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Volumn 299, Issue 3, 2002, Pages 424-431

Extracellular NAD+: A novel autocrine/paracrine signal in osteoblast physiology

Author keywords

Calcium; Local factors; Mechanical loading; NAD+; Osteoblasts

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYL CYCLASE; ALKALINE PHOSPHATASE; CALCIUM ION; CD38 ANTIGEN; NICOTINAMIDE ADENINE DINUCLEOTIDE; OSTEOCALCIN;

EID: 0036433221     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02665-7     Document Type: Article
Times cited : (17)

References (36)
  • 1
    • 0035046976 scopus 로고    scopus 로고
    • Extracellular nucleotide signaling: A mechanism for integrating local and systemic responses in the activation of bone remodeling
    • W.B. Bowler, K.A. Buckley, A. Gartland, R.A. Hipskind, G. Bilbe, J.A. Gallagher, Extracellular nucleotide signaling: a mechanism for integrating local and systemic responses in the activation of bone remodeling, Bone 28 (2001) 507-512.
    • (2001) Bone , vol.28 , pp. 507-512
    • Bowler, W.B.1    Buckley, K.A.2    Gartland, A.3    Hipskind, R.A.4    Bilbe, G.5    Gallagher, J.A.6
  • 3
    • 0034918779 scopus 로고    scopus 로고
    • Dual mechanism of intercellular communication in HOBIT osteoblastic cells: A role for gap-junctional hemichannels
    • M. Romanello, P. D3Andrea, Dual mechanism of intercellular communication in HOBIT osteoblastic cells: A role for gap-junctional hemichannels, J. Bone Min. Res. 1 (2001) 1465-1476.
    • (2001) J. Bone Min. Res. , vol.1 , pp. 1465-1476
    • Romanello, M.1    D'Andrea, P.2
  • 4
    • 0028807366 scopus 로고
    • Mechanotransduction and the functional response of bone to mechanical strain
    • R.L. Duncan, C.H. Turner, Mechanotransduction and the functional response of bone to mechanical strain, Calcif. Tissue Int. 57 (1995) 344-358.
    • (1995) Calcif. Tissue Int. , vol.57 , pp. 344-358
    • Duncan, R.L.1    Turner, C.H.2
  • 6
    • 0030882314 scopus 로고    scopus 로고
    • Direct demonstration of mechanically induced release of cellular UTP and its implication for uridine nucleotide receptor activation
    • E.R. Lazarowski, L. Homolya, R.C. Boucher, T. Kendall Harden, Direct demonstration of mechanically induced release of cellular UTP and its implication for uridine nucleotide receptor activation, J. Biol. Chem. 272 (1997) 24348-24354.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24348-24354
    • Lazarowski, E.R.1    Homolya, L.2    Boucher, R.C.3    Kendall Harden, T.4
  • 8
    • 0345609814 scopus 로고    scopus 로고
    • Mechanism of calcium signaling cyclic ADP-ribose and NAADP
    • H.C. Lee, Mechanism of calcium signaling cyclic ADP-ribose and NAADP, Physiol. Rev. 77 (1997) 1133-1164.
    • (1997) Physiol. Rev. , vol.77 , pp. 1133-1164
    • Lee, H.C.1
  • 9
    • 0031765051 scopus 로고    scopus 로고
    • The transmembrane glycoprotein CD38 is a catalytically active transporter responsible for generation and influx of the second messenger cyclic ADP-ribose across membranes
    • L. Franco, L. Guida, S. Bruzzone, E. Zocchi, C. Usai, A. De Flora, The transmembrane glycoprotein CD38 is a catalytically active transporter responsible for generation and influx of the second messenger cyclic ADP-ribose across membranes, FASEB J. 12 (1998) 1507-1520.
