Extracellular ATP Metabolism in B and T Lymphocytes

Barankiewicz, Jerzy; Cohen, Amos

doi:10.1111/j.1749-6632.1990.tb37687.x

Cited by 10 publications

(8 citation statements)

References 62 publications

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“…In this report, we show that EBV-transformed B lymphocytes have ecto-apyrase activity, whereas non-EBV-trans-formed B lymphocytes do not. Ecto-apyrase activities were also found associated with other immunocompetent cells, including cytotoxic T cells (16) and natural killer (NK) cells (4), but not with resting thymocytes and lymphomas (4,17,18). Both in our studies and those of other investigators, there is a coincidence between expression of CD39 and ecto-apyrase activity.…”

supporting

confidence: 71%

CD39 Is an Ecto-(Ca2+,Mg2+)-apyrase

Wang¹,

Guidotti

1996

Journal of Biological Chemistry

288

182

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CD39, a 70-to 100-kDa molecule expressed primarily on activated lymphoid cells, was previously identified as a surface marker of Epstein Barr virus (EBV)-transformed B cells. In this report, we show that an ecto-(Ca 2؉ ,Mg 2؉)-apyrase activity is present on EBV-transformed B cells, but not on B or T lymphomas. The coincidence between CD39 expression and ecto-apyrase activity on immune cells suggests that CD39 may be an ecto-apyrase. This supposition is supported by the observation that the amino acid sequence of CD39 is significantly homologous to those of several newly identified nucleotide triphosphatases. Finally, we show that CD39 indeed has ecto-apyrase activity by expression in COS-7 cells.

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supporting

confidence: 71%

CD39 Is an Ecto-(Ca2+,Mg2+)-apyrase

Wang¹,

Guidotti

1996

Journal of Biological Chemistry

288

182

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“…Considering the wellknown data that lymphoid follicles consist mainly of B lymphocytes [7], it seems that the activity of 5)-NT corresponds to a B-cell-rich zone of tonsillar tissue, which was also observed in the spleen by Müller-Hermelink et al [8]. This is in accordance with the fact that B lymphocytes isolated from tonsillar tissue and peripheral blood express higher activity of 5)-NT than T lymphocytes [1,9,10]. The activity of 5)-NT associated with the cells corresponding to the light zone of germinal centres and follicular mantle zones suggests the expression of this enzyme on maturing and mature B lymphocytes.…”

Section: Discussionsupporting

confidence: 74%

Localisation of Ecto-5{LC2}’- Nucleotidase and Divalent Cation-Activated Ecto-ATPase in Chronic Tonsillitis

Avramović¹,

Vlahović²,

Savić³

et al. 1998

ORL

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The histochemical localisation of two ecto-enzymes, 5′-nucleotidase (5′-NT) and Mg²⁺-ATPase, was investigated in hyperplastic and recurrent tonsillitis. Detection of enzymes was performed on frozen sections using the classical lead nitrate method. Activity of 5′-NT was demonstrated particularly in the cells of lymphoid follicles and in the basal layer of the surface tonsillar epithelium. There was no difference in localisation of 5′-NT between hyperplastic and recurrent tonsillitis, whereas a stronger reaction in follicular mantle zones was observed in recurrent tonsillitis compared to hyperplastic tonsillitis. Mg²⁺-ATPase activity was mainly associated with the cells lining the tonsillar crypt, with the interfollicular areas and blood vessels. In recurrent tonsillitis only half of the studied follicular germinal centres expressed Mg²⁺-ATPase activity, compared to hyperplastic tonsillitis. The similar localisation of 5′-NT and ecto-ATPase in both types of chronic tonsillitis suggests that in inflamed tonsils expression of investigated enzymes probably does not depend on the type of chronic tonsillitis.

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“…E-NTPDases, as defined by ecto-ATPase activity, are expressed by a variety of tissue types, including lymphocytes (7); however, the physiological role of this enzyme in lymphocytes is not well understood. By measuring the release of ␥-32 P i from [␥-32 P]ATP, activated human B cells (8), EBV-transformed human B cells (9), human NK cell lines (10), and activated CD8 ϩ CTLs from mice (11) hydrolyze extracellular ATP. Greater than 90% of the ATPase activity is cell associated and thus is not due to enzymes secreted by or released from the cytoplasm (9,11,12).…”

mentioning

confidence: 99%

Secretion of IL-2 and IFN-γ, But Not IL-4, by Antigen-Specific T Cells Requires Extracellular ATP

Langston

Gewirtz

et al. 2003

The Journal of Immunology

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Extracellular ATP and other nucleotides transmit signals to cells via surface-associated molecules whose binding sites face the extracellular milieu. Ecto-nucleoside triphosphate diphosphohydrolase is such an ATP-binding enzyme that is expressed by activated lymphocytes. We have previously shown that nonhydrolyzable ATP analogs block the lytic activity of NK cells and CD8+ T cells as well as their E-NTPDase activity. These results suggest that the hydrolysis of ATP may play a role in lymphocyte function. Here we report that E-NTPDase activity is up-regulated within 15 min of T cell stimulation and that reversible and irreversible enzyme inhibitors profoundly reduce secretion of IL-2 and IFN-γ, but not IL-4. TNF-α, IL-10, and IL-5 production showed intermediate sensitivity to these ATP analogs. Depletion of extracellular ATP also inhibited secretion of IFN-γ, but not IL-4, supporting the interpretation that extracellular ATP is required for secretion of some, but not all, cytokines. E-NTPDase antagonists reduced transcription of IL-2 mRNA and inhibited TCR-mediated intracellular calcium flux. These results suggest that extracellular ATP plays an essential role in the TCR-mediated signal transduction cascade for expression of certain cytokine genes.

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Extracellular ATP Metabolism in B and T Lymphocytes

Cited by 10 publications

References 62 publications

CD39 Is an Ecto-(Ca2+,Mg2+)-apyrase

CD39 Is an Ecto-(Ca2+,Mg2+)-apyrase

Localisation of Ecto-5{LC2}’- Nucleotidase and Divalent Cation-Activated Ecto-ATPase in Chronic Tonsillitis

Secretion of IL-2 and IFN-γ, But Not IL-4, by Antigen-Specific T Cells Requires Extracellular ATP

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