adenosine-kinase has been researched along with Diabetes-Mellitus* in 2 studies
1 review(s) available for adenosine-kinase and Diabetes-Mellitus
| Article | Year |
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Adenosine kinase and cardiovascular fetal programming in gestational diabetes mellitus.
Gestational diabetes mellitus (GDM) is a detrimental condition for human pregnancy associated with endothelial dysfunction and endothelial inflammation in the fetoplacental vasculature and leads to increased cardio-metabolic risk in the offspring. In the fetoplacental vasculature, GDM is associated with altered adenosine metabolism. Adenosine is an important vasoactive molecule and is an intermediary and final product of transmethylation reactions in the cell. Adenosine kinase is the major regulator of adenosine levels. Disruption of this enzyme is associated with alterations in methylation-dependent gene expression regulation mechanisms, which are associated with the fetal programming phenomenon. Here we propose that cellular and molecular alterations associated with GDM can dysregulate adenosine kinase leading to fetal programming in the fetoplacental vasculature. This can contribute to the cardio-metabolic long-term consequences observed in offspring after exposure to GDM. Topics: Adenosine; Adenosine Kinase; Animals; Cardiovascular System; Diabetes Mellitus; Diabetes, Gestational; DNA Methylation; Endothelium; Epigenomics; Female; Fetal Development; Gene Expression Regulation; Humans; Inflammation; Mice; Placenta; Pregnancy | 2020 |
1 other study(ies) available for adenosine-kinase and Diabetes-Mellitus
| Article | Year |
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Expression level of adenosine kinase in rat tissues. Lack of phosphate effect on the enzyme activity.
In this report we describe cloning and expression of rat adenosine kinase (AK) in Esccherichaia coli cells as a fusion protein with 6xHis. The recombinant protein was purified and polyclonal antibodies to AK were generated in rabbits. Immunoblot analysis of extracts obtained from various rat tissues revealed two protein bands reactive with anti-AK IgG. The apparent molecular mass of these bands was 48 and 38 kDa in rat kidney, liver, spleen, brain, and lung. In heart and muscle the proteins that react with AK antibodies have the molecular masses of 48 and 40.5 kDa. In order to assess the relative AK mRNA level in rat tissues we used the multiplex PCR technique with beta-actin mRNA as a reference. We found the highest level of AK mRNA in the liver, which decreased in the order kidney > spleen > lung > heart > brain > muscle. Measurement of AK activity in cytosolic fractions of rat tissues showed the highest activity in the liver (0.58 U/g), which decreased in the order kidney > spleen > lung > brain > heart > skeletal muscle. Kinetic studies on recombinant AK as well as on AK in the cytosolic fraction of various rat tissues showed that this enzyme is not affected by phosphate ions. The data presented indicate that in the rat tissues investigated at least two isoforms of adenosine kinase are expressed, and that the expression of the AK gene appears to have some degree of tissue specificity. Topics: Adenosine Kinase; Animals; Cloning, Molecular; Cytosol; Diabetes Mellitus; Gene Expression Profiling; Kinetics; Organ Specificity; Phosphates; Polymerase Chain Reaction; Rats; RNA, Messenger | 2001 |