A conceptual model of psychosomatic illness in children. Family organization and family therapy.

Linear and open systems (multiple feedback) models of psychosomatic illness in children are contrasted in terms of their implications for cause and treatment. An open systems family model is presented that describes three necessary (but not independently sufficient) conditions for the development and maintenance of severe psychosomatic problems in children: (1) a certain type of family organization that encourages somatization; (2) involvement of the child in parental conflict; and (3) physiological vulnerability. Predisposition for psychosomatic illness, symptom choice, and maintenance are discussed within this conceptual framework. We report on family therapy strategies based on this model and the results of family treatment with 48 cases of "brittle" diabetes, psychosomatic asthma, and anorexia nervosa.

Enzymes of glycogen metabolism in developing embryos of a teleost.

An acceleration of glycogenolysis after fertilization in loach (Misgurnus fossilis L.) eggs is not related to an increase of active phosphorylase (EC 2.4.1.1). The activity of "debranching" enzymes (amylo-1,6-glucosidase; dextrin-6-glucohydrolase, EC 3.2.1.33) considerably increases during early embryogenesis. These facts suggest that the enhancement of debranching enzyme activity is the controlling factor of glycogenolysis at early stages of embryonic development.Only 15-20% of the amylo-1,6-glucosidase and phosphorylase is found to be firmly associated with a particular glycogen fraction both in oocytes and embryos. The onset of glycogenolysis after fertilization is not accompanied by redistribution of the above-mentioned enzymes between different fractions of glycogen.

Redox state of nicotinamide adenine nucleotide and phosphorylated state of adenine nucleotide in oocytes and embryos of the loach (Misgurnus fossilis L.).

The decrease of the phosphorylated state of the adenine nucleotide system (ATP)/(ADP) (HPO 4-2 ) during oocyte maturation of the loach (Misgurnus fossilis L.) correlated with the fall of the (NAD+)/(NADH) ratio. A increase of the cytoplasmic (NADP+)/(NADPH) ratio was also found.

Interconversion of active and inactive forms of phosphorylase and glycogen synthetase in oocytes and embryos of the loach (Misgurnus fossilis L.).

Glycogen synthetase (EC 2.4.1.11) from oocytes and embryos of the loach (Misgurnus fossilis L.) has been found only in the D-form. The intensive glycogen accumulation during oogenesis did not correspond with the glycogen synthetase interconversion in the I-form.In isolated oocytes and embryos of the loach insulin transforms glycogen synthetase into the form which is desensitized for ATP inhibition. Insulin treatment enhancesV max without affecting theK m (UDP-glucose) only with an excess of activator-glucose-6-P. Simultaneously insulin treatment converts the phosphorylase (EC 2.4.1.1.) into the latent form.

Factors responsible for glycogenolysis acceleration in early embryogensis of teleosts.

An acceleration of the rate of glycogenolysis in the early embryogenesis of the loach (Misgurnus fossilis L.) is accompanied by an increase of the content of hexose monophosphates, the rate of lactate formation and the rate of respiration. The unfertilized egg and the intact embryo of the loach have an identical activity of phosphorylase (EC 2.4.1.1.) and a constant ratio of the active/latent phosphorylase.Following the stage of 32 blastomeres, an increase of phosphorylase activity and the glycogen content occurs in the yolk-free embryo (blastoderm); this increase stops after the onset of gastrulation. In view of the facts that a) the blastoderm contains practically no latent phosphorylase, b) an elevation of phosphorylase activity is synchronized with an increase of the glycogen content, and c) this process is not related to an increase of the total phosphorylase activity and glycogen content in the intact egg, the authors suggest that glycogen-bound phosphorylase transfers from the yolk to the embryo at the stages of cleavage and blastula.In the loach oocyte, unfertilized egg and embryo the main activity of phosphorylase (more than 3/4) is associated with low molecular weight glycogen; this form of glycogen cannot be sedimented at 144000 g, and constitutes not more than 30 % of the total glycogen.Glycogen synthetase (EC 2.4.1.11) is, on the contrary, bound completely with granular glycogen. The oocyte maturation, ovulation and the onset of glycogenolysis after fertilization do not involve a redistribution of enzymes between glycogen fractions of different molecular weights.An increase of the glucose level in oocytes accelerates the conversion of active phosphorylase into its latent form. Physiological concentrations of glucose (up to 2 × 10-2 M) do not inhibit phosphorylase activity.

Changes in enzyme activity of glycogen and hexose metabolism during oocyte maturation in a teleost,Misgurnus fossilis L.

The oocyte at the end of oogenesis, mature egg and developing embryo of the loachMisgurnus fossilis L.) are characterized by indentical enzyme profiles of the Embden-Meyerhof chain, pentose phosphate cycle and key gluconeogenic enzymes. However, the carbohydrate metabolism in the oocyte differs substantially from that in the embryo.Oocyte maturation is followed by a complete loss of hexokinase (EC2.7.1.1),2-fold decrease of glycogen synthetase (EC 2.4.1.11) and 10-fold increase of glycogen phosphorylase (EC2.4.1.1) activity. This process is correlated with a gradual decrease of the ATP/(ADP+AMP) ratio from 4∶1 to 2∶1 and increase of the Fructose-6-Phosphate/Fructose-1,6-Diphosphate ratio from 0.27 to 2.0. Thus, oocyte maturation involves a number of changes in control mechanisms resulting in cessation of glycogen accumulation and a transition of carbohydrate metabolism from gluconeogenesis to glycogenolysis.