메뉴 건너뛰기




Volumn 39, Issue 5, 2006, Pages 1008-1017

Shedding of a soluble form of BMP receptor-IB controls bone cell responses to BMP

Author keywords

Bone cells; Bone morphogenetic protein; Bone morphogenetic protein receptor; Shedding; Soluble receptor

Indexed keywords

ALKALINE PHOSPHATASE; BONE MORPHOGENETIC PROTEIN; BONE MORPHOGENETIC PROTEIN 2; BONE MORPHOGENETIC PROTEIN RECEPTOR; BONE MORPHOGENETIC PROTEIN RECEPTOR 1A; BONE MORPHOGENETIC PROTEIN RECEPTOR 1B; BONE MORPHOGENETIC PROTEIN RECEPTOR 2; INTERLEUKIN 1BETA; MESSENGER RNA; OSTEOCALCIN; PHORBOL 12 ACETATE 13 MYRISTATE; SMAD1 PROTEIN; SMAD5 PROTEIN; UNCLASSIFIED DRUG;

EID: 33749532652     PISSN: 87563282     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bone.2006.04.030     Document Type: Article
Times cited : (14)

References (62)
  • 3
    • 0031105160 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: an unconventional approach to isolation of first mammalian morphogens
    • Reddi A.H. Bone morphogenetic proteins: an unconventional approach to isolation of first mammalian morphogens. Cytokine Growth Factor Rev 8 (1997) 11-20
    • (1997) Cytokine Growth Factor Rev , vol.8 , pp. 11-20
    • Reddi, A.H.1
  • 4
    • 0034122107 scopus 로고    scopus 로고
    • Bone morphogenetic proteins and skeletal development: the kidney-bone connection
    • Reddi A.H. Bone morphogenetic proteins and skeletal development: the kidney-bone connection. Pediatr Nephrol 14 (2000) 598-601
    • (2000) Pediatr Nephrol , vol.14 , pp. 598-601
    • Reddi, A.H.1
  • 5
    • 0042360393 scopus 로고    scopus 로고
    • The application of bone morphogenetic proteins to dental tissue engineering
    • Nakashima M., and Reddi A.H. The application of bone morphogenetic proteins to dental tissue engineering. Nat Biotechnol 21 (2003) 1025-1032
    • (2003) Nat Biotechnol , vol.21 , pp. 1025-1032
    • Nakashima, M.1    Reddi, A.H.2
  • 6
    • 0033200373 scopus 로고    scopus 로고
    • BMP signalling in early Xenopus development
    • Dale L., and Jones C.M. BMP signalling in early Xenopus development. Bioessays 21 (1999) 751-760
    • (1999) Bioessays , vol.21 , pp. 751-760
    • Dale, L.1    Jones, C.M.2
  • 7
    • 0036789641 scopus 로고    scopus 로고
    • Bone growth factors in maxillofacial skeletal reconstruction
    • Schilephake H. Bone growth factors in maxillofacial skeletal reconstruction. Int J Oral Maxillofac Surg 31 (2002) 469-484
    • (2002) Int J Oral Maxillofac Surg , vol.31 , pp. 469-484
    • Schilephake, H.1
  • 8
  • 9
    • 0034242765 scopus 로고    scopus 로고
    • Evaluation of recombinant human bone morphogenetic protein-2 in oral applications including the use of endosseous implants: 3-year results of a pilot study in humans
    • Cochran D.L., Jones A.A., Lilly L.C., Fiorellini J.P., and Howell H. Evaluation of recombinant human bone morphogenetic protein-2 in oral applications including the use of endosseous implants: 3-year results of a pilot study in humans. J Periodontol 71 (2000) 1241-1257
    • (2000) J Periodontol , vol.71 , pp. 1241-1257
    • Cochran, D.L.1    Jones, A.A.2    Lilly, L.C.3    Fiorellini, J.P.4    Howell, H.5
  • 10
  • 11
    • 0042134565 scopus 로고    scopus 로고
    • Osteogenic activity of the fourteen types of human bone morphogenetic proteins (BMPs)
    • Cheng H., Jiang W., Phillips F.M., Haydon R.C., Peng Y., Zhou L., et al. Osteogenic activity of the fourteen types of human bone morphogenetic proteins (BMPs). J Bone Jt Surg Am 85-A (2003) 1544-1552
