of androgenindependent prostate cancer cells DU145 are involved in the apoptosis resistance induced by the a1A-AR. Our data show that caveolae integrity is necessary for a1A-AR function in these cells. This study reveals that a1A-AR and cav-1 expressions are positively correlated with the pathological state of human prostate and are highly expressed in advance PCa tissue samples. Our data strongly suggest that the protective function of the a1A-AR via caveolae described in DU145 cells, may contribute in synergy with other factors, to the apoptosis resistance mechanisms of PCa cells and enhancement of their survival. Aggregation of hyper-phosphorylated protein tau into filaments and eventually neurofibrillary tangles is characteristic for tauopathies, a large and diverse group of neurodegenerative Tulathromycin B disorders, including Alzheimer��s disease. Primary tauopathies present as clinically variable entities, e.g. Pick��s disease, progressive supranuclear palsy, corticobasal degeneration and frontotemporal dementia, among others. Tauopathy is defined by fibrillar and tangled aggregates of phosphorylated protein tau, which is normally a very soluble protein that binds to microtubules to secure their assembly, stability and spacing. Tau3R and Tau4R isoforms have different affinity for microtubules and their relative abundance is regulated by alternative mRNA splicing. Post-translational, dynamic regulation of microtubule-binding is thought to occur by phosphorylation of tau at various serine/threonine residues by various kinases, including GSK3, cdk5, and MARK, among others. In adult ageing brain, in primary tauopathies and in AD, protein tau becomes excessively phosphorylated, eventually changing its conformation to induce aggregation resulting in tauopathy. Interestingly, both intronic and exonic mutations in the MAPT gene encoding protein tau, are dominantly associated with various tauopathies implying that neurotoxicity results from mutant tau protein, but as well from wildtype tau by 4-(Benzyloxy)phenol isoform imbalances. Alzheimer��s disease is the most prominent secondary tauopathy, wherein intracellular tau inclusions combine with amyloid deposits. Amyloid peptides are normal constituents in human brain at any age, stemming from amyloid precursor protein by a complex set of proteinases. With ageing, amyloid peptides accumulate and aggregate, eventually becoming deposited in parenchym and vasculature, even in cognitive normal individuals as is emerging from clinical imaging studies.