메뉴 건너뛰기




Volumn 77, Issue 4, 2000, Pages 678-693

MMP-13 is induced during chondrocyte hypertrophy

Author keywords

Collagenase 3; Growth plate; Metalloproteinases; Mineralization; MMP; MMP 2

Indexed keywords

BONE MORPHOGENETIC PROTEIN 2; COLLAGENASE 3;

EID: 0034083320     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4644(20000615)77:4<678::AID-JCB15>3.0.CO;2-P     Document Type: Article
Times cited : (135)

References (62)
  • 1
    • 0028274971 scopus 로고
    • Cloning of a 72kDa matrix metalloproteinase (gelatinase) from chicken embryo fibroblasts using gene family PCR: Expression of the gelatinase increases upon malignant transformation
    • Aimes RT, French DL, Quigley JP. 1994. Cloning of a 72kDa matrix metalloproteinase (gelatinase) from chicken embryo fibroblasts using gene family PCR: expression of the gelatinase increases upon malignant transformation. Biochem J 300:729-736.
    • (1994) Biochem J , vol.300 , pp. 729-736
    • Aimes, R.T.1    French, D.L.2    Quigley, J.P.3
  • 2
    • 0026605798 scopus 로고
    • The extracellular matrix of cartilage in the growth plate before and during calcification: Changes in composition and degradation of type II collagen
    • Alini M, Matsui Y, Dodge GR, Poole AR. 1992. The extracellular matrix of cartilage in the growth plate before and during calcification: changes in composition and degradation of type II collagen. Calcif Tissue Int 50:327-335.
    • (1992) Calcif Tissue Int , vol.50 , pp. 327-335
    • Alini, M.1    Matsui, Y.2    Dodge, G.R.3    Poole, A.R.4
  • 3
    • 0028222514 scopus 로고
    • Cellular and matrix changes before and at the time of calcification in the growth plate studied in vitro: Arrest of type X collagen synthesis and net loss of collagen when calcification is initiated
    • Alini M, Carey DE, Hirata S, Grynpas MD, Pidoux I, Poole AR. 1994. Cellular and matrix changes before and at the time of calcification in the growth plate studied in vitro: arrest of type X collagen synthesis and net loss of collagen when calcification is initiated. Bone Miner Res 9:1077-1087.
    • (1994) Bone Miner Res , vol.9 , pp. 1077-1087
    • Alini, M.1    Carey, D.E.2    Hirata, S.3    Grynpas, M.D.4    Pidoux, I.5    Poole, A.R.6
  • 4
    • 0033525533 scopus 로고    scopus 로고
    • Generation and characterization of aggrecanase - A soluble, cartilage-derived aggrecan-degrading activity
    • Arner EC, Pratta MA, Trzaskos JM, Decicco CP, Tortorella MD. 1999. Generation and characterization of aggrecanase - a soluble, cartilage-derived aggrecan-degrading activity. Biol Chem 274:6594-6601.
    • (1999) Biol Chem , vol.274 , pp. 6594-6601
    • Arner, E.C.1    Pratta, Ma.2    Trzaskos, J.M.3    Decicco, C.P.4    Tortorella, M.D.5
  • 5
    • 0027209267 scopus 로고
    • TGF-β1 prevents hypertrophy of epiphyseal chondrocytes: Regulation of gene expression for cartilage matrix proteins and metalloproteases
    • Ballock RT, Heydemann A, Wakefield LM, Flanders KC, Roberts AB, Sporn MB. 1993. TGF-β1 prevents hypertrophy of epiphyseal chondrocytes: regulation of gene expression for cartilage matrix proteins and metalloproteases. Dev Biol 158:414-429.
    • (1993) Dev Biol , vol.158 , pp. 414-429
    • Ballock, R.T.1    Heydemann, A.2    Wakefield, L.M.3    Flanders, K.C.4    Roberts, A.B.5    Sporn, M.B.6
  • 9
    • 0029833035 scopus 로고    scopus 로고
    • Cytokine control of interstitial collagenase and collagenase-3 gene expression in human chondrocytes
    • Borden P, Solymar D, Sucharczuk A, Lindman B, Cannon P, Heller RA. 1996. Cytokine control of interstitial collagenase and collagenase-3 gene expression in human chondrocytes. Biol Chem 271:23577-23581.
    • (1996) Biol Chem , vol.271 , pp. 23577-23581
    • Borden, P.1    Solymar, D.2    Sucharczuk, A.3    Lindman, B.4    Cannon, P.5    Heller, R.A.6
  • 10
    • 0026864089 scopus 로고
    • Treatment of proteoglycan aggregates with physeal enzymes reduces their ability to inhibit hydroxyapatite proliferation in a gelatin gel
    • Boskey AL, Maresca M, Armstrong AL, Ehrlich MG. 1992. Treatment of proteoglycan aggregates with physeal enzymes reduces their ability to inhibit hydroxyapatite proliferation in a gelatin gel. J Orthop Res 10:313-319.
    • (1992) J Orthop Res , vol.10 , pp. 313-319
    • Boskey, A.L.1    Maresca, M.2    Armstrong, A.L.3    Ehrlich, M.G.4
  • 11
    • 0030959454 scopus 로고    scopus 로고
    • Effects of proteoglycan modification on mineral formation in a differentiating chick limb-bud mesenchymal cell culture system
    • Boskey AL, Stiner D, Binderman I, Doty SB. 1997. Effects of proteoglycan modification on mineral formation in a differentiating chick limb-bud mesenchymal cell culture system. Cell Biochem 64:632-643.
    • (1997) Cell Biochem , vol.64 , pp. 632-643
    • Boskey, A.L.1    Stiner, D.2    Binderman, I.3    Doty, S.B.4
  • 12
    • 0026515992 scopus 로고
    • Induction of proliferation or hypertrophy of chondrocytes in serum-free culture: The role of insulin-like growth factor-I, insulin, or thyroxine
    • Böhme K, Conscience-Egli M, Tschan T, Winterhalter KH, Bruckner P. 1992. Induction of proliferation or hypertrophy of chondrocytes in serum-free culture: the role of insulin-like growth factor-I, insulin, or thyroxine. Cell Biol 116:1035-1042.
    • (1992) Cell Biol , vol.116 , pp. 1035-1042
    • Böhme, K.1    Conscience-Egli, M.2    Tschan, T.3    Winterhalter, K.H.4    Bruckner, P.5
  • 15
    • 0026521283 scopus 로고
    • The influence of bone and marrow on cartilage hypertrophy and degradation during 30-day serum-free culture of the embryonic chick tibia
    • Cole AA, Luchene LJ, Linsenmayer TF, Schmid TM. 1992. The influence of bone and marrow on cartilage hypertrophy and degradation during 30-day serum-free culture of the embryonic chick tibia. Dev Dyn 193:277-285.
    • (1992) Dev Dyn , vol.193 , pp. 277-285
    • Cole, A.A.1    Luchene, L.J.2    Linsenmayer, T.F.3    Schmid, T.M.4
  • 16
    • 0027366253 scopus 로고
    • Type X collagen degradation in long-term serum-free culture of the embryonic chick tibia following production of active collagenase and gelatinase
    • Cole AA, Boyd T, Luchene L, Kuettner KE, Schmid TM. 1993. Type X collagen degradation in long-term serum-free culture of the embryonic chick tibia following production of active collagenase and gelatinase. Dev Biol 159:528-534.
    • (1993) Dev Biol , vol.159 , pp. 528-534
    • Cole, A.A.1    Boyd, T.2    Luchene, L.3    Kuettner, K.E.4    Schmid, T.M.5
  • 18
    • 0032522576 scopus 로고    scopus 로고
    • Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: Associated activation of gelatinase a, gelatinase b and collagenase 3
    • Cowell S, Knäuper V, Stewart ML, D'Ortho MP, Stanton H, Hembry RM, López-Otín C, Reynolds JJ, Murphy G. 1998. Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: associated activation of gelatinase A, gelatinase B and collagenase 3. Biochem J 331:453-458.