    • (1998) FASEB J. , vol.12 , pp. 1507-1520
    • Franco, L.1    Guida, L.2    Bruzzone, S.3    Zocchi, E.4    Usai, C.5    De Flora, A.6
  • 11
    • 0026418298 scopus 로고
    • 2+ release in sea urchin egg homogenates: Modulation by cyclic ADP-ribose
    • 2+ release in sea urchin egg homogenates: Modulation by cyclic ADP-ribose, Science 253 (1991) 1143-1146.
    • (1991) Science , vol.253 , pp. 1143-1146
    • Galione, A.1    Lee, H.C.2    Busa, W.B.3
  • 12
    • 0027393833 scopus 로고
    • Cyclic ADP-ribose in insulin secretion from pancreatic β cells
    • S. Takasawas, K. Nata, H. Yonemura, H. Okamoto, Cyclic ADP-ribose in insulin secretion from pancreatic β cells, Science 259 (1993) 370-373.
    • (1993) Science , vol.259 , pp. 370-373
    • Takasawas, S.1    Nata, K.2    Yonemura, H.3    Okamoto, H.4
  • 17
    • 0018850985 scopus 로고
    • A simple, rapid and sensitive DNA assay procedure
    • C. Labarca, K. Paigen, A simple, rapid and sensitive DNA assay procedure, Anal. Biochem. 102 (1980) 344-352.
    • (1980) Anal. Biochem. , vol.102 , pp. 344-352
    • Labarca, C.1    Paigen, K.2
  • 19
    • 0023221206 scopus 로고
    • Spectrophotometric determination of oxidized and reduced pyridine nucleotides in erythrocytes using a single extraction procedure
    • C.R. Zerez, S.J. Lee, K.R. Tanaka, Spectrophotometric determination of oxidized and reduced pyridine nucleotides in erythrocytes using a single extraction procedure, Anal. Biochem. 164 (1987) 367-373.
    • (1987) Anal. Biochem. , vol.164 , pp. 367-373
    • Zerez, C.R.1    Lee, S.J.2    Tanaka, K.R.3
  • 20
    • 0002502978 scopus 로고
    • Recommendations for determining the catalytic concentration of lactate dehydrogenase in human serum at 30°C
    • Commission Enzymologie de la Société Francaise de Biologie Clinique, Recommendations for determining the catalytic concentration of lactate dehydrogenase in human serum at 30°C, Ann. Biol. Clin. 40 (1982) 291-306.
    • (1982) Ann. Biol. Clin. , vol.40 , pp. 291-306
  • 21
    • 0023551497 scopus 로고
    • Connexin 43, a protein from rat heart homologous to a gap junction protein from liver
    • E.C. Beyer, D.L. Paul, D.A. Goodenough, Connexin 43, a protein from rat heart homologous to a gap junction protein from liver, J. Cell Biol. 105 (1987) 2621-2629.
    • (1987) J. Cell Biol. , vol.105 , pp. 2621-2629
    • Beyer, E.C.1    Paul, D.L.2    Goodenough, D.A.3
  • 22
    • 0026515733 scopus 로고
    • Development and characterization of a rapidly proliferating, well-differentiated cell line derived from normal adult osteoblast-like cells transfected with SV40 large T antigen
    • P.E. Keeting, R.E. Scott, D.S. Colvard, M.A. Anderson, M.J. Oursler, T.C. Spelsberg, B.L. Riggs, Development and characterization of a rapidly proliferating, well-differentiated cell line derived from normal adult osteoblast-like cells transfected with SV40 large T antigen, J. Bone Min. Res. 7 (1992) 127-136.
    • (1992) J. Bone Min. Res. , vol.7 , pp. 127-136
    • Keeting, P.E.1    Scott, R.E.2    Colvard, D.S.3    Anderson, M.A.4    Oursler, M.J.5    Spelsberg, T.C.6    Riggs, B.L.7
  • 23
    • 0034617096 scopus 로고    scopus 로고
    • Interaction of two classes of ADP-ribose transfer reactions in immune signaling
