T-cell lymphoma mimicking granulocytic sarcoma.

A case of diffuse large cell lymphoma is described in which eosinophils and eosinophilic myelocytes were admixed with the neoplastic lymphoid cells. Because of the eosinophilic myelocytes, a diagnosis of granulocytic sarcoma was initially considered. No abnormalities of peripheral blood or bone marrow were found. Immunohistochemical studies of lymph node tissue demonstrated membrane antigens consistent with a lymphoma of helper T-cells. Small lymphoid cells with markedly irregular nuclei were present but rather inconspicuous among the larger lymphoid cells. Although a clinical remission was attained, the patient had a relapse with central nervous system involvement.

Contribution of cyclic adenosine 3':5'-monophosphate to the regulation of bacterial glycogen synthesis in vivo. Effect of carbon source and cyclic adenosine 3':5'-monophosphate on the quantitative relationship between the rate of glycogen synthesis and the cellular concentrations of glucose 6-phosphate and fructose 1,6-diphosphate in Escherichia coli.

When either fructose, glycerol, or succinate served as a sole source of carbon and energy in nitrogen-starved cultures of Escherichia coli W4597(K) the values of the kinetic constants of the equation that expresses the relationship between glycogen synthesis and hexose phosphates were different from the values observed when glucose was the sole source of carbon and energy. Addition of glucose during either exponential growth or nitrogen starvation to a culture using one of the other carbon sources slowed the rate of glycogen synthesis and shifted the values of the constants toward the values observed in cultures using glucose alone. Addition of cyclic AMP (cyclic adenosine 3':5'-monophosphate) during exponential growth of a culture using glucose caused the values of the constants to be shifted toward the values observed in cultures using a carbon source other than glucose. In all of the metabolic conditions studied in this report the adenylate energy charge ((ATP + 1/2 ADP)/(ATP + ADP + AMP)) and the level of the rate-limiting enzyme of glycogen synthesis, ADP-glucose synthetase (glucose 1-phosphate adenylyltransferase, EC 2.7.7.27), were the same. The data presented here indicate that the difference we observed in the quantitative relationship for glycogen synthesis is the result of the different cellular levels of cyclic AMP in the cells using glucose and the cells using one of the other carbon sources. Since cyclic AMP does not affect the velocity of ADP-glucose synthetase in vitro, apparently a change in the cellular level of cyclic AMP causes a shift in the cellular level of a presently unknown (and previously undetected) effector of this enzyme. The shift in the level of this effector evidently alters the response of the enzyme in vivo to the substrate glucose 1-phosphate and the activator fructose 1,6-diphosphate.

Regulation of glycogen synthesis and glucose utilization in Escherichia coli during maintenance of the energy charge. Quantitative correlation of changes in the rates of glycogen synthesis and glucose utilization with simultaneous changes in the cellular levels of both glucose 6-phosphate and fructose 1,6-diphosphate.

Treatment of nitrogen-starved cultures of Escherichia coli W4597(K) with sodium azide results in simultaneous changes in both glucose 6-phosphate and fructose 1,6-diphosphate as well as in the rate of glycogen synthesis. Based on these observations, a comprehensive equation was developed which relates the cellular levels of both of these hexose phosphates with the rate of glycogen synthesis. This relationship apparently represents the interaction in vivo between the rate-limiting enzyme of bacterial glycogen synthesis, glucose 1-phosphate adenylyltransferase (adenosine diphosphoglucose synthetase, EC 2.7.7.27), and its substrate glucose 1-phosphate (reflected by glucose 6-phosphate) and its major allosteric activator fructose diphosphate. The form of the equation that describes this relationship was determined from studies presented here of the kinetic properties of the E. coli W4597(K) enzyme in the presence of physiological concentrations of its substrates and modulators. We show here and in subsequent reports of this series that the comprehensive relationship between glycogen synthesis and hexose phosphates can serve as a reference to evaluate the possible participation of new factors in the regulation of glycogen synthesis. Treatment with NaN3 did not change the cellular level of glucose 1-phosphate adenylyltransferase. The value of the adenylate energy charge, (ATP + 1/2 ADP)/(ATP + ADP + AMP), was maintained despite losses of up to 35% in cellular adenylates. The quantitative co-variance between hexose phosphates and the cellular rate of glucose utilization that we previously described for other metabolic conditions was also observed in the azide-treated cultures. We integrate the new information into the system of coordinated regulation of glycogen synthesis, glycolysis, and glucose utilization that we proposed previously.

Prediction of the rate of glucose utilization from cellular levels of glucose 6-phosphate and fructose 1,6-diphosphate in Escherichia coli.

A comprehensive equation, upsilon = VM/[1 + (A0.5/Fru-P2)n] [ 1 + (Glc-6-P/I0.5)], has been proposed to represent the quantitative interrelationships between the rate of glucose utilization and the levels of glucose-6-phosphate and fructose-1,6-diphosphate in the intact Escherichia coli cell. This comprehensive equation was derived from empirical equations that describe the relationship between the rate of glucose utilization and one of these hexose phosphates in metabolic situations where the other hexoses phosphate was not altered. In the experiments described in this report, treatment of nitrogen (NH4+)-starved cultures of E. coli W4597 (K) with various concentrations of sodium azide altered the levels of both hexose phosphates as well as the rate of glucose utilization. In each case the observed rate and the rate predicted by the comprehensive equation agreed closely, substantiating the validity of this comprehensive relationship as a quantitative indicator of metabolic events in the intact cell. The mechanism of metabolic regulation that is represented by this equation is discussed in light of the cellular levels of adenosine 5'-triphosphate and phosphoenolpyruvate observed in these experiments.