In Alzheimer’s disease (AD) the most prevalent dementia in the western world, levels of the soluble peptide, amyloid beta (Aβ) are increased in the cerebral spinal fluid^1,2. Elevation of this peptide has also been found in sufferers of strokes and other vascular disorders^3,4. There is a strong positive correlate between the incidence of AD and those people who have had a prior ischemic episode⁵. To clearly define the link between these two afflictions, the human neuroblastoma cell line SH-SY5Y, was used as a neuronal model, and were either hypoxically incubated, or transfected with known AD related mutations. High-throughput planar patch clamp technique has been employed to analyse K+ channel current. Biotinylation followed by western blot, probing for Kv3.1b, was also used to detect any changes in protein localisation. Results show that cells containing Presenlin-1 (PS-1) mutations (e.g. D385N) and hypoxically treated cells both have elevated K+ channel current density; 79 ± 16 pA/pF (n=38) and 31 ± 12 pA/pF (n=5) at 50mV respectively, versus the control group, 16.5 ± 1.8 pA/pF (n=3). This functional elevation in current can be explained by an increase in membrane localisation of voltage gated potassium channels, as indicated by the biotinylation assay. This effect is ablated when one of the enzymes key to generating Aβ (γ – secretase) is inhibited. This data indicates a mechanism for the initiation of sporadic AD as a result of ischemic episodes, and also illustrates a role for Aβ in the homeostatic control of ions in neurons.