External ATP-induced passive permeability change and cell lysis of cultured transformer cells: action in serum-containing growth media

Kitagawa, Toshikazu; Amino, Fumio; Akamatsu, Yuzuru

doi:10.1016/0005-2736(88)90186-1

Cited by 26 publications

(8 citation statements)

References 26 publications

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“…More sustained stimulations cause an irreversible cell damage that eventually leads to cell death (Kitagawa et al, 1988;Nagelkerke et al, 1989;Blanchard et al, 1991;Murgia et al, 1992b;Falzoni et al, 1995;Modderman et al, 1994;Vijweide et al, 1995;Zoeteweij et al, 1996).…”

Section: Functional Properties Of P2x Receptorsmentioning

confidence: 99%

“…This drawing shows the general architecture of ATP-gated channel subunits (P2X), the peculiar P2Z/P2X 7 subunit (note the extended COOH tail), the mechanosensitive channel of E. coli (mscL), the ATP/ADP-gated inward rectifier K + channel (K-ATP), the mammalian epithelial amiloride-sensitive Na channel (ENaC), the C. elegans mechanosensitive channel (Mec-4). Light blue, ectodomain; green, membrane-spanning regions; red, cytoplasmic domains P2X purinoceptors and cytotoxicity F Di Virgilio et al cells and cell lines (melanoma and mouse fibroblast cells, J774 mouse macrophages, primary mouse and human lymphocytes, mouse lymphoma and mastocytoma cells) with extracellular ATP caused cell death Kitagawa et al, 1988;Di Virgilio et al, 1989;Wiley and Dubyak, 1989;Zanovello et al, 1990). Our group also showed that cell death could be due to either colloido-osmotic lysis or apoptosis depending on the cell type and length of stimulation Murgia et al, 1992a).…”

Section: P2x Receptors and Cell Deathmentioning

confidence: 99%

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Cytolytic P2X purinoceptors

et al. 1998

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Anedoctal evidence accumulated over almost 20 years has shown that many different cell types are killed by sustained exposure to high concentrations of extracellular ATP. The plasma membrane receptors involved have been pharmacologically characterized and cloned during the last 3 years, and named purinergic P2X. P2X receptors share an intriguing structural relatedness with Caenorhabditis elegans degenerins and mammalian amiloridesensitive Na channels (ENaCs). Depending on the ATP dose, length of stimulation and receptor subtype, P2X receptor stimulation may cause necrosis or apoptosis. The intracellular pathways activated are poorly known, but the perturbation in intracellular ion homeostasis clearly plays a major role. ICE proteases (caspases) are also triggered, nonetheless their activation is not requested for ATP-dependent cell death. The physiological meaning of P2X receptor-dependent cytotoxicity is not understood, but an involvement in immune-mediated reactions is postulated.

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Section: Functional Properties Of P2x Receptorsmentioning

confidence: 99%

Section: P2x Receptors and Cell Deathmentioning

confidence: 99%

Cytolytic P2X purinoceptors

et al. 1998

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“…on cellular physiology have been described [1][2][3][4]. However, only recently has attention been paid to the long-standing observation that ATPO is also cytolytic [5][6][7][8][9]. The lytic properties of ATPO are particularly prominent in lymphocytes and lymphoid cells, in which even short exposures cause irreversible damage to the plasma membrane and release of cytosolic enzymes.…”

Section: Introductionmentioning

confidence: 99%

Extracellular ATP causes lysis of mouse thymocytes and activates a plasma membrane ion channel

Pizzo

Zanovello

Bronte

et al. 1991

Biochemical Journal

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Extracellular ATP (ATP.) caused a concentration-dependent lysis of mouse thymocytes. Lysis, as judged by release of the cytosolic enzyme lactate dehydrogenase, was preceded by depolarization of the plasma membrane and by Ca2+ influx.Both Na+ uptake (which sustained plasma membrane depolarization) and Ca2+ influx showed (1) the same dependence on the ATPo concentration; (2) the same nucleotide specificity; and (3) the same Hill coefficient. However, whereas the rise in the cytosolic free Ca2+ concentration ([Ca2+]1) was fully inhibited by the known Ca2+ blocker verapamil, plasma membrane depolarization was enhanced under these conditions. Plasma membrane depolarization was greater and was shifted to lower ATPO concentrations in the absence of extracellular Ca2+ (Ca2+0), whereas the rise in [Ca2+]1 was greater in Na+-free media. Plasma membrane depolarization also occurred in Na+-free choline-or methylglucamine-containing media, and was potentiated by chelation of free divalent ions with EDTA, supporting previous reports pointing to ATP4-as the active species. Among a number of purine and pyrimidine nucleotides, only adenosine 5'-[y-thio]triphosphate and ADP were partially effective. Furthermore, ethidium bromide (Mr 380), Lucifer Yellow (Mr 463) and Eosin Yellowish (Mr 692) did not permeate through the ATPO-activated channel. These findings suggest that lytic effects of ATPO in mouse thymocytes depend on the activation of a membrane channel with low selectivity for cations and an Mr cut-off of 200.

