HISTOLOGY AND HISTOPATHOLOGY

Cellular and Molecular Biology



Review

Distribution and pathophysiologic role of molybdenum-containing enzymes

Y. Moriwaki, T. Yamamoto and K. Higashino

Third Department of Internal Medicine, Hyogo College of Medicine, Nishinomiya, Hyogo, Japan

Offprint requests to: Dr. Yuji Moriwaki, M.D. , Third Department of Internal Medicine, Hyogo College of Medicine, Mukogawa-cho 1-1 , Nishinomiya, Hyogo 663, Japan

 

Summary. The importance of molybdenum-containing enzymes in the pathophysiology of a number of clinical disorders necessitates a comprehensive understanding of their histological localization and expression. The objectives of this review are to cover such enzymes so far reported and their enzyme- and immunohistochemical localization in various tissues and species, and to discuss their possible pathophysiological effects. The molybdenum cofactor is essential for the activity of the three molybdenum-containing enzymes, sulfite oxidase, xanthine oxidase and aldehyde oxidase. Sulfite oxidase serves as the terminal enzyme in the pathway of the oxidative degradation of sulfur amino acids, and is also involved in preventing the toxic effects of sulfur dioxide. Biochemical study has revealed a high activity of sulfite oxidase mainly in the liver, heart and kidney with lesser activity observed in other tissues. Subcellular observations have shown that this enzyme is present in the mitochondrial intermembraneous spaces. Xanthine oxidase is the final enzyme in the conversion of hypoxanthine to xanthine, and subsequently, to uric acid. Unlike sulfite and aldehyde oxidases, xanthine oxidase can be converted to xanthine dehydrogenase, and vice versa. Xanthine oxidase has been widely inves tigated for its role in post- ischemic reperfusion tissue injury. Enzyme- and immunohistochemical studies of its localization in various animal species and ti ssues have shown its ubiquitous di stribution in the liver, small and large intestine, lung and kidney, and other tissues. Aldehyde oxidase shares a similar substrate specificity with xanthine oxidase. Although the ti ssue localization of this enzyme has not been studied as thoroughly as that of xanthine oxidase, aldehyde oxidase is reportedly found in the digestive gland of terrestrial gastropods, the antennae of certain moths as well as the mammalian liver. Recently, the ubiquitous distribution of aldehyde oxidase has been demonstrated in rat tissues. The aldehyde oxidase activity of herbivores exceeds that of carnivores, suggesting a possible role of this enzyme as a protection against the effects of toxic plants. The relationship between the ti ssue localization of these enzymes and their pathophysiological roles is reviewed. Histol Histopathol 12, 513-524 (1997)

 

Key words: Molybdenum-containing enzyme, Sulfite oxidase, Xanthine oxidase, Aldehyde oxidase, Tissue distribution, Histochemistry, Pathophysiology

DOI: 10.14670/HH-12.513