P2-Purinergic receptors activate a guanine nucleotide-dependent phospholipase C in membranes from HL-60 cells

Cowen, David L.; Sanders, Michelle; Dubyak, George R.

doi:10.1016/0167-4889(90)90014-5

Cited by 41 publications

(20 citation statements)

References 35 publications

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“…ATP and UTP activated superoxide formation in HL-60 promyelocytic leukaemic cells [440] and ATP also increased [Ca 2+ ] i in these cells [441,442] probably via P2Y 2 receptors [443,444]. Reduced proliferation was produced by ATP and UTP in both HL-60 promyelocytic and U937 promonocytic human cell lines [445], perhaps via A 3 receptors [446].…”

Section: Lymphocytic Leukaemiamentioning

confidence: 99%

Purinergic signalling and cancer

Burnstock

Virgilio

2013

Purinergic Signalling

272

265

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Receptors for extracellular nucleotides are widely expressed by mammalian cells. They mediate a large array of responses ranging from growth stimulation to apoptosis, from chemotaxis to cell differentiation and from nociception to cytokine release, as well as neurotransmission. Pharma industry is involved in the development and clinical testing of drugs selectively targeting the different P1 nucleoside and P2 nucleotide receptor subtypes. As described in detail in the present review, P2 receptors are expressed by all tumours, in some cases to a very high level. Activation or inhibition of selected P2 receptor subtypes brings about cancer cell death or growth inhibition. The field has been largely neglected by current research in oncology, yet the evidence presented in this review, most of which is based on in vitro studies, although with a limited amount from in vivo experiments and human studies, warrants further efforts to explore the therapeutic potential of purinoceptor targeting in cancer.

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Section: Lymphocytic Leukaemiamentioning

confidence: 99%

Purinergic signalling and cancer

Burnstock

Virgilio

2013

Purinergic Signalling

272

265

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“…182,183 In human neutrophils, ATP and UTP were reported to be equipotent for both the [Ca ϩϩ ] i increase and superoxide anion formation, 178,179 and ATP was also shown to stimulate phospholipase C and diacylglycerol generation as well as protein kinase C activity. 183,184 It is of great interest in the light of the proposed proinflammatory role of extracellular ATP that this nucleotide also increases membrane expression of CD11b/CD18 and adhesion to albumin-coated latex beads. 185 Because ATP is released by the endothelium and its local concentration is likely to increase during inflammation as a consequence of inactivation of ecto-ATPases by oxygen radicals, 186 up-regulation of adhesion molecules by this nucleotide could be of relevance for leukocyte migration across the vessel wall.…”

Section: P2 Receptors In Polymorphonuclear Granulocytesmentioning

confidence: 99%

Nucleotide receptors: an emerging family of regulatory molecules in blood cells

Virgilio

Chiozzi

Ferrari

et al. 2001

Blood

644

683

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Nucleotides are emerging as an ubiquitous family of extracellular signaling molecules. It has been known for many years that adenosine diphosphate is a potent platelet aggregating factor, but it is now clear that virtually every circulating cell is responsive to nucleotides. Effects as different as proliferation or differentiation, chemotaxis, release of cytokines or lysosomal constituents, and generation of reactive oxygen or nitrogen species are

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“…In general, the rank order of potency at P2x is x,,-methylene ATP (o,j-MeATP) > P,y-methylene ATP > ATP = ADP > 2-methylthio ATP (2-MeSATP) and at P2Y, 2-MeSATP > ATP = ADP > ax,-MeATP > P,y-methylene ATP. The extracellular effects of ATP and its related agonists have been thoroughly investigated in cultured cell lines (Hallam & Pearson, 1986;Phaneuf et al, 1987;Rice & Singleton, 1987;Ehrlich et al, 1988;Cowen et al, 1990;Kastritsis et al, 1992;Koike et al, 1992;Sato et al, 1992) and current classification suggests the existence of at least three additional subtypes of P2-purinoceptors (see TIPS Receptor Nomenclature supplement, 1993). These include a receptor found primarily on platelets (P2T; Gordon, 1986) and one responsible for permeabilisation of mast cells (P2z; Cockroft & Gomperts, 1980).…”

Section: Introductionmentioning

confidence: 99%

Increases in intracellular calcium via activation of an endogenous P₂‐purinoceptor in cultured CHO‐K1 cells

Iredale

Hill

1993

British J Pharmacology

126

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1 Increases in intracellular calcium ([Ca2+]i) were measured in chinese hamster cultured ovary cells (clone, CHO-Ki), by use of the fluorescent, calcium-sensitive dye, fura-2.2 Addition of both ATP and UTP elicited rapid increases in [Ca2+]i due to mobilization from intracellular stores and calcium entry across the plasma membrane. 3 Omission of calcium from the extracellular medium and pre-incubation with the inorganic calcium channel blocker, nickel (Ni2l) prevented the calcium entry components of the responses. 4 Investigation of the concentration-response relationships of various analogues of ATP suggests the presence of a purinoceptor which cannot be characterized as P2X or P2Y. In addition, there appears to be a sub-population of P2y-purinoceptors which do not cross-react with the 'nucleotide' receptor population.5 Cross-desensitization and additivity experiments suggest that both ATP and UTP activate the same receptor.6 Pre-incubation with the tumour-promoting agent, P-phorbol-12,13 dibutyrate (PDBu), caused a reduction in the increases in [Ca2+]i, suggesting a role for protein kinase C in feedback inhibition of purinoceptor responses in this cell line.7 In summary, we present evidence for the existence of an endogenous P2u-purinoceptor (or 'nucleotide receptor') which is linked to increases in [Ca2+], in CHO-KI cells.

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P2-Purinergic receptors activate a guanine nucleotide-dependent phospholipase C in membranes from HL-60 cells

Cited by 41 publications

References 35 publications

Purinergic signalling and cancer

Purinergic signalling and cancer

Nucleotide receptors: an emerging family of regulatory molecules in blood cells

Increases in intracellular calcium via activation of an endogenous P₂‐purinoceptor in cultured CHO‐K1 cells

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P2-Purinergic receptors activate a guanine nucleotide-dependent phospholipase C in membranes from HL-60 cells

Cited by 41 publications

References 35 publications

Purinergic signalling and cancer

Purinergic signalling and cancer

Nucleotide receptors: an emerging family of regulatory molecules in blood cells

Increases in intracellular calcium via activation of an endogenous P2‐purinoceptor in cultured CHO‐K1 cells

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Increases in intracellular calcium via activation of an endogenous P₂‐purinoceptor in cultured CHO‐K1 cells