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“…These effects were not observed in untransformed control cells [Hatta et al, 1993[Hatta et al, , 1994Kitagawa et al, 1988;Mure et al, 1992;Rapaport, 1983]. In human tumor cell lines, ATP inhibited the growth of pancreatic adenocarcinoma cells [Rapaport, 1983], colon adenocarcinoma cells [Rapaport, 1983], melanoma cells [Kitagawa et al, 1988;Rapaport, 1983], androgenindependent prostate carcinoma cells [Fang et al, 1992], breast cancer cells [Abraham et al, 1996;Spungin and Friedberg, 1993;Vandewalle et al, 1994], myeloid and monocytic leukemia cells [Hatta et al, 1994], and multidrug resistant colon carcinoma cells [Correale et al, 1995]. In rats and mice, ATP was found to inhibit the growth of lymphomas [Nayak et al, 1990], colon carcinomas [Rapaport and Fontaine, 1989], fibrosarcomas [Froio et al, 1995], Ehrlich ascites tumors [Lasso de la Vega et al, 1994], and breast tumors [Abraham et al, 1996].…”

Section: Adenosinementioning

confidence: 87%

“…E-mail: Dagnelie@epid.unimaas.nl concentration below 50 mM [Huang et al, 1991;Wang et al, 1992], whereas higher ATP concentrations inhibited growth [Belzer and Friedberg, 1989;Chahwala and Cantley, 1984;Fang et al, 1992;Hatta et al, 1994;Rapaport, 1983;Rapaport et al, 1983;Seetulsingh-Goorah and Stewart, 1998;Spungin and Friedberg, 1993;Vandewalle et al, 1994]. These effects were not observed in untransformed control cells [Hatta et al, 1993[Hatta et al, , 1994Kitagawa et al, 1988;Mure et al, 1992;Rapaport, 1983]. In human tumor cell lines, ATP inhibited the growth of pancreatic adenocarcinoma cells [Rapaport, 1983], colon adenocarcinoma cells [Rapaport, 1983], melanoma cells [Kitagawa et al, 1988;Rapaport, 1983], androgenindependent prostate carcinoma cells [Fang et al, 1992], breast cancer cells [Abraham et al, 1996;Spungin and Friedberg, 1993;Vandewalle et al, 1994], myeloid and monocytic leukemia cells [Hatta et al, 1994], and multidrug resistant colon carcinoma cells [Correale et al, 1995].…”

Section: Adenosinementioning

confidence: 99%

Growth inhibition of lung cancer cells by adenosine 5′‐triphosphate

Agteresch

Rooijen

Berg

et al. 2003

Drug Development Research

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Preliminary clinical data suggest that adenosine 5'-triphosphate (ATP) may inhibit lung tumor growth. Because studies of ATP on lung cancer cells are lacking, the aim of the present study was to explore effects of extracellular ATP on the growth and morphology of human lung tumor cells. Five human lung tumor cell lines derived from tumors with different cellular characteristics, i.e., a small cell carcinoma (GLC4), a large cell carcinoma (H460), a squamous cell carcinoma (H520), a mesothelioma (MERO82), and a papillary adenocarcinoma (H441), were exposed to 0, 0.5, 1, 2, and 3 mM ATP. Total cell numbers and dead or damaged cells were measured on days 1, 2, and 3. ATP induced a significant, dose-dependent growth inhibition in GLC4, H460, H520, and MERO82 cells. In contrast, H441 cells showed already maximal inhibition at 0.5 mM. Compared to untreated control cell lines, a significant growth inhibition (mean 7 SEM) of 65 7 5% (GLC4), 59 7 5% (H460), 45 7 5% (H520), 3872% (MERO82), and 55 7 8% (H441) was shown after 3 days incubation with 3 mM ATP. ATP also induced changes in morphology and attachment to the substratum. Although not demonstrated by the Trypan Blue exclusion test, on photographs it seems that ATP induces death of GLC4 and H460 cells at higher concentrations. In conclusion, in four out of five explored lung tumor cell lines, ATP induces a dose-dependent growth inhibition. Lung adenocarcinoma cells show already maximal inhibition at the lowest tested ATP dose. There is a relationship between growth inhibition and morphology changes. Drug Dev.

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External ATP-induced passive permeability change and cell lysis of cultured transformer cells: action in serum-containing growth media

Cited by 26 publications

References 26 publications

Cytolytic P2X purinoceptors

Cytolytic P2X purinoceptors

Extracellular ATP causes lysis of mouse thymocytes and activates a plasma membrane ion channel

Growth inhibition of lung cancer cells by adenosine 5′‐triphosphate

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