BACKGROUND:Rotavirus illness is associated with significant cause of morbidity and is a common cause of hospitalization worldwide.OBJECTIVE:This study was performed to assess the role of rotaviruses in children presenting with acute diarrhea in two main Children's Medical Centers and one general hospital in Tehran.STUDY DESIGN:Stool specimens from 704 children less than 5 years of age suffering from diarrhea were tested for the presence of rotaviruses by a monoclonal antibody-based enzyme immunoassay. A total of 176 fecal specimens collected from healthy children in similar age group were studied as controls.RESULTS:Rotavirus antigen was detected in 15.3% of patients. Infants between 6 and 12 months of age were most frequently affected. Rotavirus infection was significantly less frequent in breast-fed than among bottle-fed babies. Watery diarrhea was present in 68.5% of children. Detection rate was highest in the spring and lowest in summer. Rotavirus can be regarded as a major etiologic agent of acute diarrhea in infants and children up to 5-years-old in Iran, immunization at birth may protect the children before their first symptomatic infection.

PET with 18F-fluoro-2-deoxy-glucose (FDG) is well established as an effective imaging modality for evaluating suspected brain tumor recurrence. Use of FDG PET imaging for spinal cord neoplasms has not yet been studied, in large part due to limitations of spatial resolution. One report of FDG PET imaging of brain involvement with primitive neuroectodermal tumor (PNET) demonstrated mild hypometabolism relative to cortical gray matter. We demonstrate with FDG PET imaging the appearance of recurrent intramedullary PNET affecting the cervical spinal cord.

This chapter investigates the performance of the two correction algorithms when applied to scatter from activity outside the field of view. Two studies with the Utah phantom have been presented in the chapter: In the first, the entire water-filled phantom contains uniform activity with the exception of the short cylinder, which contains only water, and a chamber, which is empty. The fraction of scattered events in the image can then be estimated from the mean value in a region of interest placed on the short (cold) cylinder expressed as a fraction of the activity in the inner cylinder. In the second study, the annulus contains approximately four times the activity in the inner cylinder to simulate increased cortical uptake. In addition, the long cylinder contains twice the background activity to simulate uptake in subcortical structures. This chapter also explores the quantitative potential of 3D positron emission tomography (PET), and in particular the efficacy of the two scatter correction procedures, when applied to neuroreceptor ligand studies. For this, a ligand for imaging central benzodiazepine receptors is used.

Determination of the individual geometrical and efficiency normalization factors is a more involved procedure in 3D than in 2D because of the incorporation of oblique lines-of-response which results in an order of magnitude increase in the number of correction factors required. Techniques using rotating rod source scans in both 2D and 3D, and a uniform cylinder scan in 3D, have been developed for estimating normalization factors. However, a uniform plane source is generally considered the best combination of a low scatter environment and a centrally-located isotope distribution. Plane sources are difficult and expensive to construct with the required uniformity and long half-life. The authors have investigated the use of a scanning germanium line source which simulates a plane source distribution by slowly traversing across the field-of-view. They compare 3D reconstructions using estimates of the geometrical and efficiency correction factors for normalization obtained from rotating rod, plane (scanning line) and cylinder source distributions. No significant difference is found to distinguish the 3D reconstructions of the uniform cylinder

Defects of glucose transport and phosphorylation may underlie insulin resistance in obesity and non-insulin-dependent diabetes mellitus (NIDDM). To test this hypothesis, dynamic imaging of 18F-2-deoxy-glucose uptake into midthigh muscle was performed using positron emission tomography during basal and insulin-stimulated conditions (40 mU/m2 per min), in eight lean nondiabetic, eight obese nondiabetic, and eight obese subjects with NIDDM. In additional studies, vastus lateralis muscle was obtained by percutaneous biopsy during basal and insulin-stimulated conditions for assay of hexokinase and citrate synthase, and for immunohistochemical labeling of Glut 4. Quantitative confocal laser scanning microscopy was used to ascertain Glut 4 at the sarcolemma as an index of insulin-regulated translocation. In lean individuals, insulin stimulated a 10-fold increase of 2-deoxy-2[18F]fluoro-D-glucose (FDG) clearance into muscle and significant increases in the rate constants for inward transport and phosphorylation of FDG. In obese individuals, the rate constant for inward transport of glucose was not increased by insulin infusion and did not differ from values in NIDDM. Insulin stimulation of the rate constant for glucose phosphorylation was similar in obese and lean subjects but reduced in NIDDM. Insulin increased by nearly twofold the number and area of sites labeling for Glut 4 at the sarcolemma in lean volunteers, but in obese and NIDDM subjects translocation of Glut 4 was attenuated. Activities of skeletal muscle HK I and II were similar in lean, obese and NIDDM subjects. These in vivo and ex vivo assessments indicate that impaired glucose transport plays a key role in insulin resistance of NIDDM and obesity and that an additional impairment of glucose phosphorylation is evident in the insulin resistance of NIDDM.

We have examined the onset and duration of the inhibitory effect of an intravenous infusion of lipid/heparin on total body carbohydrate and fat oxidation (by indirect calorimetry) and on glucose disappearance (with 6,6 D2-glucose and gas chromatography-mass spectrometry) in healthy men during euglycemic hyperinsulinemia. Glycogen synthase activity and concentrations of acetyl-CoA, free CoA-SH, citrate, and glucose-6-phosphate were measured in muscle biopsies obtained before and after insulin/lipid and insulin/saline infusions. Lipid increased insulin-inhibited fat oxidation (+40%) and decreased insulin-stimulated carbohydrate oxidation (-63%) within 1 h. These changes were associated with an increase (+489%) in the muscle acetyl-CoA/free CoA-SH ratio. Glucose disappearance did not decrease until 2-4 h later (-55%). This decrease was associated with a decrease in muscle glycogen synthase fractional velocity (-82%). The muscle content of citrate and glucose-6-phosphate did not change. We concluded that, during hyperinsulinemia, lipid promptly replaced carbohydrate as fuel for oxidation in muscle and hours later inhibited glucose uptake, presumably by interfering with muscle glycogen formation.

We investigated the effects of infusion of a 20% triglyceride emulsion plus heparin (LH) on carbohydrate (CHO) metabolism during basal insulin and glucose turnover conditions in normal male subjects. In study 1, LH or saline was infused at 0.5 and 1.5 ml/min for 2 h each. Plasma free fatty acids rose from ∼0.4 to 0.8 mM with the low rate and to between 1.6 and 2.1 mM with the high rate. Similar increases occurred in plasma concentrations of glycerol, acetoacetate, and β-hydroxybutyrate. LH infusions resulted in significant increases in C-peptide concentrations but had no effects on any of the other measured parameters of CHO metabolism. In study 2, LH or saline was infused as in study 1, but the compensatory insulin release was prevented by intravenous infusion of somatostatin and replacement of basal insulin and glucagon concentrations. This resulted in significant increases in plasma glucose (from 4.5 ± 0.2 to 7.1 ± 0.6 mM, P < 0.001) and hepatic glucose output (from 9.0 ± 1.5 to 11.3 ± 1.4 μmol · kg−1 · min−1, P < 0.05) and a decrease in glucose clearance (from 2.32 ± 0.13 to 1.44 ± 0.11 ml · kg−1 · min−1, P < 0.05). We conclude that lipids can have adverse effects on CHO metabolism under basal conditions and that healthy individuals can compensate for these effects with additional secretion of insulin.

We have developed a radioimmunoassay for human insulin receptor. Serum from a patient with Type B severe insulin resistance was used as anti-insulin receptor antiserum. Pure human placental insulin receptor was used as reference preparation and 125I labeled pure insulin receptor as trace. The radioimmunoassay was sensitive (limit of detection less than 17 fmol), reproducible (inter and intra-assay coefficients of variation 12.5% and 1.6% respectively) and specific (no crossreactivity with pure placental IGF-1 receptor, insulin and glucagon). The anti-insulin receptor antibody was, however, able to differentiate between insulin receptor from human placenta and from rat liver. To determine the number of insulin binding sites per receptor, we measured insulin binding (by insulin binding assay) and insulin receptor mass (by radioimmunoassay) in solubilized aliquots from 5 human placentas. The molar ratio of insulin binding to receptor mass was 0.86 +/- 0.12 when binding was determined with monoiodinated 125I-Tyr A 14-insulin. It was 1.94 +/- 0.27 when randomly iodinated 125I-insulin was used. In conclusion, using a sensitive, reproducible and specific radioimmunoassay, we have measured insulin receptor mass independent of insulin binding. Our data are most compatible with binding of one insulin molecule per human placental insulin receptor.

Amino acids stimulate the release of glucagon and insulin. To assess the role of aminogenic hyperglucagonemia, we have studied, in healthy young males, the effects of basal (less than 100 pg/ml) and high (200-400 pg/ml) plasma glucagon concentrations on amino acid metabolism during intravenous infusion (0.5 g.h-1.4 h) of a mixture of 15 amino acids. Basal plasma glucagon concentrations were obtained by infusion of somatostatin (0.5 mg/h) plus glucagon (0.25 ng.kg-1.min-1) and high plasma glucagon concentrations by infusion of somatostatin plus glucagon (3.0 ng.kg-1.min-1) or by infusion of amino acids alone. All studies were performed under conditions of euglycemic (83-91 mg/dl) hyperinsulinemia (50-80 microU/ml). Hyperglucagonemia significantly increased 1) net amino acid transport from the extracellular into the intracellular space (by approximately 4%), 2) net degradation of amino acids entering the intracellular space (by approximately 40%), and 3) conversion of degraded amino acids into glucose from 0-10% (basal glucagon) to 70-100% (high glucagon). Hyperglucagonemia did not affect the amount of amino acids excreted in the urine (approximately 4%). We conclude that glucagon plays an important role in the disposition of amino acids by increasing their inward transport, their degradation, and their conversion into glucose.