Improvement in quality of life after bilateral transthoracic endoscopic sympathectomy for palmar hyperhydrosis.

OBJECTIVE: To evaluate the efficacy of bilateral transthoracic endoscopic sympathectomy (TES), in alleviating symptoms and improving quality of life for patients in Hawaii. DESIGN: Retrospective cohort study. MATERIALS AND METHODS: Patients who had undergone TES were evaluated by phone interview and the SF-36 questionnaire to assess improvements in symptoms and the development of compensatory hyperhydrosis. SF-36 scores were divided into 8 scales and evaluated by one-tailed t-test. RESULTS: Since 1999, eight patients (five women and three men, mean age 27.4 years old, range 15-41 yrs) underwent TES without significant complication. Length of hospital stay was less than one day for all patients except one, who stayed four days. Estimated operative blood lost was less than 100 ml and no blood transfusions were required. No Horner's syndrome was suffered. After a mean follow-up of 7.0 months (range 1.2-15.8 months), none of the patients had recurrent symptoms in the palms but all reported moderate compensatory hyperhydrosis located mainly in the trunk and lower extremities (two patients). SF-36 scores showed significant improvements in social functioning (p < 0.005), mental health (p < 0.049), and role-physical (p < 0.020) along with an increase in bodily pain (p < 0.012). CONCLUSION: Although TES resulted in some bodily pain and compensatory hyperhydrosis; these elements were outweighed by the improvement in palmar symptoms, social, mental, and role physical functioning, and overall quality of life.

Pho86p, an endoplasmic reticulum (ER) resident protein in Saccharomyces cerevisiae, is required for ER exit of the high-affinity phosphate transporter Pho84p.

In the budding yeast Saccharomyces cerevisiae, PHO84 and PHO86 are among the genes that are most highly induced in response to phosphate starvation. They are essential for growth when phosphate is limiting, and they function in the high-affinity phosphate uptake system. PHO84 encodes a high-affinity phosphate transporter, and mutations in PHO86 cause many of the same phenotypes as mutations in PHO84, including a phosphate uptake defect and constitutive expression of the secreted acid phosphatase, Pho5p. Here, we show that the subcellular localization of Pho84p is regulated in response to extracellular phosphate levels; it is localized to the plasma membrane in low-phosphate medium but quickly endocytosed and transported to the vacuole upon addition of phosphate to the medium. Moreover, Pho84p is localized to the endoplasmic reticulum (ER) and fails to be targeted to the plasma membrane in the absence of Pho86p. Utilizing an in vitro vesicle budding assay, we demonstrate that Pho86p is required for packaging of Pho84p into COPII vesicles. Pho86p is an ER resident protein, which itself is not transported out of the ER. Interestingly, the requirement of Pho86p for ER exit is specific to Pho84p, because other members of the hexose transporter family to which Pho84 belongs are not mislocalized in the absence of Pho86p.

8-Azido-ATP modification of cytochrome c: retardation of its electron-transfer activity to cytochrome c oxidase.

Horse heart cytochrome c has been modified by 8-azido-ATP and the electron-transfer activity of the modified cytochrome c's to bovine heart cytochrome c oxidase (CcO) under physiological ionic strengths has been studied by the laser flash photolysis technique with 5-deazariboflavin and EDTA as the electron donor. The intermolecular electron transfer between the redox protein partners was shown to be extremely slow. The 8-azido-ATP-modified system exhibited less than 5% of the intracomplex electron-transfer rate observed between native cytochrome c and CcO under otherwise identical conditions. The binding affinity of the modified cytochrome c was greatly reduced (3 orders of magnitude) at low ionic strengths; however, it was only slightly reduced (by a factor of 2) relative to the native protein at physiological ionic strengths. Thus, the binding affinity of the ATP-cytochrome c adducts is relatively insensitive to the ionic strength compared to the native enzyme, suggesting that a different docking conformation is assumed by the ATP-cytochrome c adducts in their interaction with the oxidase. Since the redox potential of the modified cytochrome c is close to the value of its native form, we conclude that there has been a change in the docking of the cytochrome c to CcO and the electronic coupling between heme c and CuA upon 8-azido-ATP modification.