Expression of gamma-glutamyl transpeptidase in normal and neoplastic epithelial cells of human skin: a marker for distinguishing malignant epithelial tumours

Chiba, M; Jimbow, Kowichi

doi:10.1111/j.1365-2133.1986.tb02850.x

Cited by 15 publications

(11 citation statements)

References 16 publications

(10 reference statements)

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“…It is well documented in previous studies that cells or tissues during the course of tumorigenesis demonstrate a variety of phenotypical alterations by losing their normal expression and by newly acquiring an unusual or fetal nature (2,3,10,18,20,24,25). Since it is commonly observed that differentiation in function in neoplasms is retarded with frequent reappearance of fetal or embryonic phenotypes, the fetalism theory of neoplasms was proposed by early investigators to explain such phenomena (6).…”

Section: Discussionmentioning

confidence: 99%

“…

The present study was undertaken to investigate the precise correlation in the localization patterns between both enzymes by alternate detection of their activity in serial tissue sections from various stages of carcinogenesis.

MATERIALS AND METHODS

Animals Twenty adult male Wistar strain rats of 100-150 g in body weight were injected subcutaneously with DIPN (diisopropanolnitrosamine, Nakarai Chemical Co.) at a dose of 750 mg per kg body weight weekly for 10 weeks.

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mentioning

confidence: 99%

“…It is generally accepted that phenotypical alteration occurs in cells and tissues during carcinogenesis of various origins in association with functional retardation and elevated growth activity (2,3,10,18,20,24,25).…”

mentioning

confidence: 99%

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Inverse correlation between thyroid peroxidase(TPO) and gamma-glutamyl transpeptidase(GGT) activities expressed in diisopropanolnitrosamine(DIPN) induced rat thyroid lesions. An enzyme histochemical study.

Yamamoto

Kato

Matsumoto

et al. 1988

Acta Histochem. Cytochem

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The histochemical localization of thyroid peroxidase (TPO) and gammaglutamyl transpeptidase (GGT) in diisopropanolnitrosamine (DIPN) induced rat thyroid lesions was examined.The former was utilized as a marker of the endocrine function of the follicular epithelium and the latter as that of neoplastic growth.The two enzymes revealed an inverse correlation in their patterns of localization, i.e., TPO was positive in most of the benign nodular lesions and negative in malignant nodules, while GGT was positive in the nodules or areas of nodules which were negative for TPO.It is generally accepted that phenotypical alteration occurs in cells and tissues during carcinogenesis of various origins in association with functional retardation and elevated growth activity (2,3,10,18,20,24,25).In the thyroid gland, the activity of thyroid peroxidase (TPO), an essential enzyme of endocrine function (15), is known to decrease or to disappear during the course of tumorigenesis (4, 24). On the other hand, gamma-glutamyl transpeptidase (GGT) which is detected normally in the rat thyroid gland in the early stage of the fetal period, comes to be expressed in the malignant type of diisopropanolnitrosamine (DIPN) induced-rat thyroid lesions (12, 13).The present study was undertaken to investigate the precise correlation in the localization patterns between both enzymes by alternate detection of their activity in serial tissue sections from various stages of carcinogenesis. MATERIALS AND METHODSAnimals Twenty adult male Wistar strain rats of 100-150 g in body weight were injected subcutaneously with DIPN (diisopropanolnitrosamine, Nakarai Chemical Co.) at a dose of 750 mg per kg body weight weekly for 10 weeks. As controls, five rats were prepared and were injected with PBS (phosphate buffered saline) in the same manner. After the final injection, animals were sacrificed weekly by cardiac bleeding, 455

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Section: Discussionmentioning

confidence: 99%

“…

MATERIALS AND METHODS

…”

mentioning

confidence: 99%

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Inverse correlation between thyroid peroxidase(TPO) and gamma-glutamyl transpeptidase(GGT) activities expressed in diisopropanolnitrosamine(DIPN) induced rat thyroid lesions. An enzyme histochemical study.

Yamamoto

Kato

Matsumoto

et al. 1988

Acta Histochem. Cytochem

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“…5B; Rutenburg et al 1969;De Young et al 1978). Hair follicles, which are known to have active gGT in the anagen phase, served as internal positive control (Chiba and Jimbow 1986).…”

Section: Nrf2 Controls a Gsh Biosynthesis/recycling Pathway In The Mumentioning

confidence: 99%

Nrf2 establishes a glutathione-mediated gradient of UVB cytoprotection in the epidermis

Schäfer¹,

Dütsch²,

Keller³

et al. 2010

Genes Dev.

148

165

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Ultraviolet (UV) B irradiation can severely damage the skin and even induce tumorigenesis. It exerts its effects by direct DNA modification and by formation of reactive oxygen species (ROS). We developed a strategy to genetically activate target gene expression of the transcription factor NF-E2-related factor 2 (Nrf2) in keratinocytes in vivo based on expression of a constitutively active Nrf2 mutant. Activation of Nrf2 target genes strongly reduced UVB cytotoxicity through enhancement of ROS detoxification. Remarkably, the protective effect was extended to neighboring cells. Using different combinations of genetically modified mice, we demonstrate that Nrf2 activates the production, recycling, and release of glutathione and cysteine by suprabasal keratinocytes, resulting in protection of basal cells in a paracrine, glutathione/cysteine-dependent manner. Most importantly, we found that endogenous Nrf2 controls selective protection of suprabasal keratinocytes from UVB-induced apoptosis through activation of cytoprotective genes. This finding explains the preferential UVB-induced apoptosis of basal cells, which is important for elimination of mutated stem cells as well as for preservation of skin integrity. Taken together, our results identify Nrf2 as a key regulator in the UV response of the skin.[Keywords: Apoptosis; Nrf2; UVB; reactive oxygen species; glutathione] Supplemental material is available at http://www.genesdev.org.

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“…(Fiala et at., 1972;Novogrodsky et at., 1976;Mohandas et at., 1984;Chen & ' d p,,.~~~~Haskill, 1984;Chiba & Jimbow, 1986). In melanoma this enzyme has been suggested to convert glutathione-dopa to 5-s-cysteinyldopa Mojamdar et at., 1982).…”

Section: Resultsmentioning

confidence: 99%

Biochemical and ultrastructural alterations accompany the anti-proliferative effect of butyrate on melanoma cells

Nordenberg¹,

Wasserman²,

Peled³

et al. 1987

Br J Cancer

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Summary The effect of sodium butyrate on mouse and human melanoma cell lines was evaluated. Sodium butyrate (0.1-2mM) is shown to reduce the clonogenic potential of several melanoma cell lines. The antiproliferative effect of sodium butyrate is accompanied by a marked increase in the activity of the plasmamembrane bound enzyme y-glutamyl transpeptidase. Sodium butyrate treated cells acquire a well developed rough endoplasmic reticulum and accumulate fat droplets. The development of the endoplasmic reticulum is associated with a marked increase in the activity of the enzyme marker NADPH cytochrome c reductase. It is suggested that the phenotypic alterations induced by sodium butyrate may serve as markers for the action of this agent on melanoma cells and other tumours.Butyric acid, a natural four carbon fatty acid, is known as an inducer of differentiation in Friend erythroleukaemic cells (Leder & Leder, 1975;Reeves & Cserjesi, 1979). In vivo application of sodium butyrate to a child with acute myelogenous leukaemia resulted in a partial remission (Novogrodsky et al., 1983).Butyric acid (or its sodium salt) also induce phenotypic alterations in a variety of solid tumour cell lines such as Hela cells (Fishman et al., 1974;Gosh & Cox, 1976), neuroblastoma (Prasad, 1979;Rama & Prasad, 1984), breast cancer cells (Abe & Kufe, 1984;Stevens et al., 1984, colorectal carcinoma (Dexter et al., 1981;Kim et al., 1980; Hertz & Halwer, 1982) and retinoblastoma (Kyritsis et al., 1984). The anti-tumour effects of sodium butyrate that include growth inhibition and decrease in tumorigenicity (for review see Prasad, 1980; Wright, 1973;Leavitt et al., 1978;Reese et al., 1985; Nordenberg et al., 1986a, b) are accompanied by changes in enzyme activities (Simmons et al., 1975;Prasad, 1980;Dexter et al., 1981;Prager & Kanar, 1984), receptor content (Fishman & Atikkan, 1979;Jahangeer et al., 1982) and histone structure (Sealy & Chulkley, 1978;Rubenstein et al., 1979).We have recently shown that sodium butyrate markedly inhibits B 16 mouse melanoma cell growth and alters the morphologic appearance of these cells. Growth inhibition was accompanied by a marked inhibition of tyrosinase activity (Nordenberg et al., 1986a).In the present study we further evaluate the effects of sodium butyrate on mouse melanoma cells and expand our studies to human malignant melanoma cells. Sodium butyrate is shown to inhibit clonogenicity of the different melanoma cells in soft agar. This anti-proliferative effect of sodium butyrate is associated with a marked increase in the activities of the plasma membrane bound enzyme y-glutamyl transpeptidase and NADPH cytochrome c reductase, a marker of the well developed endoplasmic reticulum.These phenotypic alterations may serve as markers for butyrate activity on melanoma cells in basic and clinical studies.

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Expression of gamma-glutamyl transpeptidase in normal and neoplastic epithelial cells of human skin: a marker for distinguishing malignant epithelial tumours

Cited by 15 publications

References 16 publications

Inverse correlation between thyroid peroxidase(TPO) and gamma-glutamyl transpeptidase(GGT) activities expressed in diisopropanolnitrosamine(DIPN) induced rat thyroid lesions. An enzyme histochemical study.

Inverse correlation between thyroid peroxidase(TPO) and gamma-glutamyl transpeptidase(GGT) activities expressed in diisopropanolnitrosamine(DIPN) induced rat thyroid lesions. An enzyme histochemical study.

Nrf2 establishes a glutathione-mediated gradient of UVB cytoprotection in the epidermis

Biochemical and ultrastructural alterations accompany the anti-proliferative effect of butyrate on melanoma cells

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