    • (1998) Biochem J , vol.331 , pp. 453-458
    • Cowell, S.1    Knäuper, V.2    Stewart, M.L.3    D'Ortho, M.P.4    Stanton, H.5    Hembry, R.M.6    López-Otín, C.7    Reynolds, J.J.8    Murphy, G.9
  • 19
    • 0030774452 scopus 로고    scopus 로고
    • Articular chondrocytes produce factors that inhibit maturation of sternal chondrocytes in serum-free agarose cultures: A tgfβ independent process
    • D'Angelo M, Pacifici M. 1997. Articular chondrocytes produce factors that inhibit maturation of sternal chondrocytes in serum-free agarose cultures: a TGFβ independent process. Bone Miner Res 12:1368-1377.
    • (1997) Bone Miner Res , vol.12 , pp. 1368-1377
    • D'Angelo, M.1    Pacifici, M.2
  • 20
    • 0024811818 scopus 로고
    • Association of collagenase and tissue inhibitor of metalloproteinases (TIMP) with hypertrophic cell enlargement in the growth plate
    • Dean DD, Muniz OE, Howell DS. 1989. Association of collagenase and tissue inhibitor of metalloproteinases (TIMP) with hypertrophic cell enlargement in the growth plate. Matrix 9:376-381.
    • (1989) Matrix , vol.9 , pp. 376-381
    • Dean, D.D.1    Muniz, O.E.2    Howell, D.S.3
  • 21
    • 0025116462 scopus 로고
    • Production of collagenase and TIMP by rat growth plates in culture
    • Dean DD, Muniz OE, Woessner JF, Howell DS. 1990. Production of collagenase and TIMP by rat growth plates in culture. Matrix 10:320-330.
    • (1990) Matrix , vol.10 , pp. 320-330
    • Dean, D.D.1    Muniz, O.E.2    Woessner, J.F.3    Howell, D.S.4
  • 23
    • 0029812420 scopus 로고    scopus 로고
    • Vitamin D metabolites regulate matrix vesicle metalloproteinase content in a cell maturation-dependent manner
    • Dean DD, Boyan BD, Muniz OE, Howell DS, Schwartz Z. 1996. Vitamin D metabolites regulate matrix vesicle metalloproteinase content in a cell maturation-dependent manner. Calcif Tissue Int 59:109-116.
    • (1996) Calcif Tissue Int , vol.59 , pp. 109-116
    • Dean, D.D.1    Boyan, B.D.2    Muniz, O.E.3    Howell, D.S.4    Schwartz, Z.5
  • 24
    • 0026513193 scopus 로고
    • Defective bone formation by hyp mouse bone cells transplanted into normal mice: Evidence in favor of an intrinsic osteoblast defect
    • Ecarot B, Glorieux FH, Desbarats M, Travers R, Labelle L. 1992. Defective bone formation by Hyp mouse bone cells transplanted into normal mice: evidence in favor of an intrinsic osteoblast defect. Bone Miner Res7:215-220.
    • (1992) Bone Miner Res , vol.7 , pp. 215-220
    • Ecarot, B.1    Glorieux, F.H.2    Desbarats, M.3    Travers, R.4    Labelle, L.5
  • 27
    • 0029852094 scopus 로고    scopus 로고
    • Aggrecan is degraded by matrix metalloproteinases in human arthritis - Evidence that matrix metalloproteinase and aggrecanase activities can be independent
    • Fosang AJ, Last K, Maciewicz RA. 1996. Aggrecan is degraded by matrix metalloproteinases in human arthritis - evidence that matrix metalloproteinase and aggrecanase activities can be independent. Clin Invest 98:2292-2299.
    • (1996) Clin Invest , vol.98 , pp. 2292-2299
    • Fosang, A.J.1    Last, K.2    Maciewicz, R.A.3
  • 29
    • 0039229235 scopus 로고    scopus 로고
    • Detecting peptidases and proteases
    • Spence MTZ Eugene, OR: Molecular Probes
    • Haugland RP. 1996. Detecting peptidases and proteases. In: Spence MTZ. Handbook of fluorescent probes research chemicals, volume 6. Eugene, OR: Molecular Probes, p 230-232.
    • (1996) Handbook of Fluorescent Probes Research Chemicals , vol.6 , pp. 230-232
    • Haugland, R.P.1
  • 30
    • 0032515157 scopus 로고    scopus 로고
    • Differential expression of aggrecanase and matrix metalloproteinase activity in chondrocytes isolated from bovine and porcine articular cartilage
    • Hughes CE, Little CB, Büttner FH, Bartnik E, Caterson B. 1998. Differential expression of aggrecanase and matrix metalloproteinase activity in chondrocytes isolated from bovine and porcine articular cartilage. Biol Chem 273: 30576-30582.
    • (1998) Biol Chem , vol.273 , pp. 30576-30582
    • Hughes, C.E.1    Little, C.B.2    Büttner, F.H.3    Bartnik, E.4    Caterson, B.5
  • 31
    • 0026088709 scopus 로고
    • Role of proteoglycan in the provisional calcification of cartilage
    • Hunter GK. 1991. Role of proteoglycan in the provisional calcification of cartilage. Clin Orthop 262:256-280.
    • (1991) Clin Orthop , vol.262 , pp. 256-280
    • Hunter, G.K.1
  • 35
    • 0030037395 scopus 로고    scopus 로고
    • Cellular mechanisms for human procollagenase-g (MMP-13) activation - Evidence that MT1-MMP (MMP-14) and gelatinase A (MMP-2) are able to generate active enzyme
    • Knäuper V, Will H, López-Otin C, Smith B, Atkinson SJ, Stanton H, Hembry RM, Murphy G. 1996b. Cellular mechanisms for human procollagenase-G (MMP-13) activation - evidence that MT1-MMP (MMP-14) and gelatinase A (MMP-2) are able to generate active enzyme. Biol Chem 271:17124-17131.
    • (1996) Biol Chem , vol.271 , pp. 17124-17131
    • Knäuper, V.1    Will, H.2    López-Otin, C.3    Smith, B.4    Atkinson, S.J.5    Stanton, H.6    Hembry, R.M.7    Murphy, G.8
  • 36
    • 0030898796 scopus 로고    scopus 로고
    • The role of the c-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction
    • Knäuper V, Cowell S, Smith B, López-Otin C, O'Shea M, Morris H, Zardi L, Murphy G. 1997. The role of the c-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction. Biol Chem 272:7608-7616.
    • (1997) Biol Chem , vol.272 , pp. 7608-7616
    • Knäuper, V.1    Cowell, S.2    Smith, B.3    López-Otin, C.4    O'Shea, M.5    Morris, H.6    Zardi, L.7    Murphy, G.8
  • 38
    • 0024325259 scopus 로고
    • Ascorbic acid induces alkaline phosphatase, type X collagen and calcium deposition in cultured chick chondrocytes
    • Leboy PS, Vaias L, Uschmann B, Golub EE, Adams SL, Pacifici M. 1989. Ascorbic acid induces alkaline phosphatase, type X collagen and calcium deposition in cultured chick chondrocytes. Biol Chem 264:17281-17286.
    • (1989) Biol Chem , vol.264 , pp. 17281-17286
    • Leboy, P.S.1    Vaias, L.2    Uschmann, B.3    Golub, E.E.4    Adams, S.L.5    Pacifici, M.6
  • 39
    • 0030824826 scopus 로고    scopus 로고
    • Rapid chondrocyte maturation by serum-free culture with BMP-2 and ascorbic acid
    • Leboy PS, Sullivan TA, Nooreyazdan M, Venezian RA. 1997. Rapid chondrocyte maturation by serum-free culture with BMP-2 and ascorbic acid. Cell Biochem 66: 394-403.
    • (1997) Cell Biochem , vol.66 , pp. 394-403
    • Leboy, P.S.1    Sullivan, T.A.2    Nooreyazdan, M.3    Venezian, R.A.4
  • 41
    • 0031550263 scopus 로고    scopus 로고
    • The recombinant catalytic domain of mouse collagenase-3 depolymerizes type I collagen by cleaving its aminotelopeptides
    • Lemaitre V, Jungbluth A, Eeckhout Y. 1997. The recombinant catalytic domain of mouse collagenase-3 depolymerizes type I collagen by cleaving its aminotelopeptides. Biochem Biophys Res Commun 230:202-205.
