Abstract
Biological responses to extracellular ATP1 and adenosine2 have been documented in virtually every major organ and/or tissue system studied so far. One of these responses, cell proliferation, is usually described as a phenomenon mediated via P1- or P2- purinoceptors on the cell surface3.
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References
G.R. Dubyak, and C. El-Moatassim, 1993, Signal transduction via P2-purinergic receptors for extracellular ATP and other nucleotides, Am. J. Physiol. 265; C577–C606
K.A. Jacobson, P.J.M. van Galen, and M. Williams, 1992, Adenosine Receptors: Pharmacology, Structure-Activity Relationships, and Therapeutic Potential, J. Med. Chem. 35, 407–422
B.B. Fredholm, M.P. Abbracchio, G. Burnstock, J.W. Daly, T.K. Harden, K.A. Jacobson, P. Leff, and M. Williams, 1994, Nomenclature and classification of purinoceptors, Pharmacol Rev. 46, 143–156
J.L. Gordon, 1986, Extracellular ATP: effects, sources and fate, Biochem. J. 233, 309–319
E.H. Abraham, A.G. Prat, L. Gerweck, T. Seneveratne, R.J. Arceci, R. Kramer, G. Guidotti, and H.F. Cantiello, 1993, The multidrug resistance (mdrl) gene product functions as an ATP channel, Proc. Natl. Acad. SCi. USA 90, 312–316
H.F. Cantiello, A.G. Prat, I.L. Reisin, L.B. Ercole, E.H. Abraham, J.F. Amara, R.J. Gregory, and D.A. Ausiello, 1994, External ATP and its analogs activate cystic fibrosis transmembrane conductance regulator by a cyclic AMP-independent mechanism, J. Biol. Chem. 269, 11224–11232
J.P. Grierson, and J. Meldolesi, 1995, Shear stress-induced [Ca2+]i transients and oscillations in mouse fibroblasts are mediated by endogenously released ATP, J. Biol. Chem. 270, 4451–4456
S. Yang, D.J. Cheek, D.P. Westfall, and I.L.O. Buxton, 1994, Purinergic axis in cardiac blood vessels: agonist-mediated release of ATP from cardiac endothelial cells, Circ. Res. 74, 401–407
O. Culic, I. Sabolic, and T. Zanic-Grubisic, 1990, The stepwide hydrolysis of adenine nucleotides by ecto-enzymes of rat renal brush-border membranes, Biochim. Biophys. Acta 1030, 143–151
S-H. Lin, and G. Guidotti, 1989, Cloning and expression of a cDNA coding for a rat liver plasma membrane ecto-ATPase, J. Biol. Chem. 264, 14408–14.
Y. Misumi, S. Ogata, S. Hirose, and Y. Ikehara, 1990, Primary structure of rat liver 5′-nucleotidase deduced from cDNA. Presence of the COOH-terminal hydrophobic domain for possible post-translational modification by glycophospholipid, J. Biol. Chem. 265, 2178–83.
N.S. Dhalla, and D. Zhao, 1988, Cell membrane Ca2+/Mg2+ ATPase, Prog. Biophys. Molec. Biol. 52, 1–37.
M. Van Erum, R. Lemmens, J. Berden, H. Teuchy, and L. Vanduffel, 1995, Identification and partial purification of (Ca2+ or Mg2+)-ATPase in renal brush border membranse, Eur. J. Biochem. 227, 150–160
S-H. Lin, O. Culic, D. Flanagan, and D.C. Hixson, 1991, Immunochemical characterization of two iso-forms of rat liver ecto-ATPase that show an immunological and structural identity with a glycoprotein cell-adhesion molecule with Mr 105 000, Biochem. J. 278, 155–61.
C.J. Sippel, F.H. Suchy, M. Ananthanarayanan, and D.H. Perlmutter, 1993, The rat liver ecto-ATPase is also a canalicular bile acid transport protein, J. Biol. Chem. 268, 2083–91.
J.L. Gordon, 1986, Extracellular ATP: effects, sources and fate, Biochem. J. 233, 309–19.
H. Zimmerman, 1992, 5ø-Nucleotidase: molecular structure and functional aspects, Biochem. J. 285, 345–365
G.L. Stiles, 1992, Adenosine receptors, J. Biol. Chem. 267, 6451–54.
U. Stochaj, and H.G. Mannherz, 1992, Chicken gizzard 5′-nucleotidase functions as a binding protein for the laminin/nidogen complex, Eur. J. Cell. Biol. 59, 364–72.
H. Harris, 1989, The human alkaline phosphatase: what we know and what we don’t know, Clin. Chim. Acta 186, 133–150
R.A. Stinson, J.L. McPhee, and H.B. Colier, 1987, Phosphotransferase activity of human alkaline phosphatase and role of enzyme, Biochim. Biophys. Acta 913, 272–278
K. Müller, V. Schellenberger, P. Borneleit, and Treide A, 1991, The alkaline phosphatase from bone: transphosphorylaing activity and kinetic mechanism, Biochim. Biophys. Acta 1076, 308–313
J.M. Pizauro, P. Ciancaglini, and F.A. Leone, 1992, Phosphotransferase activity associated with rat osseous plate alkaline phosphatase: a possible role in biomineralization, Int. J. Biochem 24, 1391–1396
D. Sarrouilhe, P. Lalegerie, and M. Baudry, 1992, Endogenous phosphorylation and dephosphorylation of rat liver plasma membrane proteins, suggesting a 18 kDa phosphoprotein as a potential substrate for alkaline phosphatase, Biochim. Biophys. Acta 1118, 116–122
From O. Culic, R. Lemmens, H. Teuchy, and L. Vanduffel, 1995, Autoradiography-based cytochemical detection of Ecto-ATPase, Ecto-ADPase, 5′-nucleotidase, and extracellular adenosine production, employing CE as a capturing agent, Histochem. J. 27, 555–564
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Lemmens, R., Culic, O., Vanduffel, L., Teuchy, H. (1997). The Role of Ecto-Enzymes (Ecto-ATPase, 5′-Nucleotidase and Alkaline Phosphatase) in the Proliferation of LLC-MK2-Cells. In: Plesner, L., Kirley, T.L., Knowles, A.F. (eds) Ecto-ATPases. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5955-9_31
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DOI: https://doi.org/10.1007/978-1-4615-5955-9_31
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