Magic™ Anti-TH (aa 50-150) polyclonal antibody

Background and purpose The aim was to clarify the features affecting cardiac sympathetic denervation in autopsy-confirmed dementia with Lewy bodies (DLB) patients. Methods Fifty-four autopsy-confirmed DLB patients were enrolled. Tissue samples of the left ventricular anterior wall were immunostained with anti-tyrosine hydroxylase antibody to identify catecholaminergic nerve axons. Immunostained areas were quantified as residual cardiac sympathetic nerve (CSN) axons and the relationship between the degree of residual CSN axons and clinical and neuropathological features was examined. Results Virtually all patients showed small amounts of residual CSN axons (0.87%, range 0.02%-9.98%), with 50 patients (92.6%) showing <2.0% of residual axons. The patients who showed psychological symptoms within the first year of the disease had significantly more residual CSN axons than the remaining patients did (1.50% vs. 0.40%, P < 0.01). Patients with a short disease duration and neocortical-type Lewy body pathology tended to have more preserved CSN axons, although this difference was not statistically significant. Fifty-three patients (98.1%) who had neurofibrillary tangles in the brain and strong concomitant Alzheimer's disease pathology also had statistically significantly more preserved CSN axons. The patient with the most preserved CSN axons showed different characteristics from the results, except for the first symptom. Conclusion Psychological symptoms within the first year of the disease, a short disease duration, neocortical-type Lewy body pathology and strong concomitant Alzheimer's disease pathology may be related to mild CSN degeneration in DLB patients. Thus, DLB patients with broad Lewy body pathology in the brain in the early stages may show mild CSN degeneration.

Phenylketonuria (PKU) is a rare, loss-of-function, inborn error of metabolism. It is a chronic amino acid transport disorder caused by a heritable mutation that results in decreased metabolism of the essential amino acid phenylalanine (Phe). It is a common genetic disorder that arises from deficient activity of phenylalanine-4-hydroxylase (phenylalanine hydroxylase; PAH), the rate-limiting enzyme of the metabolic pathway that degrades Phe to tyrosine. The disorder is caused by mutations in the PAH gene, which encodes for the enzyme PAH. The majority of PKU-causing mutations in PAH are missense mutations. The current mainstay of treatment is lifelong dietary modification, including restriction of Phe and tyrosine supplementation. However, because the diet is so restrictive, adherence is extremely difficult. Further investigation is needed to find agents that may activate or act as a chaperone for PAH. This article presents those drug targets that are currently under active investigation for the treatment of PKU.