    • M.K. Han, Y.S. Cho, Y.S. Kim, C.Y. Yim, U.H. Kim, Interaction of two classes of ADP-ribose transfer reactions in immune signaling, J. Biol. Chem. 275 (2000) 20799-20805.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20799-20805
    • Han, M.K.1    Cho, Y.S.2    Kim, Y.S.3    Yim, C.Y.4    Kim, U.H.5
  • 24
    • 0027180293 scopus 로고
    • Purification and characterization of NAD glycohydrolase from rabbit erythrocytes
    • U.H. Kim, M.K. Kim, J.S. Han, M.K. Park, H.R. Kim, Purification and characterization of NAD glycohydrolase from rabbit erythrocytes, Arch. Biochem. Biophys. 305 (1993) 147-152.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 147-152
    • Kim, U.H.1    Kim, M.K.2    Han, J.S.3    Park, M.K.4    Kim, H.R.5
  • 26
    • 0025316785 scopus 로고
    • Progressive development of the rat osteoblast phenotype in vitro: Reciprocal relationship in expression of genes associated with osteoblasts proliferation and differentiation during formation of the bone extracellular matrix
    • T.A. Owen, M. Aronow, V. Shalhoub, L.M. Barone, L. Wilming, M.S. Tassinari, M.B. Kennedy, S. Pockwinse, J.B. Lian, G.S. Stein, Progressive development of the rat osteoblast phenotype in vitro: Reciprocal relationship in expression of genes associated with osteoblasts proliferation and differentiation during formation of the bone extracellular matrix, J. Cell. Physiol. 143 (1990) 420-430.
    • (1990) J. Cell. Physiol. , vol.143 , pp. 420-430
    • Owen, T.A.1    Aronow, M.2    Shalhoub, V.3    Barone, L.M.4    Wilming, L.5    Tassinari, M.S.6    Kennedy, M.B.7    Pockwinse, S.8    Lian, J.B.9    Stein, G.S.10
  • 27
    • 0032895910 scopus 로고    scopus 로고
    • 3 attenuates the confluence-dependent differences in the osteoblast characteristic proteins alkaline phosphatase, procollagen I peptide, and osteocalcin
    • 3 attenuates the confluence-dependent differences in the osteoblast characteristic proteins alkaline phosphatase, procollagen I peptide, and osteocalcin, Calcif Tissue Int. 64 (1998) 414-421.
    • (1998) Calcif Tissue Int. , vol.64 , pp. 414-421
    • Siggelkow, H.1    Schulz, H.2    Kaesler, S.3    Benzler, K.4    Atkinson, M.J.5    Hüfner, M.6
  • 28
    • 0029974655 scopus 로고    scopus 로고
    • Connections with connexins: The molecular basis of direct intercellular signaling
    • R. Bruzzone, T.W. White, D.L. Paul, Connections with connex-ins: The molecular basis of direct intercellular signaling, Eur. J. Biochem. 238 (1996) 1-27.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 1-27
    • Bruzzone, R.1    White, T.W.2    Paul, D.L.3
  • 29
    • 0029800089 scopus 로고    scopus 로고
    • Properties and regulation of gap junctional hemichannels in plasma membrane of cultured cells
    • H. Li, T.F. Liu, A. Lazrak, C. Peracchia, G.S. Goldberg, P.D. Lampe, R.G. Johnson, Properties and regulation of gap junctional hemichannels in plasma membrane of cultured cells, J. Cell Biol. 134 (1996) 1019-1030.
    • (1996) J. Cell Biol. , vol.134 , pp. 1019-1030
    • Li, H.1    Liu, T.F.2    Lazrak, A.3    Peracchia, C.4    Goldberg, G.S.5    Lampe, P.D.6    Johnson, R.G.7
  • 31
    • 0002036601 scopus 로고    scopus 로고
    • Prostaglandins and bone metabolism
    • J.P. Bilezikian, L.G. Raisz, G.A. Rodan (Eds.), Academic Press, San Diego, CA
