Extracellular ATP: effects, sources and fate

Gordon, John L.

doi:10.1042/bj2330309

Cited by 1,594 publications

(1,029 citation statements)

References 133 publications

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“…It has been speculated that extracellular NAD + might become available to CD38 + lymphoid cells, even at transiently elevated concentrations, following apoptosis of neighboring cells [1,2]. Recently, NAD + has been detected for the first time in the interstitial fluid of rat cerebellum [15], thus adding to ATP [33] as a previously unidentified extracellular signal metabolite. GSH, which shows additive effects with NAD + in eliciting CD38 self-aggregation, might also be an extracellular ligand resulting from cell lysis and cooperating with NAD + in triggering CD38 internalization in responsive cells.…”

Section: Discussionmentioning

confidence: 99%

NAD⁺‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

Zocchi¹,

Franco²,

Guida³

et al. 1996

FEBS Letters

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CD38 is a transmembrane glycoprotein involved as an orphan receptor in many physiological processes of lymphocytes. It is also a bifunctional enzyme that catalyzes at its ectocellular domain the synthesis from NAD + (cyclase) and the hydrolysis (hydrolase) of the calcium-mobilizing metabolite cyclic ADPribose (cADPR). A still unexplained paradox concerns the relationship between ectocellular localization of CD38 and intracellular calcium-releasing activity of its intermediate product cADPR. Incubation of CD38 + human Namalwa B cells with external NAD + elicited extensive membrane down-regulation of CD38 and its internalization in non-clathrin-coated vesicles. Since the internalized CD38 was demonstrated to be enzymatically active, this NAD+-dependent process is a hitherto unrecognized means for shifting cADPR metabolism from the cell surface to the intracellular environment.

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Section: Discussionmentioning

confidence: 99%

NAD⁺‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

Zocchi¹,

Franco²,

Guida³

et al. 1996

FEBS Letters

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“…Higher ATP levels (up to 100 mmol/l) are present in secretory vesicles of neurons, serotonergic granules of platelets and exocrine glands (e.g., chromaffin granules of adrenal medulla, insulin-containing granules of pancreatic β-cells, and secretory granules of mast cells) [23][24][25]. The content of these vesicles and granules is released by exocytosis induced by mechanic stimulation or specific stimuli (such as cholinergic stimulation of pancreatic acini or triggering of FcεRI by antigen/IgE cross-linking in mast cells) [23,25].…”

Section: Mast Cellsmentioning

confidence: 99%

P2 receptor-mediated signaling in mast cell biology

Bulanova

Bulfone–Paus∥

2009

Purinergic Signalling

100

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Mast cells are widely recognized as effector cells of allergic inflammatory reactions. They contribute to the pathogenesis of different chronic inflammatory diseases, wound healing, fibrosis, thrombosis/fibrinolysis, and antitumor immune responses. In this paper, we summarized the role of P2X and P2Y receptors in mast cell activation and effector functions. Mast cells are an abundant source of ATP which is stored in their granules and secreted upon activation. We discuss the contribution of mast cells to the extracellular ATP release and to the maintenance of extracellular nucleotides pool. Recent publications highlight the importance of purinergic signaling for the pathogenesis of chronic airway inflammation. Therefore, the role of ATP and P2 receptors in allergic inflammation with focus on mast cells was analyzed. Finally, ATP functions as mast cell autocrine/paracrine factor and as messenger in intercellular communication between mast cells, nerves, and glia in the central nervous system.

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“…Participation of this enzyme in the formation of adenosine would depend upon the presence of micromolar concentrations of AMP in extracellular fluids. One developmental process likely to contribute such high levels of extracellular AMP is cell death (Pearson and Gordon, 1979;Gordon, 1986;Papadimitriou et al, 1991). This process has been described in the uterine epithelium (El-Shershaby and Hinchliffe, 1975;Parr and Parr, 1987), primary decidua (Welsh and Enders, 1987;Parr and Parr, 19891, and secondary decidua (Welsh and Enders, 1985;Katz and Abrahamsohn, 1987) during implantation chamber morphogenesis in rodents.…”

