Localization of a cytochrome P-450 isozyme (cytochrome P-450 PB-B) and NADPH-cytochrome P-450 reductase in rat nasal mucosa

Voigt, Jeffrey M.; Guengerich, F. Peter; Baron, Jeffrey

doi:10.1016/0304-3835(85)90180-6

Cited by 73 publications

(26 citation statements)

References 7 publications

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“…Non-ciliated cuboidal cells of the transitional epithelium, which were not investigated in this study, have also been reported to contain significant amounts of cytochrome P450 lAl (33). In contrast, cytochrome P450 2B1, the major form of cytochrome P-450 induced in hepatic microsomes by phenobarbital, and NADPH-cytochrome P450 reductase were previously found to be distributed quite uniformly throughout the epithelia and glands of both the olfactory and respiratory regions in untreated rats (20). It is therefore apparent that A,C,E,G) Olfactory regions; (B,D,F,H) respiratory regions.…”

Section: Discussionmentioning

confidence: 62%

“…After rats were decapitated, the nasal septum and dorsal turbinates were removed, faed at 4'C in a solution consisting of 1% acetic acid in 95% ethanol, and processed as previously described (20). Cytochrome P450 1Al was localized at the light microscopic level in paraffin sections of the nasal mucosa by means of immunoperoxidase (avidin-biotin-peroxidase) (30) as well as immunofluorescence (avihn-fluorescein kothigranate) (31) staining.…”

Section: Methodsmentioning

confidence: 99%

“…Characterization of the enzymatic capabilities of individual cell types in situ can be accomplished through the use of immunohistochemical and histochemical techniques. Previously, NADPH-cytochrome P450 reductase and cytochrome P450 2B1 (see 19 for nomenclature) were found to be localized in epithelial cells and Bowman's glands in the olfactory region and in epithelial cells and seromucous glands in the respiratory region of untreated rats (20), whereas cytochrome P450 1Al (21) and an olfactory-specific UDP-glucuronosyltransferase (22) were found in the olfactory epithelium and Bowman's glands of untreated rats. In the present study, the localization and distribution of cytochrome P450 1Al were investigated immunohistochemically in the nasal mucosa of untreated and xenobiotic-pre-treated rats.…”

Section: Introductionmentioning

confidence: 99%

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Localization and induction of cytochrome P450 1A1 and aryl hydrocarbon hydroxylase activity in rat nasal mucosa.

Voigt

Guengerich²,

Baron³

1993

J Histochem Cytochem.

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Cytochrome P450 1A1 was localized immunohistochemically and benzo[a]pyrene hydroxylase activity was identified in situ by means of fluorescence histochemistry in the nasal mucosa of untreated, 3-methylcholanthrene-treated or Aroclor 1254-treated rats. Cytochrome P450 1A1 was localized predominantly within Bowman's glands, with considerably less staining occurring in the olfactory epithelium of untreated rats. Similarly, benzo[a]pyrene was hydroxylated to the greatest extent in Bowman's glands and, to a lesser extent, in olfactory epithelial cells. Pre-treatment of tissue sections of nasal mucosa with anti-P450 1A1 inhibited most of the benzo[a]pyrene hydroxylase activity present. Although 3-methylcholanthrene treatment did not affect either cytochrome P450 1A1 or hydroxylase activity in the nasal mucosa, a single intraperitoneal injection of Aroclor 1254 significantly increased anti-P450 1A1 binding in Bowman's glands and in the olfactory and respiratory epithelia, and dramatically enhanced benzo[a]pyrene hydroxylase activity in the epithelia and the subepithelial ducts and glands in both the olfactory and respiratory regions. In contrast to its effects on cytochrome P450 1A1, Aroclor 1254 produced a considerably greater induction of hydroxylase activity in the respiratory region, especially in the seromucous glands, than in the olfactory region. These results suggest that Aroclor 1254 treatment also induces other forms of cytochrome P450 in the respiratory region of the nasal mucosa.

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Section: Discussionmentioning

confidence: 62%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Localization and induction of cytochrome P450 1A1 and aryl hydrocarbon hydroxylase activity in rat nasal mucosa.

Voigt

Guengerich²,

Baron³

1993

J Histochem Cytochem.

