메뉴 건너뛰기




Volumn 6, Issue 6, 2006, Pages 947-956

cAMP-PKA signaling pathway regulates bone resorption mediated by processing of cathepsin K in cultured mouse osteoclasts

Author keywords

cAMP antagonist; Cathepsin; Osteoblast; Oteoclast; Protein kinase A inhibitor

Indexed keywords

ADENYLATE CYCLASE ACTIVATOR; CALPHOSTIN C; CATHEPSIN K; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE INHIBITOR; FORSKOLIN; KT 5720; MANNOSE 6 PHOSPHATE; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; PROTEIN KINASE C; PROTEIN KINASE C INHIBITOR; RP CYCLIC AMP; UNCLASSIFIED DRUG; WORTMANNIN;

EID: 33646110737     PISSN: 15675769     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.intimp.2006.01.005     Document Type: Article
Times cited : (11)

References (41)
  • 1
    • 0141453221 scopus 로고    scopus 로고
    • Interleukin-1β and tumor necrosis factor-α induce collagenolysis and bone resorption by regulation of matrix metalloproteinase-2 in mouse calvarial bone cells
    • Moon S.K., Kang B.S., Lee Y.C., Lee T.K., and Kim C.H. Interleukin-1β and tumor necrosis factor-α induce collagenolysis and bone resorption by regulation of matrix metalloproteinase-2 in mouse calvarial bone cells. Immunopharm Immunotoxicol 25 3 (2003) 347-364
    • (2003) Immunopharm Immunotoxicol , vol.25 , Issue.3 , pp. 347-364
    • Moon, S.K.1    Kang, B.S.2    Lee, Y.C.3    Lee, T.K.4    Kim, C.H.5
  • 2
    • 0023784985 scopus 로고
    • Cellular biology and biochemical mechanism of bone resorption
    • Vaes G. Cellular biology and biochemical mechanism of bone resorption. Clin Orthop 231 (1988) 239-271
    • (1988) Clin Orthop , vol.231 , pp. 239-271
    • Vaes, G.1
  • 3
    • 4143138784 scopus 로고    scopus 로고
    • Effects of TGF-β, TNF-α, IL-β and IL-6 alone or in combination, and tyrosine kinase inhibitor on cyclooxygenase expression, prostaglandin E(2) production and bone resorption in mouse calvarial bone cells
    • Park Y.G., Kang S.K., Kim W.J., Lee Y.C., and Kim C.H. Effects of TGF-β, TNF-α, IL-β and IL-6 alone or in combination, and tyrosine kinase inhibitor on cyclooxygenase expression, prostaglandin E(2) production and bone resorption in mouse calvarial bone cells. Int J Biochem Cell Biol 36 11 (2004) 2270-2280
    • (2004) Int J Biochem Cell Biol , vol.36 , Issue.11 , pp. 2270-2280
    • Park, Y.G.1    Kang, S.K.2    Kim, W.J.3    Lee, Y.C.4    Kim, C.H.5
  • 4
    • 0026712292 scopus 로고
    • Lysosomal cysteine endopeptidases mediate interleukin 1-stimulated cartilage proteoglycan degradation
    • Buttle D.J., and Saklatvala J. Lysosomal cysteine endopeptidases mediate interleukin 1-stimulated cartilage proteoglycan degradation. Biochem J 287 (1992) 657-661
    • (1992) Biochem J , vol.287 , pp. 657-661
    • Buttle, D.J.1    Saklatvala, J.2
  • 5
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • Chapman H.A., Riese R.J., and Shi G.O. Emerging roles for cysteine proteases in human biology. Annu Rev Phys 59 (1997) 63-88
    • (1997) Annu Rev Phys , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.O.3
  • 6
    • 0021736750 scopus 로고
    • In vivo and in vitro evidence for the involvement of cysteine proteinases in bone resorption
    • Delaisse J.M., Eeckout Y., and Vaes G. In vivo and in vitro evidence for the involvement of cysteine proteinases in bone resorption. Biochem Biophys Res Commun 125 (1984) 441-447
    • (1984) Biochem Biophys Res Commun , vol.125 , pp. 441-447
    • Delaisse, J.M.1    Eeckout, Y.2    Vaes, G.3
  • 7
    • 0030850648 scopus 로고    scopus 로고
    • The expression and function of cystatin C and cathepsin B and cathepsin L during mouse embryo implantation and placentation
    • Afonso S., Romagnano L., and Babiarz B. The expression and function of cystatin C and cathepsin B and cathepsin L during mouse embryo implantation and placentation. Development 124 (1997) 3415-3425
    • (1997) Development , vol.124 , pp. 3415-3425
    • Afonso, S.1    Romagnano, L.2    Babiarz, B.3
  • 8
    • 0030949751 scopus 로고    scopus 로고
    • Macrophage cathepsin L, a factor in the erosion of subchondral bone in rheumatoid arthritis
    • Iwata Y., Mort J.S., Tateishi H., and Lee E.R. Macrophage cathepsin L, a factor in the erosion of subchondral bone in rheumatoid arthritis. Arthritis Rheum 40 (1997) 499-509
    • (1997) Arthritis Rheum , vol.40 , pp. 499-509
    • Iwata, Y.1    Mort, J.S.2    Tateishi, H.3    Lee, E.R.4
  • 9
    • 0024348296 scopus 로고
    • Suppression by cathepsin L inhibitors of the invasion of the amnion membranes by murine cancer cells
    • Yagel S., Warner A.H., Nellans H.N., Lala P.K., Waghorne C., and Denhardt D.T. Suppression by cathepsin L inhibitors of the invasion of the amnion membranes by murine cancer cells. Cancer Res 49 (1989) 3553-3557
    • (1989) Cancer Res , vol.49 , pp. 3553-3557
    • Yagel, S.1    Warner, A.H.2    Nellans, H.N.3    Lala, P.K.4    Waghorne, C.5    Denhardt, D.T.6
  • 10
    • 0026559860 scopus 로고
    • Increased expression of cathepsins L and B and decreased activity of their inhibitors in metastatic, ras-transformed NIH 3T3 cells
    • Chambers A.F., Colella R., Denhardt D.T., and Wilson S.M. Increased expression of cathepsins L and B and decreased activity of their inhibitors in metastatic, ras-transformed NIH 3T3 cells. Mol Carcin 5 (1992) 238-245
    • (1992) Mol Carcin , vol.5 , pp. 238-245
    • Chambers, A.F.1    Colella, R.2    Denhardt, D.T.3    Wilson, S.M.4
  • 11
    • 0028055132 scopus 로고
    • Cysteine proteinase inhibitors decrease articular cartilage and bone destruction in chronic inflammatory arthritis
    • Esser R.E., Angelo R.A., Murphey M.D., Watts L.M., Thornburg L.P., Palmer J.T., et al. Cysteine proteinase inhibitors decrease articular cartilage and bone destruction in chronic inflammatory arthritis. Arthritis Rheum 37 (1994) 236-247
    • (1994) Arthritis Rheum , vol.37 , pp. 236-247
    • Esser, R.E.1    Angelo, R.A.2    Murphey, M.D.3    Watts, L.M.4    Thornburg, L.P.5    Palmer, J.T.6
  • 12
    • 0023886162 scopus 로고
    • Human cathepsin B and cysteine proteinase inhibitors (CPIs) in inflammatory and metabolic joint diseases
    • Lenarcic B., Gabrijelcic D., Rozman B., Drobnic-Kosorok M., and Turk V. Human cathepsin B and cysteine proteinase inhibitors (CPIs) in inflammatory and metabolic joint diseases. Biol Chem Hoppe-Seyler 369 (1988) 257-261
    • (1988) Biol Chem Hoppe-Seyler , vol.369 , pp. 257-261
    • Lenarcic, B.1    Gabrijelcic, D.2    Rozman, B.3    Drobnic-Kosorok, M.4    Turk, V.5
  • 13
    • 0030026637 scopus 로고    scopus 로고
    • Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts
    • Bromme D., Okamoto K., Wang B.B., and Biroc S. Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. J Biol Chem 271 (1996) 2126-2132
    • (1996) J Biol Chem , vol.271 , pp. 2126-2132
    • Bromme, D.1    Okamoto, K.2    Wang, B.B.3    Biroc, S.4
  • 14
    • 0028123480 scopus 로고
    • Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts
    • Tezuka K., Tezuka Y., Maejima M., Sato T., Nemoto K., Kamioka H., et al. Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts. J Biol Chem 269 (1994) 1106-1109
    • (1994) J Biol Chem , vol.269 , pp. 1106-1109
    • Tezuka, K.1    Tezuka, Y.2    Maejima, M.3    Sato, T.4    Nemoto, K.5    Kamioka, H.6
  • 15
    • 0029097802 scopus 로고
    • Cloning and complete coding sequence of a novel human cathepsin expressed in giant cells of osteoclastomas
    • Li Y.P., Alexander M., Wucherpfennig A.L., Yelick P., Chen W., and Stashenko P. Cloning and complete coding sequence of a novel human cathepsin expressed in giant cells of osteoclastomas. J Bone Miner Res 10 (1995) 1197-1202
    • (1995) J Bone Miner Res , vol.10 , pp. 1197-1202
    • Li, Y.P.1    Alexander, M.2    Wucherpfennig, A.L.3    Yelick, P.4    Chen, W.5    Stashenko, P.6
  • 16
    • 0030463939 scopus 로고    scopus 로고
    • Cathepsin K: isolation and characterization of the murine cDNA and genomic sequence, the homologue of the human pycnodysostosis gene
    • Gelb B.D., Moissoglu K., Zhang J., Martgnetti J.A., Bromme D., and Desnick R.J. Cathepsin K: isolation and characterization of the murine cDNA and genomic sequence, the homologue of the human pycnodysostosis gene. Biochem Molec Med 59 (1996) 200-206
    • (1996) Biochem Molec Med , vol.59 , pp. 200-206
    • Gelb, B.D.1    Moissoglu, K.2    Zhang, J.3    Martgnetti, J.A.4    Bromme, D.5    Desnick, R.J.6
  • 17
    • 0030590476 scopus 로고    scopus 로고
    • Mouse cathepsin KL cDNA cloning and predominant expression of the gene in osteoclasts, and in some hypertrophying chondrocytes during mouse development
    • Rantakokko J., Aro H.T., Savontaus M., and Vuorio E. Mouse cathepsin KL cDNA cloning and predominant expression of the gene in osteoclasts, and in some hypertrophying chondrocytes during mouse development. FEBS Lett 393 (1996) 307-313
    • (1996) FEBS Lett , vol.393 , pp. 307-313
    • Rantakokko, J.1    Aro, H.T.2    Savontaus, M.3    Vuorio, E.4
  • 18
    • 0032994720 scopus 로고    scopus 로고
    • Characterization of mouse cathepsin K gene, the gene promoter, and the gene expression
    • Li Y.P., and Chen W. Characterization of mouse cathepsin K gene, the gene promoter, and the gene expression. J Bone Miner Res 14 (1999) 487-499
    • (1999) J Bone Miner Res , vol.14 , pp. 487-499
    • Li, Y.P.1    Chen, W.2
  • 19
  • 20
    • 0028831635 scopus 로고
    • Molecular cloning of human cDNA for cathepsin K. Novel cysteine proteinase predominantly expressed in bone
    • Inaoka T., Bilbe G., Ishibashi O., Tezuka K., Kumegawa M., and Kokubo T. Molecular cloning of human cDNA for cathepsin K. Novel cysteine proteinase predominantly expressed in bone. Biochem Biophys Res Commun 206 (1995) 89-96
    • (1995) Biochem Biophys Res Commun , vol.206 , pp. 89-96
    • Inaoka, T.1    Bilbe, G.2    Ishibashi, O.3    Tezuka, K.4    Kumegawa, M.5    Kokubo, T.6
  • 21
    • 0028123480 scopus 로고
    • Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts
    • Tezuka K.Y., Tezuka A., Maejima T., Sato K., Nemoto H., Kamioka Y., et al. Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts. J Biol Chem 269 (1994) 1100-1109
    • (1994) J Biol Chem , vol.269 , pp. 1100-1109
    • Tezuka, K.Y.1    Tezuka, A.2    Maejima, T.3    Sato, K.4    Nemoto, H.5    Kamioka, Y.6
  • 22
    • 0033610853 scopus 로고    scopus 로고
    • The collagenolytic activity of cathepsin K is unique among mammalian proteinases
    • Garnero P., Borel O., Byrjalsen I., Ferreras M., Drake F.H., McQueney M.S., et al. The collagenolytic activity of cathepsin K is unique among mammalian proteinases. J Biol Chem 273 (1998) 32347-32352
    • (1998) J Biol Chem , vol.273 , pp. 32347-32352
    • Garnero, P.1    Borel, O.2    Byrjalsen, I.3    Ferreras, M.4    Drake, F.H.5    McQueney, M.S.6
  • 23
    • 0032080113 scopus 로고    scopus 로고
    • Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple complex
    • Kafienah W.D., Bromme D.J., Buttle L.J., Croucher C., and Holander A.P. Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple complex. Biochem J 331 (1998) 727-732
    • (1998) Biochem J , vol.331 , pp. 727-732
    • Kafienah, W.D.1    Bromme, D.J.2    Buttle, L.J.3    Croucher, C.4    Holander, A.P.5
  • 24
    • 0035127395 scopus 로고    scopus 로고
    • Biosynthesis and processing of cathepsin k in cultured human osteoblasts
    • Rieman D.J., Mcclung H.A., Dodds R.A., Hwang S.M., Lark M.W., Holmes S., et al. Biosynthesis and processing of cathepsin k in cultured human osteoblasts. Bone 28 (2001) 282-289
    • (2001) Bone , vol.28 , pp. 282-289
    • Rieman, D.J.1    Mcclung, H.A.2    Dodds, R.A.3    Hwang, S.M.4    Lark, M.W.5    Holmes, S.6
  • 25
    • 0027981066 scopus 로고
    • Prostanoid-induced expression of matrix metalloproteinase-1 messenger ribonucleic acid in rat osteosarcoma cells
    • Clohisy J.C., Connolly T.J., Bergman K.D., Quinn C.O., and Patridge N.C. Prostanoid-induced expression of matrix metalloproteinase-1 messenger ribonucleic acid in rat osteosarcoma cells. Endocrinology 135 (1994) 1447-1453
    • (1994) Endocrinology , vol.135 , pp. 1447-1453
    • Clohisy, J.C.1    Connolly, T.J.2    Bergman, K.D.3    Quinn, C.O.4    Patridge, N.C.5
  • 27
    • 0141749336 scopus 로고    scopus 로고
    • Inhibition of Drynariae Rhizoma extracts on bone resorption mediated by processing of cathepsin K in cultured mouse osteoclasts
    • Jeong J.C., Kang S.K., Youn C.H., Jeong C.W., Kim H.M., Lee Y.C., et al. Inhibition of Drynariae Rhizoma extracts on bone resorption mediated by processing of cathepsin K in cultured mouse osteoclasts. Int Immunopharmacol 3 (2003) 1563-1697
    • (2003) Int Immunopharmacol , vol.3 , pp. 1563-1697
    • Jeong, J.C.1    Kang, S.K.2    Youn, C.H.3    Jeong, C.W.4    Kim, H.M.5    Lee, Y.C.6
  • 28
    • 0029875308 scopus 로고    scopus 로고
    • Analysis of 5′-flanking and promoter region of Human N-acetylglucosaminyltransferase gene
    • Kim Y.J., Kim K.S., Chang J.E., Lee Y.C., Ko J.H., Chung T.W., et al. Analysis of 5′-flanking and promoter region of Human N-acetylglucosaminyltransferase gene. Gene 170 (1996) 281-283
    • (1996) Gene , vol.170 , pp. 281-283
    • Kim, Y.J.1    Kim, K.S.2    Chang, J.E.3    Lee, Y.C.4    Ko, J.H.5    Chung, T.W.6
  • 29
    • 0025176592 scopus 로고
    • The effects of recombinant human interleukin-1β on cellular proliferation and the production of prostaglandin E2, plasminogen activator, osteocalcin and alkaline phosphatase by osteoblast-like cells derived from human bone
    • Evans D.B., Bunning R.A.D., and Russell R.G.G. The effects of recombinant human interleukin-1β on cellular proliferation and the production of prostaglandin E2, plasminogen activator, osteocalcin and alkaline phosphatase by osteoblast-like cells derived from human bone. Biochem Biophys Res Commun 166 (1990) 208-216
    • (1990) Biochem Biophys Res Commun , vol.166 , pp. 208-216
    • Evans, D.B.1    Bunning, R.A.D.2    Russell, R.G.G.3
  • 30
    • 0036172328 scopus 로고    scopus 로고
    • Inhibotory effect of a Korean traditional medicine, Honghwain-Jahage (water extracts of Carthamus tinctorius L. seed and Homminis placenta) on interleukin-1-mediated bone resorption
    • Hong H.T., Kim H.J., Kim D.W., Lee Y.C., Par Y.G., Kim H.M., et al. Inhibotory effect of a Korean traditional medicine, Honghwain-Jahage (water extracts of Carthamus tinctorius L. seed and Homminis placenta) on interleukin-1-mediated bone resorption. J Ethnopharm 79 (2002) 143-148
    • (2002) J Ethnopharm , vol.79 , pp. 143-148
    • Hong, H.T.1    Kim, H.J.2    Kim, D.W.3    Lee, Y.C.4    Par, Y.G.5    Kim, H.M.6
