메뉴 건너뛰기




Volumn 396, Issue 1, 2010, Pages 23-29

Quantification of extracellular UDP-galactose

Author keywords

Galactosyltransferase; Nucleotide release; UDP galactose

Indexed keywords

GLUCOSE;

EID: 70449674264     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.08.022     Document Type: Article
Times cited : (16)

References (36)
  • 1
    • 0033680583 scopus 로고    scopus 로고
    • P2 purinergic receptors: modulation of cell function and therapeutic potential
    • Burnstock G., and Williams M. P2 purinergic receptors: modulation of cell function and therapeutic potential. J. Pharmacol. Exp. Ther. 295 (2000) 862-869
    • (2000) J. Pharmacol. Exp. Ther. , vol.295 , pp. 862-869
    • Burnstock, G.1    Williams, M.2
  • 2
    • 30444450816 scopus 로고    scopus 로고
    • Purinergic signalling
    • Burnstock G. Purinergic signalling. Br. J. Pharmacol. 147 Suppl. 1 (2006) S172-S181
    • (2006) Br. J. Pharmacol. , vol.147 , Issue.SUPPL. 1
    • Burnstock, G.1
  • 5
    • 67649884495 scopus 로고    scopus 로고
    • Gi-dependent cell signaling responses of the human P2Y14-receptor in model cell systems
    • Fricks I.P., Carter R.L., Lazarowski E.R., and Harden T.K. Gi-dependent cell signaling responses of the human P2Y14-receptor in model cell systems. J. Pharmacol. Exp. Ther. 330 (2009) 162-168
    • (2009) J. Pharmacol. Exp. Ther. , vol.330 , pp. 162-168
    • Fricks, I.P.1    Carter, R.L.2    Lazarowski, E.R.3    Harden, T.K.4
  • 6
    • 1542704056 scopus 로고    scopus 로고
    • GPR105, a novel Gi/o-coupled UDP-glucose receptor expressed on brain glia and peripheral immune cells, is regulated by immunologic challenge: possible role in neuroimmune function
    • Moore D.J., Murdock P.R., Watson J.M., Faull R.L., Waldvogel H.J., Szekeres P.G., Wilson S., Freeman K.B., and Emson P.C. GPR105, a novel Gi/o-coupled UDP-glucose receptor expressed on brain glia and peripheral immune cells, is regulated by immunologic challenge: possible role in neuroimmune function. Brain Res. Mol. Brain Res. 118 (2003) 10-23
    • (2003) Brain Res. Mol. Brain Res. , vol.118 , pp. 10-23
    • Moore, D.J.1    Murdock, P.R.2    Watson, J.M.3    Faull, R.L.4    Waldvogel, H.J.5    Szekeres, P.G.6    Wilson, S.7    Freeman, K.B.8    Emson, P.C.9
  • 7
    • 33746198758 scopus 로고    scopus 로고
    • Functional expression of the P2Y(14) receptor in human neutrophils
    • Scrivens M., and Dickenson J.M. Functional expression of the P2Y(14) receptor in human neutrophils. Eur. J. Pharmacol. 543 (2006) 166-173
    • (2006) Eur. J. Pharmacol. , vol.543 , pp. 166-173
    • Scrivens, M.1    Dickenson, J.M.2
  • 8
    • 27144478111 scopus 로고    scopus 로고
    • Functional expression of the P2Y(14) receptor in murine T-lymphocytes
    • Scrivens M., and Dickenson J.M. Functional expression of the P2Y(14) receptor in murine T-lymphocytes. Br. J. Pharmacol. 146 (2005) 435-444
    • (2005) Br. J. Pharmacol. , vol.146 , pp. 435-444
    • Scrivens, M.1    Dickenson, J.M.2
  • 10
    • 17844385044 scopus 로고    scopus 로고
    • Pathophysiological roles of extracellular nucleotides in glial cells: differential expression of purinergic receptors in resting and activated microglia
    • Bianco F., Fumagalli M., Pravettoni E., D'Ambrosi N., Volonte C., Matteoli M., Abbracchio M.P., and Verderio C. Pathophysiological roles of extracellular nucleotides in glial cells: differential expression of purinergic receptors in resting and activated microglia. Brain Res. Brain Res. Rev. 48 (2005) 144-156
    • (2005) Brain Res. Brain Res. Rev. , vol.48 , pp. 144-156
    • Bianco, F.1    Fumagalli, M.2    Pravettoni, E.3    D'Ambrosi, N.4    Volonte, C.5    Matteoli, M.6    Abbracchio, M.P.7    Verderio, C.8
  • 13
    • 0042134893 scopus 로고    scopus 로고
    • Human immature monocyte-derived dendritic cells express the G protein-coupled receptor GPR105 (KIAA0001, P2Y14) and increase intracellular calcium in response to its agonist, uridine diphosphoglucose