    • (2003) J Bone Jt Surg Am , vol.85 -A , pp. 1544-1552
    • Cheng, H.1    Jiang, W.2    Phillips, F.M.3    Haydon, R.C.4    Peng, Y.5    Zhou, L.6
  • 12
    • 0037587239 scopus 로고    scopus 로고
    • Bone regeneration in critical size defects by cell-mediated BMP-2 gene transfer: a comparison of adenoviral vectors and liposomes
    • Park J., Ries J., Gelse K., Kloss F., von der M.K., Wiltfang J., et al. Bone regeneration in critical size defects by cell-mediated BMP-2 gene transfer: a comparison of adenoviral vectors and liposomes. Gene Ther 10 (2003) 1089-1098
    • (2003) Gene Ther , vol.10 , pp. 1089-1098
    • Park, J.1    Ries, J.2    Gelse, K.3    Kloss, F.4    von der, M.K.5    Wiltfang, J.6
  • 13
    • 0346996450 scopus 로고    scopus 로고
    • Signal transduction of bone morphogenetic protein receptors
    • Nohe A., Keating E., Knaus P., and Petersen N.O. Signal transduction of bone morphogenetic protein receptors. Cell Signal 16 (2004) 291-299
    • (2004) Cell Signal , vol.16 , pp. 291-299
    • Nohe, A.1    Keating, E.2    Knaus, P.3    Petersen, N.O.4
  • 14
    • 0028332818 scopus 로고
    • Identification of type I receptors for osteogenic protein-1 and bone morphogenetic protein-4
    • ten Dijke P., Yamashita H., Sampath T.K., Reddi A.H., Estevez M., Riddle D.L., et al. Identification of type I receptors for osteogenic protein-1 and bone morphogenetic protein-4. J Biol Chem 269 (1994) 16985-16988
    • (1994) J Biol Chem , vol.269 , pp. 16985-16988
    • ten Dijke, P.1    Yamashita, H.2    Sampath, T.K.3    Reddi, A.H.4    Estevez, M.5    Riddle, D.L.6
  • 15
    • 0029153741 scopus 로고
    • Identification of a human type II receptor for bone morphogenetic protein-4 that forms differential heteromeric complexes with bone morphogenetic protein type I receptors
    • Nohno T., Ishikawa T., Saito T., Hosokawa K., Noji S., Wolsing D.H., et al. Identification of a human type II receptor for bone morphogenetic protein-4 that forms differential heteromeric complexes with bone morphogenetic protein type I receptors. J Biol Chem 270 (1995) 22522-22526
    • (1995) J Biol Chem , vol.270 , pp. 22522-22526
    • Nohno, T.1    Ishikawa, T.2    Saito, T.3    Hosokawa, K.4    Noji, S.5    Wolsing, D.H.6
  • 16
    • 0029008597 scopus 로고
    • Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs
    • Liu F., Ventura F., Doody J., and Massague J. Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs. Mol Cell Biol 15 (1995) 3479-3486
    • (1995) Mol Cell Biol , vol.15 , pp. 3479-3486
    • Liu, F.1    Ventura, F.2    Doody, J.3    Massague, J.4
  • 18
    • 0042134658 scopus 로고    scopus 로고
    • Signal transduction of bone morphogenetic proteins in osteoblast differentiation
    • ten Dijke P., Fu J., Schaap P., and Roelen B.A.J. Signal transduction of bone morphogenetic proteins in osteoblast differentiation. J Bone Jt Surg 85 (2003) 34-38
    • (2003) J Bone Jt Surg , vol.85 , pp. 34-38
    • ten Dijke, P.1    Fu, J.2    Schaap, P.3    Roelen, B.A.J.4
  • 19
    • 0037144841 scopus 로고    scopus 로고
    • TGF beta receptor internalization into EEA1-enriched early endosomes: role in signaling to Smad2
    • Hayes S., Chawla A., and Corvera S. TGF beta receptor internalization into EEA1-enriched early endosomes: role in signaling to Smad2. J Cell Biol 158 (2002) 1239-1249
