Streptozotocin-induced diabetes influences the activity of ecto-nucleoside triphosphate diphosphohydrolase 1 of rat osseous plate membranes
We report the kinetic characterization of an ecto-nucleosidetriphosphate diphosphohydrolase 1 from rat osseous plate membranes in streptozotocin-induced diabetic rats, which arises during ectopic mineralization twenty days after a subcutaneous implantation of demineralized bone matrix, Insulin defic...
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Published in | Molecular and cellular biochemistry Vol. 267; no. 1-2; pp. 99 - 106 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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Springer Nature B.V
01.12.2004
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Abstract | We report the kinetic characterization of an ecto-nucleosidetriphosphate diphosphohydrolase 1 from rat osseous plate membranes in streptozotocin-induced diabetic rats, which arises during ectopic mineralization twenty days after a subcutaneous implantation of demineralized bone matrix, Insulin deficiency decreased the ecto-nucleoside triphosphate diphosphohydrolase activity from 1293.1 +/- 39.8 (control rats) to 556.0 +/- 8.2 nmol Pi/(min mg). Two families of ATP hydrolyzing sites showed cooperative effects with specific activities of 256.2 +/- 7.7 nmol Pi/(min mg) and 299.8 +/- 8.9 nmol Pi/(min mg), and studies on the stimulation of the enzyme by magnesium and calcium ions showed that the decrease in enzyme activity results from changes in the affinity of the enzyme for these ions. To our knowledge this is the first study associating the effects of type I diabetes with an ecto-nucleoside triphosphate diphosphohydrolase activity from rat osseous plate membranes. |
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AbstractList | We report the kinetic characterization of an ecto-nucleosidetriphosphate diphosphohydrolase 1 from rat osseous plate membranes in streptozotocin-induced diabetic rats, which arises during ectopic mineralization twenty days after a subcutaneous implantation of demineralized bone matrix, Insulin deficiency decreased the ecto-nucleoside triphosphate diphosphohydrolase activity from 1293.1 ± 39.8 (control rats) to 556.0 ± 8.2 nmol Pi/(min mg). Two families of ATP hydrolyzing sites showed cooperative effects with specific activities of 256.2 ± 7.7 nmol Pi/(min mg) and 299.8 ± 8.9 nmol Pi/(min mg), and studies on the stimulation of the enzyme by magnesium and calcium ions showed that the decrease in enzyme activity results from changes in the affinity of the enzyme for these ions. To our knowledge this is the first study associating the effects of type I diabetes with an ecto-nucleoside triphosphate diphosphohydrolase activity from rat osseous plate membranes. (Mol Cell Biochem 267: 99-106, 2004)[PUBLICATION ABSTRACT] We report the kinetic characterization of an ecto-nucleosidetriphosphate diphosphohydrolase 1 from rat osseous plate membranes in streptozotocin-induced diabetic rats, which arises during ectopic mineralization twenty days after a subcutaneous implantation of demineralized bone matrix, Insulin deficiency decreased the ecto-nucleoside triphosphate diphosphohydrolase activity from 1293.1 +/- 39.8 (control rats) to 556.0 +/- 8.2 nmol Pi/(min mg). Two families of ATP hydrolyzing sites showed cooperative effects with specific activities of 256.2 +/- 7.7 nmol Pi/(min mg) and 299.8 +/- 8.9 nmol Pi/(min mg), and studies on the stimulation of the enzyme by magnesium and calcium ions showed that the decrease in enzyme activity results from changes in the affinity of the enzyme for these ions. To our knowledge this is the first study associating the effects of type I diabetes with an ecto-nucleoside triphosphate diphosphohydrolase activity from rat osseous plate membranes. We report the kinetic characterization of an ecto-nucleosidetriphosphate diphosphohydrolase 1 from rat osseous plate membranes in streptozotocin-induced diabetic rats, which arises during ectopic mineralization twenty days after a subcutaneous implantation of demineralized bone matrix, Insulin deficiency decreased the ecto-nucleoside triphosphate diphosphohydrolase activity from 1293.1 c 39.8 (control rats) to 556.0 c 8.2 nmol Pi/(min mg). Two families of ATP hydrolyzing sites showed cooperative effects with specific activities of 256.2 c 7.7 nmol Pi/(min mg) and 299.8 c 8.9 nmol Pi/(min mg), and studies on the stimulation of the enzyme by magnesium and calcium ions showed that the decrease in enzyme activity results from changes in the affinity of the enzyme for these ions. To our knowledge this is the first study associating the effects of type I diabetes with an ecto-nucleoside triphosphate diphosphohydrolase activity from rat osseous plate membranes. (Mol Cell Biochem 267: 99-106, 2004) We report the kinetic characterization of an ecto-nucleosidetriphosphate diphosphohydrolase 1 from rat osseous plate membranes in streptozotocin-induced diabetic rats, which arises during ectopic mineralization twenty days after a subcutaneous implantation of demineralized bone matrix, Insulin deficiency decreased the ecto-nucleoside triphosphate diphosphohydrolase activity from 1293.1 plus or minus 39.8 (control rats) to 556.0 plus or minus 8.2 nmol Pi/(min mg). Two families of ATP hydrolyzing sites showed cooperative effects with specific activities of 256.2 plus or minus 7.7 nmol Pi/(min mg) and 299.8 plus or minus 8.9 nmol Pi/(min mg), and studies on the stimulation of the enzyme by magnesium and calcium ions showed that the decrease in enzyme activity results from changes in the affinity of the enzyme for these ions. To our knowledge this is the first study associating the effects of type I diabetes with an ecto-nucleoside triphosphate diphosphohydrolase activity from rat osseous plate membranes. (Mol Cell Biochem 267: 99-106, 2004) |
Author | Petenusci, Sergio O Leone, Francisco A Rezende, Adriana A Furriel, Rosa P M |
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SubjectTerms | Adenosine Triphosphatases - metabolism Animals Calcium - pharmacology Diabetes Diabetes Mellitus, Experimental - metabolism Enzymatic activity Growth Plate - enzymology Insulin - deficiency Ions Kinetics Magnesium Magnesium - pharmacology Male Mineralization Rats Rats, Wistar Rodents |
Title | Streptozotocin-induced diabetes influences the activity of ecto-nucleoside triphosphate diphosphohydrolase 1 of rat osseous plate membranes |
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