Effect of Iron Lactate Overloading on Adenine Nucleotide Levels and Adenosine 3'-Monophosphate Forming Enzyme in Rat Liver and Spleen(Pharmacology)
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概要
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To elucidate the pathophysiological significance of adenosine 3'-monophosphate (3'-AMP) forming enzyme in rats, the effect of iron lactate overloading on the enzyme activities and adenine nucleotide levels in the liver and spleen was examined. Sprague-Dawley rats were fed a diet supplemented with 0%, 0.625% or 5.0% of iron lactate for 4 weeks. Iron deposition was found in periportal hepatocytes, Kupffer cells and macrophages of red pulp of the spleen. No significant changes in hematological parameters were detected. Although serum alkaline phosphatase and inorganic phosphorus levels elevated slightly in the 5.0% group, activities of alanine aminotransferase and aspartate aminotransferase, and levels of serum urea nitrogen and creatinine were not changed significantly. The ATP levels in the liver and spleen of iron fed groups were significantly decreased, but adenosine 5'-diphosphate (ADP) and adenosine 5'-monophosphate (AMP) levels were within control levels. On the other hand, the levels of ATP, ADP and AMP in the erythrocytes without mitochondria were not suppressed by the iron lactate overloading. Free activity of 3'-AMP forming enzyme, one of ribonucleases (RNase), was not changed in the liver of iron-overloaded rat, and total amount of 3'-AMP and adenosine formed after the treatment of the crude enzyme (s) with p-chloromercuribenzensulfonic acid, a SH blocker of RNase inhibitors, was decreased dose-dependently. On the contrary, free activity of 3'-AMP forming enzyme was enhanced dose-depen-dently in the spleen of iron-overloaded rat but the total activity was not changed. However, the free and total 3'-AMP forming enzyme activities in the liver and spleen of iron-overloaded rats became equal at the dosage of 5.0% of iron lactate. The results obtained suggested that iron loading might induce significant decrease in hepatic and splenic ATP levels via malfunction of their mitochondria and might lead dissociation of RNase-RNase inhibitor complex to activate 3'-AMP forming enzyme in both tissues.
- 社団法人日本薬学会の論文
- 2004-09-01
著者
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PAN-HOU Hidemitsu
Faculty of Pharmaceutical Sciences, Setsunan University
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Pan‐hou H
Setsunan Univ. Osaka Jpn
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OZAKI Kiyokazu
Department of Pathology, Faculty of Pharmaceutical Sciences, Setsunan University
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MATSUURA Tetsuro
Department of Pathology, Faculty of Pharmaceutical Sciences, Setsunan University
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NARAMA Isao
Department of Pathology, Faculty of Pharmaceutical Sciences, Setsunan University
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Narama I
Department Of Pathology Faculty Of Pharmaceutical Sciences Setsunan University
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Narama Isao
Department Of Comparative Pathology Faculty Of Veterinary Medicine Hokkaido University
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Ozaki Kiyokazu
Department Of Pathology Faculty Of Pharmaceutical Sciences Setsunan University
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Ozaki Kiyokazu
Department Of Pathology Faculty Of Pharmaceutical Science Setsunan University
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Pan-hou Hidemitsu
Faculty Of Pharmaceutical Sciences Setsunan University
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Matsuura Tetsuro
Department Of Pathology Faculty Of Pharmaceutical Sciences Setsunan University
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FUJIMORI Hiroyuki
Department of Analytical Chemistry in Hygiene, Faculty of Pharmaceutical Sciences, Setsunan Universi
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MATSUSHIMA Shuuichi
Pathology Section, Drug Safety Evaluation, Developmental Research Laboratories, Shionogi & Co., Ltd.
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PAN-HOU Hidemitsu
Department of Analytical Chemistry in Hygiene, Faculty of Pharmaceutical Sciences, Setsunan Universi
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Narama I
Setsunan Univ. Osaka Jpn
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Fujimori H
Faculty Of Pharmaceutical Sciences Setsunan University
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Matsushima S
Pathology Section Drug Safety Evaluation Developmental Research Laboratories Shionogi & Co. Ltd.
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