An ultracytochemical study of cytochrome oxidase activity in rat metaphyseal bone cells.

Yamamoto, Tetsuro; Nagai, Hiroshi

doi:10.1267/ahc.24.411

Cited by 2 publications

(1 citation statement)

References 25 publications

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“…The activity of cytochrome c oxidase was also investigated, since osteoclasts contain a large number of mitochondria and the activity of cytochrome c oxidase in osteoclasts has been reported to increase when these cells are actively resorbing bone (Noda et al, 1985;Yamamoto et al, 1991). To localize cytochrome c oxidase activity, the original DAB method without Mn 2÷ was used (Seligman et al, 1968).…”

Section: Discussionmentioning

confidence: 99%

NADPH-oxidase expression and in situ production of superoxide by osteoclasts actively resorbing bone.

Steinbeck

Appel

Verhoeven

et al. 1994

The Journal of Cell Biology

159

109

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Abstract. Recent reports have suggested that production of superoxide or other reactive oxygen species by activated osteoclasts may play a role in the complex process of bone resorption; however, the enzyme responsible for production of superoxide by osteoclasts has not been characterized. To determine if osteoclasts express NADPH-oxidase, a superoxide-generating enzyme found in phagocytic leukocytes, immunohistochemical studies were performed on tibia from 1-5-d-old rats using mAbs 449 and 48 and an antiserum specific for p47-phox. These antibodies recognize epitopes on the et and/3 subunits of cytochrome b558, respectively, and the p47 cytosolic component of NADPH-oxidase. We found that osteoclasts attached to bone surfaces in tibia expressed all three components, as did mature polymorphonuclear and some mononuclear leukocytes in the bone marrow. In many adherent osteoclasts, the cytochrome b55s subunits were localized to the ruffled-border and bone interfaces. Studies were also performed on mature rat tibia that had undergone controlled fracture. By two weeks the healing fractures develop a callus rich in actively resorbing osteoclasts. Osteoclasts within the calluses, and attached to bone surface, also expressed the cytochrome b558 proteins. In addition to demonstrating the expression of NADPH-oxidase, the active production of superoxide by osteoclasts was also demonstrated in situ in freshly isolated tibia using 3,3'-diaminobenzidine (DAB)-Mn 2+, a histochemical method specific for superoxide localization. Osteoclasts attached to bone surfaces contained deposits of oxidized DAB which were observed by light microscopy. Nonstimulated polymorphonuclear and mononuclear leukocytes in the bone marrow did not contain DAB deposits unless stimulated with phorbol myristate acetate, a known activator of NADPH-oxidase. These findings indicate that osetoclasts contain NADPH-oxidase, and during the process of resorbing bone, are actively producing superoxide.ESORPTION of bone by activated osteoclasts is well documented; however, how osteoclasts are formed and activated or the mechanisms by which bone is resorbed by osteoclasts remain unclear. Bone resorption is a complex process that involves the differentiation of precursor cells to osteoclasts, the release of mineral from bone and degradation of the proteinaceous bone matrix. Recent reports have suggested that the production of superoxide or other reactive oxygen species (ROSy by activated osteoclasts play a role in the complex process of bone resorption Animals used in this study were maintained and manipulated in accordance with the guidelines of the Committee on Animals of the Harvard Medical School and those prepared by the Committee on Care and Use

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Section: Discussionmentioning

confidence: 99%

NADPH-oxidase expression and in situ production of superoxide by osteoclasts actively resorbing bone.

Steinbeck

Appel

Verhoeven

et al. 1994

The Journal of Cell Biology

159

109

View full text Add to dashboard Cite

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Effects of development and altered gravity conditions on cytochrome oxidase activity in a vestibular nucleus of the larval teleost brain: A quantitative electronmicroscopical study

Paulus¹,

Körtje²,

Rahmann³

1993

J. Neurobiol.

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The mitochondrial enzyme, cytochrome oxidase, was localized cytochemically in the nucleus magnocellularis, a primary relay nucleus of vestibular information within the area octavolateralis in the fish brain. Larvae of the cichlid fish Oreochromis mossambicus were analyzed at different developmental stages (4, 10, and 35 days post-hatching) and after long-term exposure (8 days) to increased gravity (2-4 g). Quantification of highly reactive, moderately reactive, and nonreactive mitochondria reveals differences in the cytochrome oxidase activity of various cellular structures, for example, perikarya of neurons, presynaptic terminals, and myelinated and nonmyelinated cell profiles. Cytochrome oxidase activity in the mitochondria of neuronal perikarya increases during development which parallels the differentiation of the area octavolateralis. This possibly reflects the increasing energy demand during maturation and innervation of the magnocellular nucleus. Hyper-g-exposure of the larvae for 8 days (centrifuge) caused a further augmentation of cytochrome oxidase activity in the perikarya within the nucleus magnocellularis. This may reflect an increased oxidative metabolism resulting from the need for compensation of altered inputs from gravity-sensitive epithelia in the inner ear. Another possibility is that acceleration within a centrifuge causes physiological stress for the animals and, therefore, influences the cytochrome oxidase activity in neurons.

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An ultracytochemical study of cytochrome oxidase activity in rat metaphyseal bone cells.

Cited by 2 publications

References 25 publications

NADPH-oxidase expression and in situ production of superoxide by osteoclasts actively resorbing bone.

NADPH-oxidase expression and in situ production of superoxide by osteoclasts actively resorbing bone.

Effects of development and altered gravity conditions on cytochrome oxidase activity in a vestibular nucleus of the larval teleost brain: A quantitative electronmicroscopical study

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