A Study of Spectrum of Cardiac Rhythm Disturbance after Acute Ischemic Stroke Using 24 Hours Holter Monitoring.

Studies have reported that acute stroke leads to imbalance of central autonomic control; stroke can cause over activity of sympathetic or parasympathetic control, myocardial injury, ECG abnormalities, cardiac arrhythmias and even sudden death. Studies support the notion that patients with acute cerebrovascular events are susceptible to cardiac arrhythmias. MATERIAL: This cross Sectional Study was conducted in over a period of One and half year duration and included subjects of acute ischemic stroke confirmed by brain imaging. After performing a 12 lead ECG in emergency ward, all eligible stroke patients were subjected to 24 hour Holter monitoring. OBSERVATION: Out of 92 stroke patients, 35.28% had abnormal ECG. Changes included LVH in 10.87%, T wave inversion in 9.78%, ST segment depression in4.35%% followed by QTc prolongation 3.26% .24 hours Holter monitoring revealed that common cardiac rhythm disturbances were ventricular ectopics (44.57%) supraventricular ectopics (30.43%), supraventricular tachycardia (11.96%), atrial fibrillation (7.60%). Amongst brady-arrhythmias sinus pause was detected in 1.09%. CONCLUSION: ECG changes occur commonly in case of acute ischemic stroke, even in those having no history of coronary heart disease as suggested clinically. Identification of paroxysmal Atrial Fibrilation episodes is important due to its relevance for planning of long-term treatment.

Parkinson's disease alpha-synuclein mutations exhibit defective axonal transport in cultured neurons.

Alpha-synuclein is a major protein constituent of Lewy bodies and mutations in alpha-synuclein cause familial autosomal dominant Parkinson's disease. One explanation for the formation of perikaryal and neuritic aggregates of alpha-synuclein, which is a presynaptic protein, is that the mutations disrupt alpha-synuclein transport and lead to its proximal accumulation. We found that mutant forms of alpha-synuclein, either associated with Parkinson's disease (A30P or A53T) or mimicking defined serine, but not tyrosine, phosphorylation states exhibit reduced axonal transport following transfection into cultured neurons. Furthermore, transfection of A30P, but not wild-type, alpha-synuclein results in accumulation of the protein proximal to the cell body. We propose that the reduced axonal transport exhibited by the Parkinson's disease-associated alpha-synuclein mutants examined in this study might contribute to perikaryal accumulation of alpha-synuclein and hence Lewy body formation and neuritic abnormalities in diseased brain.