Summary
1. In normal leucocytes, glycogen-transferase was only found in the glucose-6-phosphate dependent D-form. An increase in activity was observed within 30 min after glucose feeding, and is assumed to be mediated through the action of released insulin. A late secondary increase in activity occurred simultaneously with an increase in serum growth hormone. — 2. In most diabetic leucocytes, glycogen-transferase was found in both the I- (independent of glucose-6-phosphate) and D-form. The I+D activity was low in uncontrolled diabetes and increased in response to insulin treatment. The I-activity was low immediately upon isolation of the leucocytes, but increased during incubation of the enzyme, especially in the presence of Mg2+; indicating that diabetic leucocytes possess transferase-D phosphatase activity in contrast to normal cells. The D to I transformation of the enzyme was greatly increased by insulin treatment. — 3. K m for UDPG and K a for glucose-6-phosphate did not vary between normal and diabetic leucocytes. — 4. The D to I interconversion of the incubated enzyme from diabetic cells was found to depend on the concentration of ATP and ADP in the incubation medium. It is suggested, that the activating effect of Mg2+ on the D to I transformation is due to an activation of an endogenous ATP-ase and adenylate kinase.
Résumé
1. Dans les leucocytes normaux, la glyeogène-transférase n'a été trouvée que sous la forme-D glucose-6-phosphate-dépendante. On a observé une augmentation de l'activité dans les 30 min consécutives à l'absorption de glucose, et on a supposé qu'elle était provoquée par l'action de l'insuline libérée. Une augmentation secondaire ultérieure de l'activité s'est produite en même temps qu'une augmentation de l'hormone de croissance du sérum. — 2. Dans la plupart des leucocytes de diabétiques, la glycogène-transférase a été trouvée à la fois sous la forme-D et la forme-I (indépendante du glucose-6-phosphate). L'activité I+D était faible dans le diabète non-contrôle et augmentait en réponse à un traitement insulinique. L'activité-I était faible immédiatement après isolement des leucocytes, mais augmentait pendant l'incubation de l'enzyme, particulièrement en présence de Mg2+, indiquant que les leucocytes de diabétiques possèdent une activité transférase-D phosphatase contrairement aux cellules normales. La transformation de l'enzyme de D en I était fortement accrue par le traitement insulinique. — 3.K m pour l'UDPG et K a pour le glucose-6-phosphate ne variaient pas entre les leucocytes normaux et diabétiques. — 4. La transformation de D en I de l'enzyme incubé à partir des cellules de diabétiques s'est avérée dépendre de la concentration d'ATP et d'ADP dans le milieu d'incubation. On suggère que l'effet activant du Mg2+ sur la transformation de D en I est due à une activation d'une ATPase endogène et d'une adénylate kinase.
Zusammenfassung
1. In normalen Leukozyten wurde die Glycogen-Transferase nur in der Glucose-6-Phosphatabhängigen Form D angetroffen. Ihre Aktivität steigt in den 30 min nach oraler Glucosezufuhr an, was auf die Insulinfreisetzung bezogen wird. Eine zweite spätere Aktivitätssteigerung erfolgte gleichzeitig mit dem Anstieg der Wachstumshormonspiegel im Serum. — 2. In den meisten diabetischen Leukozyten fand sich die Glykogen-Transferase in der D und der I Form (Glucose-6-Phosphat unabhängig). Die I+D Aktivität war bei entgleistem Diabetes niedrig und stieg nach Insulinbehandlung an. Unmittelbar nach der Isolierung der Leukozyten wurde nur eine geringe I Aktivität festgestellt, diese steigerte sich aber während der Inkubation des Enzyms, vor allem wenn diese in Gegenwart von Mg2+ erfolgte, was dafür spricht, daß diabetische Leukozyten im Gegensatz zu normalen Transferase-D Phosphatase Aktivität besitzen. Die Überführung der D in die I Form des Enzyms wurde durch Insulinbehandlung stark gefördert. — 3. Die K m für UDPG und K a für Glucose-6-Phosphat unterschieden sich bei normalen und diabetischen Leukozyten nicht. — 4. Es wurde festgestellt, daß die D zu I Umwandlung während der Inkubation des aus diabetischen Zellen gewonnenen Enzyms vom Gehalt des Mediums an ATP und ADP abhängt. Die Förderung der I zu D Umwandlung durch Mg2+ scheint auf der Aktivierung einer endogenen ATPase und einer Adenylat-Kinase zu beruhen.
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Esmann, V., Hedeskov, C.J. & Rosell Perez, M. UDP-glucose-glucan glucosyl-transferase activity of polymorphonuclear leukocytes from diabetic subjects. Diabetologia 4, 181–187 (1968). https://doi.org/10.1007/BF00430093
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DOI: https://doi.org/10.1007/BF00430093