    • (2002) J Cell Biol , vol.158 , pp. 1239-1249
    • Hayes, S.1    Chawla, A.2    Corvera, S.3
  • 20
    • 0037598870 scopus 로고    scopus 로고
    • Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover
    • Di Guglielmo G.M., Le C., Roy A.F., and Goodfellow J.L. Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover. Nat Cell Biol 5 (2003) 410-421
    • (2003) Nat Cell Biol , vol.5 , pp. 410-421
    • Di Guglielmo, G.M.1    Le, C.2    Roy, A.F.3    Goodfellow, J.L.4
  • 21
    • 0030728295 scopus 로고    scopus 로고
    • Distinct endocytic responses of heteromeric and homomeric transforming growth factor beta receptors
    • Anders R.A., Arline S.L., Dore J.J., and Leof E.B. Distinct endocytic responses of heteromeric and homomeric transforming growth factor beta receptors. Mol Biol Cell 8 (1997) 2133-2143
    • (1997) Mol Biol Cell , vol.8 , pp. 2133-2143
    • Anders, R.A.1    Arline, S.L.2    Dore, J.J.3    Leof, E.B.4
  • 22
    • 0035158960 scopus 로고    scopus 로고
    • Mechanisms of transforming growth factor-beta receptor endocytosis and intracellular sorting differ between fibroblasts and epithelial cells
    • Dore Jr. J.J., Yao D., Edens M., Garamszegi N., Sholl E.L., and Leof E.B. Mechanisms of transforming growth factor-beta receptor endocytosis and intracellular sorting differ between fibroblasts and epithelial cells. Mol Biol Cell 12 (2001) 675-684
    • (2001) Mol Biol Cell , vol.12 , pp. 675-684
    • Dore Jr., J.J.1    Yao, D.2    Edens, M.3    Garamszegi, N.4    Sholl, E.L.5    Leof, E.B.6
  • 23
    • 0030985618 scopus 로고    scopus 로고
    • Internalization and intracellular processing of bone morphogenetic protein (BMP) in rat skeletal muscle myoblasts (L6)
    • Jortikka L., Laitinen M., Lindholm T.S., and Marttinen A. Internalization and intracellular processing of bone morphogenetic protein (BMP) in rat skeletal muscle myoblasts (L6). Cell Signal 9 (1997) 47-51
    • (1997) Cell Signal , vol.9 , pp. 47-51
    • Jortikka, L.1    Laitinen, M.2    Lindholm, T.S.3    Marttinen, A.4
  • 24
    • 0032223679 scopus 로고    scopus 로고
    • PDGF-alpha receptor subunit expression down-regulated by IL-1beta in human periodontal ligament cells
    • Oates T.W., Xie J.F., Clinton S., Hoang A.M., Graves D.T., and Cochran D.L. PDGF-alpha receptor subunit expression down-regulated by IL-1beta in human periodontal ligament cells. J Dent Res 77 (1998) 1791-1798
    • (1998) J Dent Res , vol.77 , pp. 1791-1798
    • Oates, T.W.1    Xie, J.F.2    Clinton, S.3    Hoang, A.M.4    Graves, D.T.5    Cochran, D.L.6
  • 25
    • 0033532191 scopus 로고    scopus 로고
    • Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival
    • Lum L., Wong B.R., Josien R., Becherer J.D., Erdjument-Bromage H., Schlondorff J., et al. Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival. J Biol Chem 274 (1999) 13613-13618
    • (1999) J Biol Chem , vol.274 , pp. 13613-13618
    • Lum, L.1    Wong, B.R.2    Josien, R.3    Becherer, J.D.4    Erdjument-Bromage, H.5    Schlondorff, J.6
  • 26
    • 0033135695 scopus 로고    scopus 로고
    • Ectodomain cleavage and shedding of the type III transforming growth factor-beta receptor in lung membranes effect of temperature, ligand binding and membrane solubilization
    • Philip A., Hannah R., and O'connor-McCourt M. Ectodomain cleavage and shedding of the type III transforming growth factor-beta receptor in lung membranes effect of temperature, ligand binding and membrane solubilization. Eur J Biochem 261 (1999) 618-628
