Electron cytochemical studies on an NAD(P)H-dependent H2O2-generating enzyme activity in the rat small intestine.

Ishikawa, Yoshimaro; Hirai, Kei-Ichi; Ogawa, Kazuo

doi:10.1267/ahc.14.727

Cited by 12 publications

(6 citation statements)

References 8 publications

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“…the thyroid gland (19), the liver (18,30), the small intestine (14), the uterus (15) and the kidney (2). It has been suggested that several H2O2 generating oxidases may be involved in H2O2 generation in these epithelial tissues, such as NAD(P)H oxidase on the plasma membrane (14,15,18,19) or D-amino acid oxidase in peroxisome (30). In the rat parotid gland, Hand (13) reported the presence of peroxisome by catalase cytochemistry.…”

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confidence: 99%

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Reaction Sites by Cerium-Cytochemistry for the Hydrogen-Peroxide Generating Enzymes in the Mongolian Gerbil Parotid Gland.

Miyazaki

Takano

1993

Acta Histochem. Cytochem

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In order to cytochemically demonstrate the endogenous glandular source of hydrogen-peroxide (H2O2), which is a component of the salivary peroxidase antimicrobial system, we applied the cerium method to the Mongolian gerbil parotid gland. When NADH and NADPH were used as substrates of the H2O2 generating enzyme, reaction products were observed in association with the plasma membrane and pinocytotic vesicles of the myoepithelial cell. No reaction product was formed in the absence of these substrates. The reaction was inhibited by the addition to the complete medium of catalase (H2O2 scavenger) or of p-benzoquinone (O2-scavenger), or by heating prior to incubation. These results suggest that NADH-and NADPH-dependent H2O2 generating oxidase may be present in the myoepithelial cell. In addition, electron-dense precipitates, formed by the reaction of cerous ions, were also observed on the outer surface of the luminar plasma membrane of acinar and intercalated duct cells, and in the cristae and outer compartment of mitochondria mainly of duct cells. However, these reaction products were formed whether the substrates were contained in the cerium medium or not. Since the reaction was also weakened by catalase or p-benzoquinone, or by preheating, it is likely that some endogenous H2O2-generating factors, independent bf the exogenous substrates, may exist in these sites.

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“…the thyroid follicular cell (19), the epithelial cell of the endometrium (15), the hepatocyte, and the absorptive cell of the duodeno-jejunum (14). It has been suggested that it is involved in the biosynthesis of thyroid hormone (9) and of estradiol (16), and also in antimicrobial actions, and in the control of transport system.…”

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confidence: 99%

Reaction Sites by Cerium-Cytochemistry for the Hydrogen-Peroxide Generating Enzymes in the Mongolian Gerbil Parotid Gland.

Miyazaki

Takano

1993

Acta Histochem. Cytochem

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“…A glutaraldehyde-insensitive, NAD(P)H-dependent H2O2-generating enzyme activity in the rat small intestine and its regional differences in the small intestine of the adult rat have been described previously by us (5,6). In the present investigation the postnatal changes of this enzyme activity in the small intestine were studied using 1-day to 6-months old male Kyo-Wistar rats.…”

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confidence: 70%

Postnatal changes in the localization of small intestinal NAD(P)H-dependent H2O2-generating enzyme activity in the rat.

Ishikawa

Hirai

Ogawa

1982

Acta Histochem. Cytochem

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A glutaraldehyde-insensitive, NAD(P)H-dependent H2O2-generating enzyme activity in the rat small intestine and its regional differences in the small intestine of the adult rat have been described previously by us (5, 6). In the present investigation the postnatal changes of this enzyme activity in the small intestine were studied using 1-day to 6-months old male Kyo-Wistar rats.It was found in this study that the NAD(P)H-dependent H2O2-generating enzyme activity showed a marked postnatal change.The enzyme activity was significantly higher in the apical membrane of absorptive cells of both duodenojejunum and ileum in newborn rats, however the activity in the apical membrane of the ileum was decreased from the 7th postnatal day on, reaching eventually to an extremely weak activity in the adult.The activity in the apical membrane of the duodeno jejunum remained the same throughout the course of growth.These findings are discussed in connection with the postnatal changes in absorptive function.Our previous papers (5, 6) have described that a glutaraldehyde-insensitive NAD (P) H-dependent H202-generating enzyme activity is localized in the rat duodeno jejunal mucosa. The localization of the activity is limited on the apical membranes of differentiated absorptive cells and goblet cells when generated H202 is electron-cytochemically demonstrated by means of Briggs' cerium method (1). The ileum also showed an H202-generating activity, but the intensity was much weaker than that of the duodeno jejunum (6).In the present paper, we have investigated the postnatal changes of the H202-generating enzyme activity which is dependent on NADH in the rat small intestine. MATERIALS AND METHODSMale Kyo-Wistar rats, 1-day old newborn to 6-months old, were fasted 24 hr and killed by bleeding. Duodeno jejunum from the portion of 3 cm anal to the pyloric ring, and ileum from the portion of 3 cm oral to the ileum end were dissected out. The tissues were cut into fragments of 0.5 mm squares and fixed for 10 min 372

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“…For example, the plasma membrane-bound NADPH oxidase system is well known to be essential for the microbicidal activity in leukocytes [23] or for the biosynthesis of thyroid hormones in thyroid follicular cells [5]. Similar membrane-bound NAD(P)H oxidase systems have also been recognized in several epithelial cells [9,10,15], fibroblasts [11], osteoclasts [22], endothelial cells [16] and smooth muscle cells [7]. The existence of the NAD(P)H oxidase system in smooth muscle cells is interesting to us because MEC have been shown to share many features with smooth muscle cells [6,20].…”

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“…Also, NAD(P)H oxidase has been known to localize on the plasma membranes of several epithelial cells, e.g., the thyroid follicular cells [3], the epithelial cells of the endometrium [10], the hepatocytes [15], and the absorptive cells of the duodeno-jejunum [9]. In the thyroid follicular cells, NADPH oxidase is known to be involved in the biosynthesis of thyroid hormone [5].…”

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Cytochemical Localization of NAD(P)H Oxidase in the Myoepithelial Cells of Salivary and Other Exocrine Glands.

Miyazaki

Inoue

Takano

1995

Acta Histochem. Cytochem

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Electron cytochemical studies on an NAD(P)H-dependent H2O2-generating enzyme activity in the rat small intestine.

Cited by 12 publications

References 8 publications

Reaction Sites by Cerium-Cytochemistry for the Hydrogen-Peroxide Generating Enzymes in the Mongolian Gerbil Parotid Gland.

Reaction Sites by Cerium-Cytochemistry for the Hydrogen-Peroxide Generating Enzymes in the Mongolian Gerbil Parotid Gland.

Postnatal changes in the localization of small intestinal NAD(P)H-dependent H2O2-generating enzyme activity in the rat.

Cytochemical Localization of NAD(P)H Oxidase in the Myoepithelial Cells of Salivary and Other Exocrine Glands.

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