  • 32
    • 0032831651 scopus 로고    scopus 로고
    • Development and characterization of a human in vitro resorption assay: demonstration of utility using novel antiresorptive agents
    • James I.E., Lark M.W., Zembryki D., Lee-Rykaczewski W., Hwang S.M., Tomaszek T.A., et al. Development and characterization of a human in vitro resorption assay: demonstration of utility using novel antiresorptive agents. J Bone Miner Res 14 (1999) 1562-1569
    • (1999) J Bone Miner Res , vol.14 , pp. 1562-1569
    • James, I.E.1    Lark, M.W.2    Zembryki, D.3    Lee-Rykaczewski, W.4    Hwang, S.M.5    Tomaszek, T.A.6
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1950) 680-685
    • (1950) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0028962845 scopus 로고
    • Wortmannin, a specific inhibitor of phosphatidylinositol-3 kinase, blocks osteoclastic bone resorption
    • Nakamura I., Takahashi N., Sasaki T., Tanaka S., Udagawa N., Murakami H., et al. Wortmannin, a specific inhibitor of phosphatidylinositol-3 kinase, blocks osteoclastic bone resorption. Fed Eur Bone Soc Lett 361 (1995) 79-84
    • (1995) Fed Eur Bone Soc Lett , vol.361 , pp. 79-84
    • Nakamura, I.1    Takahashi, N.2    Sasaki, T.3    Tanaka, S.4    Udagawa, N.5    Murakami, H.6
  • 37
    • 33646107280 scopus 로고    scopus 로고
    • Phosphoinositol 3-kinase is not required for recycling of mannose-6-phosphate receptors from late endosomes to the trans-Golgi network
    • Nakajima Y., and Pfeffer S.R. Phosphoinositol 3-kinase is not required for recycling of mannose-6-phosphate receptors from late endosomes to the trans-Golgi network. Mol Cell Biol 8 (1997) 677-682
    • (1997) Mol Cell Biol , vol.8 , pp. 677-682
    • Nakajima, Y.1    Pfeffer, S.R.2
  • 38
    • 0031574267 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase association with the osteoclast cytoskeleton, and its involvement in osteoclast attachment and spreading
    • Lakkakorpi P.T., Wesolowski G., Zimolo Z., Rodan G.A., and Rodan S.B. Phosphatidylinositol 3-kinase association with the osteoclast cytoskeleton, and its involvement in osteoclast attachment and spreading. Exp Cell Res 237 (1997) 296-306
    • (1997) Exp Cell Res , vol.237 , pp. 296-306
    • Lakkakorpi, P.T.1    Wesolowski, G.2    Zimolo, Z.3    Rodan, G.A.4    Rodan, S.B.5
  • 39
    • 0029090980 scopus 로고
    • Regulation of insulin-like growth factor I transcription by cyclic adenosine 3′,5′-monophosphate (cAMP) in fetal rat bone cells through an element within exon 1: protein kinase A-dependent control without a consensus AMP response element
    • McCarthy T.L., Thomas M.J., Centrella M., and Rotwein P. Regulation of insulin-like growth factor I transcription by cyclic adenosine 3′,5′-monophosphate (cAMP) in fetal rat bone cells through an element within exon 1: protein kinase A-dependent control without a consensus AMP response element. Endocrinology 136 (1995) 3901-3908
    • (1995) Endocrinology , vol.136 , pp. 3901-3908
    • McCarthy, T.L.1    Thomas, M.J.2    Centrella, M.3    Rotwein, P.4
  • 40
    • 0031807380 scopus 로고    scopus 로고
    • Regulation of interleukin-6 production by prostaglandin E2 in fetal rat osteoblasts: role of protein kinase A signaling pathway
    • Millet I., McCarthy T.L., and Vignery A. Regulation of interleukin-6 production by prostaglandin E2 in fetal rat osteoblasts: role of protein kinase A signaling pathway. J Bone Miner Res 13 (1998) 1092-1100
    • (1998) J Bone Miner Res , vol.13 , pp. 1092-1100
    • Millet, I.1    McCarthy, T.L.2    Vignery, A.3
  • 41


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.