    • (1999) Eur J Biochem , vol.261 , pp. 618-628
    • Philip, A.1    Hannah, R.2    O'connor-McCourt, M.3
  • 27
    • 0033560025 scopus 로고    scopus 로고
    • Inflammatory cytokines and vascular endothelial growth factor stimulate the release of soluble tie receptor from human endothelial cells via metalloprotease activation
    • Yabkowitz R., Meyer S., Black T., Elliott G., Merewether L.A., and Yamane H.K. Inflammatory cytokines and vascular endothelial growth factor stimulate the release of soluble tie receptor from human endothelial cells via metalloprotease activation. Blood 93 (1999) 1969-1979
    • (1999) Blood , vol.93 , pp. 1969-1979
    • Yabkowitz, R.1    Meyer, S.2    Black, T.3    Elliott, G.4    Merewether, L.A.5    Yamane, H.K.6
  • 28
    • 0035793430 scopus 로고    scopus 로고
    • Structural characterization of the circulating soluble FGF receptors reveals multiple isoforms generated by secretion and ectodomain shedding
    • Hanneken A. Structural characterization of the circulating soluble FGF receptors reveals multiple isoforms generated by secretion and ectodomain shedding. FEBS Lett 489 (2001) 176-181
    • (2001) FEBS Lett , vol.489 , pp. 176-181
    • Hanneken, A.1
  • 29
    • 0141509970 scopus 로고    scopus 로고
    • Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is mediated by tumor necrosis factor-alpha-converting enzyme (ADAM 17)
    • Garton K.J., Gough P.J., Philalay J., Wille P.T., Blobel C.P., Whitehead R.H., et al. Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is mediated by tumor necrosis factor-alpha-converting enzyme (ADAM 17). J Biol Chem 278 (2003) 37459-37464
    • (2003) J Biol Chem , vol.278 , pp. 37459-37464
    • Garton, K.J.1    Gough, P.J.2    Philalay, J.3    Wille, P.T.4    Blobel, C.P.5    Whitehead, R.H.6
  • 30
    • 1942466613 scopus 로고    scopus 로고
    • Soluble vascular endothelial growth factor receptor 1, and not receptor 2, is an independent prognostic factor in acute myeloid leukemia and myelodysplastic syndromes
    • Hu Q., Dey A.L., Yang Y., Shen Y., Jilani I.B., Estey E.H., et al. Soluble vascular endothelial growth factor receptor 1, and not receptor 2, is an independent prognostic factor in acute myeloid leukemia and myelodysplastic syndromes. Cancer 100 (2004) 1884-1891
    • (2004) Cancer , vol.100 , pp. 1884-1891
    • Hu, Q.1    Dey, A.L.2    Yang, Y.3    Shen, Y.4    Jilani, I.B.5    Estey, E.H.6
  • 31
    • 1442358746 scopus 로고    scopus 로고
    • Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands
    • Sahin U., Weskamp G., Kelly K., Zhou H.M., Higashiyama S., Peschon J., et al. Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands. J Cell Biol 164 (2004) 769-779
    • (2004) J Cell Biol , vol.164 , pp. 769-779
    • Sahin, U.1    Weskamp, G.2    Kelly, K.3    Zhou, H.M.4    Higashiyama, S.5    Peschon, J.6
  • 32
    • 0036122955 scopus 로고    scopus 로고
    • Transmodulation of cell surface regulatory molecules via ectodomain shedding
    • Dello S.P., and Rovida E. Transmodulation of cell surface regulatory molecules via ectodomain shedding. Biol Chem 383 (2002) 69-83
    • (2002) Biol Chem , vol.383 , pp. 69-83
    • Dello, S.P.1    Rovida, E.2
  • 33
    • 13344250490 scopus 로고    scopus 로고
    • Interleukin-6 and soluble interleukin-6 receptors in the synovial fluids from rheumatoid arthritis patients are responsible for osteoclast-like cell formation
    • Kotake S., Sato K., Kim K.J., Takahashi N., Udagawa N., Nakamura I., et al. Interleukin-6 and soluble interleukin-6 receptors in the synovial fluids from rheumatoid arthritis patients are responsible for osteoclast-like cell formation. J Bone Miner Res 11 (1996) 88-95
    • (1996) J Bone Miner Res , vol.11 , pp. 88-95
    • Kotake, S.1    Sato, K.2    Kim, K.J.3    Takahashi, N.4    Udagawa, N.5    Nakamura, I.6
  • 34
    • 0035164602 scopus 로고    scopus 로고
    • The soluble interleukin 6 receptor: mechanisms of production and implications in disease
    • Jones S.A., Horiuchi S., Topley N., Yamamoto N., and Fuller G.M. The soluble interleukin 6 receptor: mechanisms of production and implications in disease. FASEB J 15 (2001) 43-58
    • (2001) FASEB J , vol.15 , pp. 43-58
    • Jones, S.A.1    Horiuchi, S.2    Topley, N.3    Yamamoto, N.4    Fuller, G.M.5
  • 35
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells
    • Black R.A., Rauch C.T., Kozlosky C.J., Peschon J.J., Slack J.L., Wolfson M.F., et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385 (1997) 729-733
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3    Peschon, J.J.4    Slack, J.L.5    Wolfson, M.F.6
  • 36
    • 0031569611 scopus 로고    scopus 로고
    • Constitutive shedding of both p55 and p75 murine TNF receptors in vivo
    • Pinckard J.K., Sheehan K.C., Arthur C.D., and Schreiber R.D. Constitutive shedding of both p55 and p75 murine TNF receptors in vivo. J Immunol 158 (1997) 3869-3873
    • (1997) J Immunol , vol.158 , pp. 3869-3873
    • Pinckard, J.K.1    Sheehan, K.C.2    Arthur, C.D.3    Schreiber, R.D.4
  • 37
    • 0037053394 scopus 로고    scopus 로고
    • Shedding of the interleukin-6 (IL-6) receptor (gp80) determines the ability of IL-6 to induce gp130 phosphorylation in human osteoblasts
    • Vermes C., Jacobs J.J., Zhang J., Firneisz G., Roebuck K.A., and Glant T.T. Shedding of the interleukin-6 (IL-6) receptor (gp80) determines the ability of IL-6 to induce gp130 phosphorylation in human osteoblasts. J Biol Chem 277 (2002) 16879-16887
    • (2002) J Biol Chem , vol.277 , pp. 16879-16887
    • Vermes, C.1    Jacobs, J.J.2    Zhang, J.3    Firneisz, G.4    Roebuck, K.A.5    Glant, T.T.6
  • 38
    • 4143111325 scopus 로고    scopus 로고
    • The mechanism of cleavage of EGFR ligands induced by inflammatory cytokines in gastric cancer cells
    • Tanida S., Joh T., Itoh K., Kataoka H., Sasaki M., Ohara H., et al. The mechanism of cleavage of EGFR ligands induced by inflammatory cytokines in gastric cancer cells. Gastroenterology 127 (2004) 559-569
    • (2004) Gastroenterology , vol.127 , pp. 559-569
    • Tanida, S.1    Joh, T.2    Itoh, K.3    Kataoka, H.4    Sasaki, M.5    Ohara, H.6
  • 39
    • 19944430946 scopus 로고    scopus 로고
    • Interleukin-6 receptor shedding is enhanced by interleukin-1beta and tumor necrosis factor alpha and is partially mediated by tumor necrosis factor alpha-converting enzyme in osteoblast-like cells
    • Franchimont N., Lambert C., Huynen P., Ribbens C., Relic B., Chariot A., et al. Interleukin-6 receptor shedding is enhanced by interleukin-1beta and tumor necrosis factor alpha and is partially mediated by tumor necrosis factor alpha-converting enzyme in osteoblast-like cells. Arthritis Rheum 52 (2005) 84-93
    • (2005) Arthritis Rheum , vol.52 , pp. 84-93
    • Franchimont, N.1    Lambert, C.2    Huynen, P.3    Ribbens, C.4    Relic, B.5    Chariot, A.6
  • 40
    • 0034815142 scopus 로고    scopus 로고
    • Opposite effects of bone morphogenetic protein-2 and transforming growth factor-beta1 on osteoblast differentiation
    • Spinella-Jaegle S., Roman-Roman S., Faucheu C., Dunn F.W., Kawai S., Gallea S., et al. Opposite effects of bone morphogenetic protein-2 and transforming growth factor-beta1 on osteoblast differentiation. Bone 29 (2001) 323-330
    • (2001) Bone , vol.29 , pp. 323-330
    • Spinella-Jaegle, S.1    Roman-Roman, S.2    Faucheu, C.3    Dunn, F.W.4    Kawai, S.5    Gallea, S.6
  • 41
    • 0026216602 scopus 로고
    • Characterization of endosteal osteoblasts isolated from human maxilla and mandible: an experimental system for biocompatibility tests
    • Doglioli P., and Scortecci G. Characterization of endosteal osteoblasts isolated from human maxilla and mandible: an experimental system for biocompatibility tests. Cytotechnology 7 (1991) 39-48
    • (1991) Cytotechnology , vol.7 , pp. 39-48
    • Doglioli, P.1    Scortecci, G.2
  • 42
    • 30844465511 scopus 로고    scopus 로고
    • Influence of harvesting technique and donor site location on in vitro growth of osteoblastlike cells from facial bone
    • Pradel W., Tenbieg P., and Lauer G. Influence of harvesting technique and donor site location on in vitro growth of osteoblastlike cells from facial bone. Int J Oral Maxillofac Implants 20 (2005) 860-866
    • (2005) Int J Oral Maxillofac Implants , vol.20 , pp. 860-866
    • Pradel, W.1    Tenbieg, P.2    Lauer, G.3
  • 43
    • 0035007415 scopus 로고    scopus 로고
    • Retroviral transduction of alveolar bone cells with a temperature-sensitive SV40 large T antigen
    • Salih V., Knowles J.C., O'Hare M.J., and Olsen I. Retroviral transduction of alveolar bone cells with a temperature-sensitive SV40 large T antigen. Cell Tissue Res 304 (2001) 371-376
    • (2001) Cell Tissue Res , vol.304 , pp. 371-376
    • Salih, V.1    Knowles, J.C.2    O'Hare, M.J.3    Olsen, I.4
  • 44
    • 0035433938 scopus 로고    scopus 로고
    • Flow cytometry analysis of guided tissue regeneration-associated human periodontal cells
    • Kuru L., Parkar M.H., Griffiths G.S., and Olsen I. Flow cytometry analysis of guided tissue regeneration-associated human periodontal cells. J Periodontol 72 (2001) 1016-1024
    • (2001) J Periodontol , vol.72 , pp. 1016-1024
    • Kuru, L.1    Parkar, M.H.2    Griffiths, G.S.3    Olsen, I.4
  • 45
    • 0023202335 scopus 로고
    • Expression of differentiated function by mineralizing cultures of chicken osteoblasts
    • Gerstenfeld L.C., Chipman S.D., Glowacki J., and Lian J.B. Expression of differentiated function by mineralizing cultures of chicken osteoblasts. Dev Biol 122 (1987) 49-60
    • (1987) Dev Biol , vol.122 , pp. 49-60
    • Gerstenfeld, L.C.1    Chipman, S.D.2    Glowacki, J.3    Lian, J.B.4
  • 46
    • 0027181746 scopus 로고
    • Kinetics of in vitro mineralization by an osteogenic clonal cell line (C1) derived from mouse teratocarcinoma
    • Chentoufi J., Hott M., Lamblin D., Buc-Caron M.H., Marie P.J., and Kellermann O. Kinetics of in vitro mineralization by an osteogenic clonal cell line (C1) derived from mouse teratocarcinoma. Differentiation 53 (1993) 181-189
    • (1993) Differentiation , vol.53 , pp. 181-189
    • Chentoufi, J.1    Hott, M.2    Lamblin, D.3    Buc-Caron, M.H.4    Marie, P.J.5    Kellermann, O.6
  • 48
    • 0028226196 scopus 로고
    • Soluble receptors for cytokines and growth factors: generation and biological function
    • Rose-John S., and Heinrich P.C. Soluble receptors for cytokines and growth factors: generation and biological function. Biochem J 300 (1994) 281-290
    • (1994) Biochem J , vol.300 , pp. 281-290
    • Rose-John, S.1    Heinrich, P.C.2
  • 50
    • 0029932769 scopus 로고    scopus 로고
    • Purification and characterization of the soluble interleukin-6 receptor from human plasma and identification of an isoform generated through alternative splicing
    • Muller-Newen G., Kohne C., Keul R., Hemmann U., Muller-Esterl W., Wijdenes J., et al. Purification and characterization of the soluble interleukin-6 receptor from human plasma and identification of an isoform generated through alternative splicing. Eur J Biochem 236 (1996) 837-842
    • (1996) Eur J Biochem , vol.236 , pp. 837-842
    • Muller-Newen, G.1    Kohne, C.2    Keul, R.3    Hemmann, U.4    Muller-Esterl, W.5    Wijdenes, J.6
  • 51
    • 0029853095 scopus 로고    scopus 로고
    • Pervanadate activation of intracellular kinases leads to tyrosine phosphorylation and shedding of syndecan-1
    • Reiland J., Ott V.L., Lebakken C.S., Yeaman C., McCarthy J., and Rapraeger A.C. Pervanadate activation of intracellular kinases leads to tyrosine phosphorylation and shedding of syndecan-1. Biochem J 319 (1996) 39-47
    • (1996) Biochem J , vol.319 , pp. 39-47
    • Reiland, J.1    Ott, V.L.2    Lebakken, C.S.3    Yeaman, C.4    McCarthy, J.5    Rapraeger, A.C.6
  • 52
    • 0029764504 scopus 로고    scopus 로고
    • Selective cleavage of the heregulin receptor ErbB-4 by protein kinase C activation
    • Vecchi M., Baulida J., and Carpenter G. Selective cleavage of the heregulin receptor ErbB-4 by protein kinase C activation. J Biol Chem 271 (1996) 18989-18995
    • (1996) J Biol Chem , vol.271 , pp. 18989-18995
    • Vecchi, M.1    Baulida, J.2    Carpenter, G.3
  • 53
    • 0030661989 scopus 로고    scopus 로고
    • Constitutive proteolysis of the ErbB-4 receptor tyrosine kinase by a unique, sequential mechanism
    • Vecchi M., and Carpenter G. Constitutive proteolysis of the ErbB-4 receptor tyrosine kinase by a unique, sequential mechanism. J Cell Biol 139 (1997) 995-1003
    • (1997) J Cell Biol , vol.139 , pp. 995-1003
    • Vecchi, M.1    Carpenter, G.2
  • 54
    • 0032487494 scopus 로고    scopus 로고
    • An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3
    • Izumi Y., Hirose T., Tamai Y., Hirai S., Nagashima Y., Fujimoto T., et al. An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3. J Cell Biol 143 (1998) 95-106
    • (1998) J Cell Biol , vol.143 , pp. 95-106
    • Izumi, Y.1    Hirose, T.2    Tamai, Y.3    Hirai, S.4    Nagashima, Y.5    Fujimoto, T.6
  • 55
    • 0032493646 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and proteolysis. Pervanadate-induced, metalloprotease-dependent cleavage of the ErbB-4 receptor and amphiregulin
    • Vecchi M., Rudolph-Owen L.A., Brown C.L., Dempsey P.J., and Carpenter G. Tyrosine phosphorylation and proteolysis. Pervanadate-induced, metalloprotease-dependent cleavage of the ErbB-4 receptor and amphiregulin. J Biol Chem 273 (1998) 20589-20595
    • (1998) J Biol Chem , vol.273 , pp. 20589-20595
    • Vecchi, M.1    Rudolph-Owen, L.A.2    Brown, C.L.3    Dempsey, P.J.4    Carpenter, G.5
  • 56
    • 0033618401 scopus 로고    scopus 로고
    • Cell volume-dependent regulation of L-selectin shedding in neutrophils. A role for p38 mitogen-activated protein kinase
    • Rizoli S.B., Rotstein O.D., and Kapus A. Cell volume-dependent regulation of L-selectin shedding in neutrophils. A role for p38 mitogen-activated protein kinase. J Biol Chem 274 (1999) 22072-22080
    • (1999) J Biol Chem , vol.274 , pp. 22072-22080
    • Rizoli, S.B.1    Rotstein, O.D.2    Kapus, A.3
  • 57
    • 0035839427 scopus 로고    scopus 로고
    • A dual signaling cascade that regulates the ectodomain shedding of heparin-binding epidermal growth factor-like growth factor
    • Umata T., Hirata M., Takahashi T., Ryu F., Shida S., Takahashi Y., et al. A dual signaling cascade that regulates the ectodomain shedding of heparin-binding epidermal growth factor-like growth factor. J Biol Chem 276 (2001) 30475-30482
    • (2001) J Biol Chem , vol.276 , pp. 30475-30482
    • Umata, T.1    Hirata, M.2    Takahashi, T.3    Ryu, F.4    Shida, S.5    Takahashi, Y.6
  • 58
    • 0032994043 scopus 로고    scopus 로고
    • Signal transduction by bone morphogenetic protein receptors: functional roles of Smad proteins
    • Miyazono K. Signal transduction by bone morphogenetic protein receptors: functional roles of Smad proteins. Bone 25 (1999) 91-93
    • (1999) Bone , vol.25 , pp. 91-93
    • Miyazono, K.1
  • 59
    • 0028904472 scopus 로고
    • Interleukin-1 modulates phosphorylation of proteins in human osteoblastic cells
    • Kang Y.M., Yeh Y.L., and Graves D.T. Interleukin-1 modulates phosphorylation of proteins in human osteoblastic cells. J Bone Miner Res 10 (1995) 96-105
    • (1995) J Bone Miner Res , vol.10 , pp. 96-105
    • Kang, Y.M.1    Yeh, Y.L.2    Graves, D.T.3
  • 60
    • 0037102474 scopus 로고    scopus 로고
    • Mechanism for the action of bone morphogenetic proteins and regulation of their activity
    • Ebara S., and Nakayama K. Mechanism for the action of bone morphogenetic proteins and regulation of their activity. Spine 27 (2002) S10-S15
    • (2002) Spine , vol.27
    • Ebara, S.1    Nakayama, K.2
  • 61
    • 0036957713 scopus 로고    scopus 로고
    • Differentiation of murine preosteoblastic KS483 cells depends on autocrine bone morphogenetic protein signaling during all phases of osteoblast formation
    • van der H.G., van Bezooijen R.L., Deckers M.M., Hoogendam J., Visser A., Lowik C.W., et al. Differentiation of murine preosteoblastic KS483 cells depends on autocrine bone morphogenetic protein signaling during all phases of osteoblast formation. Bone 31 (2002) 661-669
    • (2002) Bone , vol.31 , pp. 661-669
    • van der, H.G.1    van Bezooijen, R.L.2    Deckers, M.M.3    Hoogendam, J.4    Visser, A.5    Lowik, C.W.6
  • 62
    • 17544395678 scopus 로고    scopus 로고
    • Activation of p38 and Smads mediates BMP-2 effects on human trabecular bone-derived osteoblasts
    • Noth U., Tuli R., Seghatoleslami R., Howard M., Shah A., Hall D.J., et al. Activation of p38 and Smads mediates BMP-2 effects on human trabecular bone-derived osteoblasts. Exp Cell Res 291 (2003) 201-211
    • (2003) Exp Cell Res , vol.291 , pp. 201-211
    • Noth, U.1    Tuli, R.2    Seghatoleslami, R.3    Howard, M.4    Shah, A.5    Hall, D.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.