    • Skelton L., Cooper M., Murphy M., and Platt A. Human immature monocyte-derived dendritic cells express the G protein-coupled receptor GPR105 (KIAA0001, P2Y14) and increase intracellular calcium in response to its agonist, uridine diphosphoglucose. J. Immunol. 171 (2003) 1941-1949
    • (2003) J. Immunol. , vol.171 , pp. 1941-1949
    • Skelton, L.1    Cooper, M.2    Murphy, M.3    Platt, A.4
  • 15
    • 0038745422 scopus 로고    scopus 로고
    • Release of cellular UDP-glucose as a potential extracellular signaling molecule
    • Lazarowski E.R., Shea D.A., Boucher R.C., and Harden T.K. Release of cellular UDP-glucose as a potential extracellular signaling molecule. Mol. Pharmacol. 63 (2003) 1190-1197
    • (2003) Mol. Pharmacol. , vol.63 , pp. 1190-1197
    • Lazarowski, E.R.1    Shea, D.A.2    Boucher, R.C.3    Harden, T.K.4
  • 18
    • 50849127131 scopus 로고    scopus 로고
    • Similarities between UDP-glucose and adenine nucleotide release in yeast: involvement of the secretory pathway
    • Esther Jr. C.R., Sesma J.I., Dohlman H.G., Ault A.D., Clas M.L., Lazarowski E.R., and Boucher R.C. Similarities between UDP-glucose and adenine nucleotide release in yeast: involvement of the secretory pathway. Biochemistry 47 (2008) 9269-9278
    • (2008) Biochemistry , vol.47 , pp. 9269-9278
    • Esther Jr., C.R.1    Sesma, J.I.2    Dohlman, H.G.3    Ault, A.D.4    Clas, M.L.5    Lazarowski, E.R.6    Boucher, R.C.7
  • 20
    • 0034613299 scopus 로고    scopus 로고
    • Constitutive release of ATP and evidence for major contribution of ecto-nucleotide pyrophosphatase and nucleoside diphosphokinase to extracellular nucleotide concentrations
    • Lazarowski E.R., Boucher R.C., and Harden T.K. Constitutive release of ATP and evidence for major contribution of ecto-nucleotide pyrophosphatase and nucleoside diphosphokinase to extracellular nucleotide concentrations. J. Biol. Chem. 275 (2000) 31061-31068
    • (2000) J. Biol. Chem. , vol.275 , pp. 31061-31068
    • Lazarowski, E.R.1    Boucher, R.C.2    Harden, T.K.3
  • 22
    • 0141457730 scopus 로고    scopus 로고
    • Mechanisms of release of nucleotides and integration of their action as P2X- and P2Y-receptor activating molecules
    • Lazarowski E.R., Boucher R.C., and Harden T.K. Mechanisms of release of nucleotides and integration of their action as P2X- and P2Y-receptor activating molecules. Mol. Pharmacol. 64 (2003) 785-795
    • (2003) Mol. Pharmacol. , vol.64 , pp. 785-795
    • Lazarowski, E.R.1    Boucher, R.C.2    Harden, T.K.3
  • 23
    • 42949090427 scopus 로고    scopus 로고
    • Structure and function of beta-1,4-galactosyltransferase
    • Qasba P.K., Ramakrishnan B., and Boeggeman E. Structure and function of beta-1,4-galactosyltransferase. Curr. Drug Targets 9 (2008) 292-309
    • (2008) Curr. Drug Targets , vol.9 , pp. 292-309
    • Qasba, P.K.1    Ramakrishnan, B.2    Boeggeman, E.3
  • 25
    • 42649095381 scopus 로고    scopus 로고
    • Calcium-dependent release of adenosine and uridine nucleotides from A549 cells
    • Tatur S., Kreda S., Lazarowski E., and Grygorczyk R. Calcium-dependent release of adenosine and uridine nucleotides from A549 cells. Purinerg. Signal. 4 (2008) 139-146
    • (2008) Purinerg. Signal. , vol.4 , pp. 139-146
    • Tatur, S.1    Kreda, S.2    Lazarowski, E.3    Grygorczyk, R.4
  • 27
    • 0037593535 scopus 로고    scopus 로고
    • Colocalization of ATP release sites and ecto-ATPase activity at the extracellular surface of human astrocytes
    • Joseph S.M., Buchakjian M.R., and Dubyak G.R. Colocalization of ATP release sites and ecto-ATPase activity at the extracellular surface of human astrocytes. J. Biol. Chem. 278 (2003) 23342
    • (2003) J. Biol. Chem. , vol.278 , pp. 23342
    • Joseph, S.M.1    Buchakjian, M.R.2    Dubyak, G.R.3
  • 28
    • 3843142923 scopus 로고    scopus 로고