    • C. Pilbeam, J.R. Harrison, L.G. Raisz, Prostaglandins and bone metabolism, in: J.P. Bilezikian, L.G. Raisz, G.A. Rodan (Eds.), Principles of Bone Biology, Academic Press, San Diego, CA, 1996, pp. 715-728.
    • (1996) Principles of Bone Biology , pp. 715-728
    • Pilbeam, C.1    Harrison, J.R.2    Raisz, L.G.3
  • 32
    • 0002981330 scopus 로고    scopus 로고
    • Local regulators of bone: Epidermal growth factor-transforming growth factor α
    • J.P. Bilezikian, L.G. Raisz, G.A. Rodan (Eds.), Academic Press, San Diego, CA
    • T. Yoneda, Local regulators of bone: Epidermal growth factor-transforming growth factor α, in: J.P. Bilezikian, L.G. Raisz, G.A. Rodan (Eds.), Principles of Bone Biology, Academic Press, San Diego, CA, 1996, pp. 729-738.
    • (1996) Principles of Bone Biology , pp. 729-738
    • Yoneda, T.1
  • 33
    • 0002591095 scopus 로고    scopus 로고
    • Local regulators of bone: IL-1, TNF, lymphotoxin, interferon-γ, IL-8, IL-10, IL-4, the LIF/IL-6 family and additional cytokines
    • J.P. Bilezikian, L.G. Raisz, G.A. Rodan (Eds.), Academic Press, San Diego, CA
    • M.C. Horowitz, J.A. Lorenzo, Local regulators of bone: IL-1, TNF, lymphotoxin, interferon-γ, IL-8, IL-10, IL-4, the LIF/IL-6 family and additional cytokines, in: J.P. Bilezikian, L.G. Raisz, G.A. Rodan (Eds.), Principles of Bone Biology, Academic Press, San Diego, CA, 1996, pp. 687-700.
    • (1996) Principles of Bone Biology , pp. 687-700
    • Horowitz, M.C.1    Lorenzo, J.A.2
  • 34
    • 0035409337 scopus 로고    scopus 로고
    • Regulation of spontaneous glutamate release activity in osteoblastic cells and its role in differentiation and survival: Evidence for intrinsic glutamatergic signaling in bone
    • P.G. Genever, T.M. Skerry, Regulation of spontaneous glutamate release activity in osteoblastic cells and its role in differentiation and survival: Evidence for intrinsic glutamatergic signaling in bone, FESEB J. 15 (2001) 1586-1588.
    • (2001) FESEB J. , vol.15 , pp. 1586-1588
    • Genever, P.G.1    Skerry, T.M.2
  • 35
    • 0034899682 scopus 로고    scopus 로고
    • Evidence for a role of cyclic ADP-ribose in calcium signalling and in neurotransmitter release in cultured astrocytes
    • C. Verderio, S. Bruzzone, E. Zocchi, E. Fedele, U. Schenk, A. De Flora, M. Matteoli, Evidence for a role of cyclic ADP-ribose in calcium signalling and in neurotransmitter release in cultured astrocytes, J. Neurochem. 78 (2001) 646-657.
    • (2001) J. Neurochem. , vol.78 , pp. 646-657
    • Verderio, C.1    Bruzzone, S.2    Zocchi, E.3    Fedele, E.4    Schenk, U.5    De Flora, A.6    Matteoli, M.7
  • 36
    • 0002303623 scopus 로고    scopus 로고
    • Mechanisms regulating osteoblast proliferation and differentiation
    • J.P. Bilezikian, L.G. Raisz, G.A. Rodan (Eds.), Academic Press, San Diego, CA
    • G.S. Stein, J.B. Lian, J.L. Stein, A.J. van Wijnen, B. Frenkel, M. Montecino, Mechanisms regulating osteoblast proliferation and differentiation, in: J.P. Bilezikian, L.G. Raisz, G.A. Rodan (Eds.), Principles of Bone Biology, Academic Press, San Diego, CA, 1996, pp. 69-86.
    • (1996) Principles of Bone Biology , pp. 69-86
    • Stein, G.S.1    Lian, J.B.2    Stein, J.L.3    Van Wijnen, A.J.4    Frenkel, B.5    Montecino, M.6


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