Summary
Glycerol kinase was measured by a modification of the radiochemical enzyme test described by Newsholme and coworkers in isolated epididymal and parametrial fat cells and liver tissue of obese hyperglycaemic Bar Harbor mice (obob) and their lean littermates (ob+ob+). The specific activity of glycerol kinase was independent of age in the control animals. It was about 90 times greater in liver than in fat cells. In obese animals glycerol kinase was dependent on age. Compared with the controls, the activity was significantly increased in fat cells of 2–12-month old mice and in liver of 5-month old mice. In fat cells of 2–12-month old mice fedad libitum, glycerol kinase activity was significantly correlated to serum IRI-levels. — Glycerol kinase activity decreased during fasting or experimental insulin deficiency, induced by streptozotocin. It was significantly increased in fat cells and liver by insulin substitution. This insulin effect was suppressed by actinomycin D. — It is concluded that insulin regulates glycerol kinase activity by enzyme induction. — The significance of these results for the adipose tissue metabolism in obob mice is discussed.
Résumé
La glycéro-kinase a été mesurée à l'aide du test enzymatique radiochimique modifié de Newsholme et collaborateurs dans les cellules adipeuses isolées de l'épididyme et du parametrium et dans le tissu hépatique chez des souris obèses hyperglycémiques de Bar Harbor (obob) et chez des souris de la même portée et de poids normal (ob+ob+). — L'activité spécifique de la glycérokinase ne dépendait pas de l'âge chez les animaux témoins; elle était environ 90 fois plus grande dans le foie que dans les cellules adipeuses. Chez les animaux obèses, la glycérokinase dépendait de l'âge; par rapport aux animaux témoins, l'activité était nettement augmentée dans les cellules adipeuses des souris de 2 à 12 mois et dans le foie de celles de 5 mois. L'activité enzymatique dans les cellules adipeuses des souris de 2 à 12 mois nourries ad libitum, montrait une corrélation significative avec le taux de l'insuline du sérum. Après carence de nourriture ou réduction du taux d'insuline par la streptozotocine, l'activité de la glycéro-kinase était diminuée. Mais elle était augmentée dans les cellules adipeuses et dans le foie par un traitement substitutif à l'insuline. L'actinomycine D inhibait cet effet de l'insuline. On en conclut que l'insuline règle l'activité de la glycéro-kinase par induction enzymatique. La signification de ces résultats quant au métabolisme du tissu adipeux chez la souris obob est discutée.
Zusammenfassung
Glycerokinase wurde mit einer Modifikation des radiochemischen Enzymtests von Newsholme und Mitarb. in isolierten epididymalen und parametranen Fettzellen und im Lebergewebe von fettsüchtigen hyperglykämischen Bar Harbor-Mäusen (obob) und deren normgewichtigen Wurfgeschwistern (ob+ob+) bestimmt. Die spezifische Aktivität der Glycerokinase war bei den Kontrolltieren altersunabhängig; sie war in der Leber etwa 90 x größer als in Fettzellen. Bei den fettsüchtigen Tieren war die GK altersabhängig; sie lag in Fettzellen 2–12 Monate alter Tiere und in der Leber 5 Monate alter Tiere um ein Vielfaches über den Kontrollen. In Fettzellen von 2–12 Monate alten, ad libitum gefütterten Tieren korrelierte die Enzymaktivität signifikant zum Seruminsulinspiegel. — Bei Nahrungskarenz oder bei experimenteller Senkung des Insulinspiegels durch Streptozotocin war die Glycerokinaseaktivität vermindert. Sie wurde durch Insulinsubstitutionin vivo gesteigert. Dieser Insulineffekt konnte durch Actinomycin D gehemmt werden. Es wird angenommen, daß Insulin die Glycerokinaseaktivität durch Enzyminduktion reguliert. — Die Bedeutung der Befunde für den Fettgewebsstoffwechsel der obob-Maus wird besprochen.
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Koschinsky, T., Gries, F.A. & Herberg, L. Regulation of glycerol kinase by insulin in isolated fat cells and liver of Bar Harbor Obese Mice. Diabetologia 7, 316–322 (1971). https://doi.org/10.1007/BF01219464
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DOI: https://doi.org/10.1007/BF01219464