    • Methylene ATP analogs as modulators of extracellular ATP metabolism and accumulation
    • Joseph S.M., Pifer M.A., Przybylski R.J., and Dubyak G.R. Methylene ATP analogs as modulators of extracellular ATP metabolism and accumulation. Br. J. Pharmacol. 142 (2004) 1002-1014
    • (2004) Br. J. Pharmacol. , vol.142 , pp. 1002-1014
    • Joseph, S.M.1    Pifer, M.A.2    Przybylski, R.J.3    Dubyak, G.R.4
  • 29
    • 0027961107 scopus 로고
    • Separation and analysis of 4′-epimeric UDP-sugars, nucleotides, and sugar phosphates by anion-exchange high-performance liquid chromatography with conductimetric detection
    • Hull S.R., and Montgomery R. Separation and analysis of 4′-epimeric UDP-sugars, nucleotides, and sugar phosphates by anion-exchange high-performance liquid chromatography with conductimetric detection. Anal. Biochem. 222 (1994) 49-54
    • (1994) Anal. Biochem. , vol.222 , pp. 49-54
    • Hull, S.R.1    Montgomery, R.2
  • 30
    • 0035369256 scopus 로고    scopus 로고
    • Determination of nucleotides and sugar nucleotides involved in protein glycosylation by high-performance anion-exchange chromatography: sugar nucleotide contents in cultured insect cells and mammalian cells
    • Tomiya N., Ailor E., Lawrence S.M., Betenbaugh M.J., and Lee Y.C. Determination of nucleotides and sugar nucleotides involved in protein glycosylation by high-performance anion-exchange chromatography: sugar nucleotide contents in cultured insect cells and mammalian cells. Anal. Biochem. 293 (2001) 129-137
    • (2001) Anal. Biochem. , vol.293 , pp. 129-137
    • Tomiya, N.1    Ailor, E.2    Lawrence, S.M.3    Betenbaugh, M.J.4    Lee, Y.C.5
  • 31
    • 29244453502 scopus 로고    scopus 로고
    • Intracellular nucleotide and nucleotide sugar contents of cultured CHO cells determined by a fast, sensitive, and high-resolution ion-pair RP-HPLC
    • Kochanowski N., Blanchard F., Cacan R., Chirat F., Guedon E., Marc A., and Goergen J.L. Intracellular nucleotide and nucleotide sugar contents of cultured CHO cells determined by a fast, sensitive, and high-resolution ion-pair RP-HPLC. Anal. Biochem. 348 (2006) 243-251
    • (2006) Anal. Biochem. , vol.348 , pp. 243-251
    • Kochanowski, N.1    Blanchard, F.2    Cacan, R.3    Chirat, F.4    Guedon, E.5    Marc, A.6    Goergen, J.L.7
  • 32
    • 0015159047 scopus 로고
    • Evidence for cell-surface glycosyltransferases. Their potential role in cellular recognition
    • Roth S., McGuire E.J., and Roseman S. Evidence for cell-surface glycosyltransferases. Their potential role in cellular recognition. J. Cell Biol. 51 (1971) 536-547
    • (1971) J. Cell Biol. , vol.51 , pp. 536-547
    • Roth, S.1    McGuire, E.J.2    Roseman, S.3
  • 33
    • 0016604870 scopus 로고
    • The sialic acids. XVIII. Subcellular distribution of seven glycosyltransferases in embryonic chicken brain
    • Den H., Kaufman B., McGuire E.J., and Roseman S. The sialic acids. XVIII. Subcellular distribution of seven glycosyltransferases in embryonic chicken brain. J. Biol. Chem. 250 (1975) 739-746
    • (1975) J. Biol. Chem. , vol.250 , pp. 739-746
    • Den, H.1    Kaufman, B.2    McGuire, E.J.3    Roseman, S.4
  • 34
    • 0035834665 scopus 로고    scopus 로고
    • Reflections on glycobiology
    • Roseman S. Reflections on glycobiology. J. Biol. Chem. 276 (2001) 41527-41542
    • (2001) J. Biol. Chem. , vol.276 , pp. 41527-41542
    • Roseman, S.1
  • 36
    • 0031711820 scopus 로고    scopus 로고
    • Transporters of nucleotide sugars, ATP, and nucleotide sulfate in the endoplasmic reticulum and Golgi apparatus
    • Hirschberg C.B., Robbins P.W., and Abeijon C. Transporters of nucleotide sugars, ATP, and nucleotide sulfate in the endoplasmic reticulum and Golgi apparatus. Annu. Rev. Biochem. 67 (1998) 49-69
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 49-69
    • Hirschberg, C.B.1    Robbins, P.W.2    Abeijon, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.