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“…In all studies the antibody has been raised against purified rat hepatic cytochrome P-450 and, therefore, recognizes antigens in nasal mucosa of immunochemical similarity to those in liver. The phenobarbital-inducible isozyme of cytochrome P-450 and NADPH-cytochrome P-450 reductase and the P-naphthoflavone-inducible form of P-450 have been studied (52)(53)(54). The pattern of enzyme distribution for both P-450 isozymes is similar to that for NBE and parallels the distribution of covalently bound radiolabeled compounds known to be metabolized to reactive products by cytochrome P-450.…”

Section: Metabolism Of P-450 Substratesmentioning

confidence: 89%

Biotransformation Enzymes in the Rodent Nasal Mucosa: The Value of a Histochemical Approach

Bogdanffy¹

1990

Environmental Health Perspectives

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An increasing number of chemicals have been identified as being toxic to the nasal mucosa of rats. While many chemicals exert their effects only after inhalation exposure, others are toxic following systemic administration, suggesting that factors other than direct deposition on the nasal mucosa may be important in mechanisms of nasal toxicity. The mucosal lining of the nasal cavity consists of a heterogeneous population of ciliated and nonciliated cells, secretory cells, sensory cells, and glandular and other cell types. For chemicals that are metabolized in the nasal mucosa, the balance between metabolic activation and detoxication within a cell type may be a key factor in determining whether that cell type will be a target for toxicity. Recent research in the area of xenobiotic metabolism in nasal mucosa has demonstrated the presence of many enzymes previously described in other tissues. In particular, carboxylesterase, aldehyde dehydrogenase, cytochromes P-450, epoxide hydrolase, and glutathione S-transferases have been localized by histochemical techniques. The distribution of these enzymes appears to be cell-type-specific and the presence of the enzyme may predispose particular cell types to enhanced susceptibility or resistance to chemical-induced injury. This paper reviews the distribution of these enzymes within the nasal mucosa in the context oftheir contribution to xenobiotic metabolism. The localization of the enzymes by histochemical techniques has provided important information on the potential mechanism of action of esters, aldehydes, and cytochrome P-450 substrates known to injure the nasal mucosa.

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“…Cytochrome P-450 associated monooxygenase activity has been demonstrated in human alveolar type II cells (Devereux et al, 1986) and colonic epithelium (Autrup et al, 1982;Cohen et al, 1983). Cytochrome P-450 has been shown in human adrenal gland, placenta, breast and prostate gland (Chung et al, 1987;Mendelson et al,1985;Baron et al, 1983), in rat olfactory epithelium and rat and rabbit nasal epithelium (Reed etal., 1986;Foster et al, 1986;Ding et al, 1986;Voigt et al, 1985) and in rat brain (Haglund et al, 1984;Walker et al, 1986). The absence of immunostaining by MAb-HL3 in tissues which have been reported to contain cytochrome P-450 suggests that these tissues contain forms of cytochrome P-450 different from that (or those) recognised by MAb-HL3.…”

Section: Discussionmentioning

confidence: 99%

The immunocytochemical localisation and distribution of cytochrome P‐ 450 in normal human hepatic and extrahepatic tissues with a monoclonal antibody to human cytochrome P‐450.

Murray

Sewell

et al. 1988

Brit J Clinical Pharma

136

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2ZD, 2Department of Biochemistry and 3Department of Pharmacology, Marischal College, University of Aberdeen AB9 lAS 1 The localisation and distribution of cytochrome P-450 in human tissues has been studied by immunocytochemistry using a monoclonal antibody to a major form of human hepatic cytochrome P-450, P-45OhA7, which is closely related to cytochromes P-450 HLp and P-45ONF. 2 Strong immunoreactivity was identified in hepatocytes, columnar absorptive epithelial cells of the small intestine, polymorphonuclear leucocytes and their precursors in the bone marrow, and in mast cells.3 Weak immunoreactivity was present in the proximal tubules of the kidney, pancreatic acini, gall bladder epithelium, squamous epithelium and sebaceous glands of the skin, interstitial cells of the testis and luteal cells of the ovary. 4 Immunoreactivity could not be demonstrated in the adrenal gland, placenta, colonic epithelium and alveolar type II cells and Clara cells of the lung.

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Localization of a cytochrome P-450 isozyme (cytochrome P-450 PB-B) and NADPH-cytochrome P-450 reductase in rat nasal mucosa

Cited by 73 publications

References 7 publications

Localization and induction of cytochrome P450 1A1 and aryl hydrocarbon hydroxylase activity in rat nasal mucosa.

Localization and induction of cytochrome P450 1A1 and aryl hydrocarbon hydroxylase activity in rat nasal mucosa.

Biotransformation Enzymes in the Rodent Nasal Mucosa: The Value of a Histochemical Approach

The immunocytochemical localisation and distribution of cytochrome P‐ 450 in normal human hepatic and extrahepatic tissues with a monoclonal antibody to human cytochrome P‐450.

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