Section: Transmural Asymmetry Of Adenosine Concentration Across the Amentioning

confidence: 99%

Adenosine levels in the postimplantation mouse uterus: Quantitation by HPLC‐fluorometric detection and spatiotemporal regulation by 5′‐nucleotidase and adenosine deaminase

Blackburn

Gao

Airhart

et al. 1992

Developmental Dynamics

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Extracellular adenosine has the potential to influence many aspects of target cell metabolism. The present study has determined the endogenous levels of adenosine in the pregnant mouse uterus and developing embryodecidual unit with respect to the expression of two key enzymes of adenosine metabolism, 5'-nucleotidase (5'-NT; EC 3.1.3.5) and adenosine deaminase (ADA; EC 3.5.4.4). To measure adenosine levels, nucleoside extracts were etheno-derivatized and quantitated by high-performance liquid chromatography-fluorescence detection (0.03 pmollmg protein sensitivity). Adenosine levels were determined to be 0.18 nmol/mg protein in the nonpregnant uterus; however, two statistically significant changes were identified in the pregnant uterus: (1) a periimplantation surge between day 3 (0.24 nmoVmg protein) and day 5 (0.59 nmoYmg protein) of gestation (plug day 0; implantation day 4); and (2) an early postimplantation decline between day 6 (0.54 nmollmg protein) and day 7 (0.10 nmollmg protein). The periimplantation adenosine surge coincided with uterine expression of 5'-NT, an enzyme which catalyzes the irreversible dephosphorylation of 5'-AMP to adenosine. 5'-NT expression was shown by Northern blot analysis to peak in the embryo-decidual unit on day 5 of gestation and then to decline through day 9; transcripts remained elevated in the placenta between day 9 and day 13 (the latest day examined in this study). By use of specific enzyme histochemistry, most 5'-NT activity was localized to the primary decidual :zone on day 5. This expression subsequently declined during regression of the primary decidua; however, 5'-NT appeared on giant trophoblast ((days 7-13) and the metrial gland (days 11-13).Other purine catabolic enzymes degrading AMP (adenylate deaminase) or generating adenosine (S-adenosylhomocysteine hydrolase) were not detected in the embryo-decidual unit suggesting that the net flux of utero-placental AMP catabolism proceeds with adenosine as an intermediate, this being the major pathway of adenosine formation.The sharp drop in adenosine levels between day 6 and day 7 coincided with a rise in the activity and mRNA expression of ADA, an enzyme which catalyzes the irreversible deamination of adenosine to inosine. ADA was previously localized to the secondary decidual zone (days 6 1 l), secondary giant cells (days 7-13), and spongiotrophoblasts (days 8-13) in the mouse (Knudsen et al., 1991). Results of developmental Northern blot analysis demonstrated a direct correlation of relative 5'-NT/ADA mRNA band intensity to adenosine content between day 4 and day 9 of gestation, suggesting that the local availability of adenosine in the antimesometrium is dependent upon the distribution of these enzymatic activities. Purine nucleoside phosphorylase and xanthine oxidase, which are two catabolic enzymes acting subsequent to 5'-NT and ADA in the sequential degradation of AMP to xanthine, remained low and constant in the tissues examined suggesting that the catabolic pathway is geared toward regulation of adenosine le...

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Extracellular ATP: effects, sources and fate

Cited by 1,594 publications

References 133 publications

NAD⁺‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

NAD⁺‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

P2 receptor-mediated signaling in mast cell biology

Adenosine levels in the postimplantation mouse uterus: Quantitation by HPLC‐fluorometric detection and spatiotemporal regulation by 5′‐nucleotidase and adenosine deaminase

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Extracellular ATP: effects, sources and fate

Cited by 1,594 publications

References 133 publications

NAD+‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

NAD+‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

P2 receptor-mediated signaling in mast cell biology

Adenosine levels in the postimplantation mouse uterus: Quantitation by HPLC‐fluorometric detection and spatiotemporal regulation by 5′‐nucleotidase and adenosine deaminase

Contact Info

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Resources

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NAD⁺‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

NAD⁺‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells