Assessing positive and negative symptoms in children and adolescents.

OBJECTIVE: The purpose of this study was to test the reliability and validity of a new assessment instrument for positive and negative symptoms in severely disturbed children and adolescents (Kiddie-PANSS). METHOD: The Positive and Negative Syndrome Scale for adult schizophrenia was modified through successive field trials on the basis of developmental characteristics of children and adolescents. The scale was then given to 34 inpatients (19 children, mean age = 9.35 years, and 15 adolescents, mean age = 14.33 years) with DSM-III-R diagnoses of schizophrenia, psychosis not otherwise specified, schizoaffective, affective, conduct, personality, and developmental disorders determined independently by child psychiatrists. All patients with schizophrenia were placed in the schizophrenic group, and all others were placed in a general inpatient group. The Kiddie-PANSS ratings were given by three trained child psychiatrists after a 30-35-minute structured interview. The Achenbach Child Behavior Checklist, the Scale for the Assessment of Positive Symptoms, and the Scale for the Assessment of Negative Symptoms were also administered in order to determine criterion-related association. RESULTS: Intraclass correlation coefficients revealed that all subscales and total psychopathology were reliably assessed among raters. The Kiddie-PANSS and Scale for the Assessment of Positive Symptoms/Scale for the Assessment of Negative Symptoms correlated with one another, indicating criterion-related association. Differences on measures of positive, negative, and general psychopathology, as measured by the Kiddie-PANSS, between the patients with schizophrenia and the general inpatient group were highly significant. CONCLUSIONS: The Kiddie-PANSS shows good interrater reliability and criterion-related validity. In a cohort of inpatient children and adolescents the scale successfully differentiated schizophrenic patients from nonschizophrenic patients.

The effects of aestivation on the catalytic and regulatory properties of pyruvate kinase from Helix aspersa.

1. Pyruvate kinase was partially purified from the foot, mantle, and digestive gland of active and aestivating snails. 2. At pH 7.0 the apparent Km values for phosphoenolpyruvate (PEP) were 0.064 mmol/l for the enzyme from foot and 0.071 mmol/l for the enzyme from mantle; those for ADP were 0.35 mmol/l for the foot enzyme and 0.33 mmol/l for the mantle enzyme. 3. Both enzymes were inhibited by alanine, and this could be reversed by fructose 1,6-bisphosphate (FBP), although FBP alone was a weak activator. 4. Decreasing the pH to 6.5 markedly increased the inhibition by alanine and reduced the response to FBP. 5. The enzymes from these tissues of aestivating snails showed a small decrease in their affinity for PEP and a small increase in the effectiveness of alanine as an inhibitor. 6. These changes are indicative of a down-regulation of this enzyme which is consistent with the observations in other species during metabolic depression. 7. In contrast the enzyme from the digestive gland of active animals showed sigmoidal saturation kinetics for PEP with a S0.5 of 1.2 mmol/l, but had a markedly higher affinity for PEP, S0.5 = 0.20 mmol/l during aestivation. This may be indicative of other metabolic changes occurring in the digestive gland.

NAD(+)-linked isocitrate dehydrogenase in fish tissues.

NAD(+)-linked isocitrate dehydrogenase was found in the brain, heart, gills, kidney, liver and muscle of trout, and in the liver and muscle of eel. A complex homogenization buffer containing 1 mM ADP, 5 mM MgSO4, 5 mM citrate and 40% glycerol is required for retrieval of significant amounts of stable enzyme. The highest activities were found in brain of trout and the lowest in white muscle of trout and eel. The enzyme was partially purified from frozen trout heart to a final activity of 0.04 µM/min/mg protein, and the kinetic properties of this partially purified enzyme were studied. The enzyme requires either Mn(2+) or Mg(2+) for activity, higher activities being observed with Mn(2+). Saturation kinetics for DL-isocitrate were sigmoidal, apparent S0·5=8.2±0.6 mM and nH=1.8±0.2, in the absence of ADP, changing to hyperbolic, apparent S0·5=1.4±0.3 mM and nH=1.0, with 1 mM ADP added. Citrate and Ca(2+) were found to activate the enzyme to a small extent. NADH strongly inhibited the enzyme, I50=3.7±0.5 µM. ATP was also found to be an inhibitor, I50=7.2±1.4 mM. These properties are consistent with the role of the enzyme as a major control site of the tricarboxylic acid cycle.

Purification and properties of glutamate dehydrogenase from the mantle muscle of the squid, Loligo pealeii. Role of the enzyme in energy production from amino acids.

1. The activity of glutamate dehydrogenase was measured in the tissues of the squid, Loligo pealeii. The enzyme occurs in high activity in digestive pouch, systemic heart, and all muscle tissues. 2. Glutamate dehydrogenase from mantle muscle is located intra-mitochondrially, has a molecular weight of 310,000, and is electrophoretically similar to the enzyme from all other squid tissues. 3. The enzyme from mantle muscle was purified 40-fold by elution from DEAE-cellulose and used for kinetic studies. The enzyme is NAD+-specific, activated by ADP, AMP, and leucine, and inhibited by GTP, GDP, ATP, and reaction products (in particular NADH). 4. Squid glutamate dehydrogenase shows an almost absolute dependence on ADP. The purified enzyme is activated over 100-fold by saturating concentrations of ADP (Ka = 0,75 7M); The pH optima are also altered significantly by ADP. 5. The enzyme appears to be kinetically adapted to favour glutamate oxidation in comparison to glutamate dehydrogenase from other resources. The evidence indicates that the primary role of glutamate dehydrogenase in squid mantle muscle is in regulating the catabolism of amino acids for energy production.

Octopine as an end product of anaerobic glycolysis in the chambered nautilus.

The terminal step in the anaerobic glycolysis of muscle in the chambered nautilus, Nautilus pompilius, is not pyruvate reduction to lactate as in vertebrate muscle. Instead of lactate dehydrogenase, these organisms utilize octopine dehydrogenase (E.C. 1.5.1.11), catalyzing the reductive condensation of pyruvate and arginine, which is dependent on the reduced form of nicotinamide adenine dinucleotide, to form octopine and the oxidized form of the coenzyme. The kinetic properties of octopine dehydrogenase favor the production of octopine, which accumulates under a variety of conditions.