    • (1997) Biochem Biophys Res Commun , vol.230 , pp. 202-205
    • Lemaitre, V.1    Jungbluth, A.2    Eeckhout, Y.3
  • 42
    • 0028650295 scopus 로고
    • Matrix metalloproteinase gene expression
    • Matrisian LM. 1994. Matrix metalloproteinase gene expression. Ann NY Acad Sci 732:42-50.
    • (1994) Ann NY Acad Sci , vol.732 , pp. 42-50
    • Matrisian, L.M.1
  • 44
    • 0023114192 scopus 로고
    • Elaboration of neutral proteoglycanases by growth plate tissue cultures
    • Mercier P, Ehrlich MG, Armstrong AL, Mankin HJ. 1987. Elaboration of neutral proteoglycanases by growth plate tissue cultures. Bone Joint Surg 69:76-82.
    • (1987) Bone Joint Surg , vol.69 , pp. 76-82
    • Mercier, P.1    Ehrlich, M.G.2    Armstrong, A.L.3    Mankin, H.J.4
  • 46
    • 0030868574 scopus 로고    scopus 로고
    • Collagenase-3 (MMP-13) is preferentially synthesized in situ in the deeper layer or human arthritic cartilage. In vitro mimicking effect by TGFβ
    • Moldovan F, Pelletier J-P, Hambor JE, Cloutier J-M, Martel-Pelletier J. 1997. Collagenase-3 (MMP-13) is preferentially synthesized in situ in the deeper layer or human arthritic cartilage. In vitro mimicking effect by TGFβ. Arthritis Rheum 40:1653-1661.
    • (1997) Arthritis Rheum , vol.40 , pp. 1653-1661
    • Moldovan, F.1    Pelletier, J.-P.2    Hambor, J.E.3    Cloutier, J.-M.4    Martel-Pelletier, J.5
  • 47
    • 0004045813 scopus 로고    scopus 로고
    • Retinoic acid treatment elevates matrix metalloproteinase-2 protein and mRNA levels in avian growth plate chondrocyte cultures
    • Nie D, Ishikawa Y, Yoshimori T, Wuthier RE, Wu LN. 1998. Retinoic acid treatment elevates matrix metalloproteinase-2 protein and mRNA levels in avian growth plate chondrocyte cultures. Cell Biochem 68: 90-99.
    • (1998) Cell Biochem , vol.68 , pp. 90-99
    • Nie, D.1    Ishikawa, Y.2    Yoshimori, T.3    Wuthier, R.E.4    Wu, L.N.5
  • 48
    • 0026446897 scopus 로고
    • Thyroid hormone, insulin, and glucocorticoids are sufficient to support chondrocyte differentiation to hypertrophy: A serum-free analysis
    • Quarto R, Campanile G, Cancedda R, Dozin B. 1992. Thyroid hormone, insulin, and glucocorticoids are sufficient to support chondrocyte differentiation to hypertrophy: a serum-free analysis. Cell Biol 119:989-995.
    • (1992) Cell Biol , vol.119 , pp. 989-995
    • Quarto, R.1    Campanile, G.2    Cancedda, R.3    Dozin, B.4
  • 49
    • 0029880393 scopus 로고    scopus 로고
    • The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes - A role in osteoarthritis
    • Reboul P, Pelletier JP, Tardif G, Cloutier J-M, Martel-Pelletier J. 1996. The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes - a role in osteoarthritis. Clin Invest 97:2011-2019.
    • (1996) Clin Invest , vol.97 , pp. 2011-2019
    • Reboul, P.1    Pelletier, J.P.2    Tardif, G.3    Cloutier, J.-M.4    Martel-Pelletier, J.5
  • 50
    • 0033228697 scopus 로고    scopus 로고
    • In situ localization and characterization of active proteases in chronically inflamed and healthy human gingival tissues
    • Sarment DP, Korostoff J, D'Angelo M, Polson AM, Feldman RS, Billings PC. 1999. In situ localization and characterization of active proteases in chronically inflamed and healthy human gingival tissues. Periodontology 70: 1303-1312.
    • (1999) Periodontology , vol.70 , pp. 1303-1312
    • Sarment, D.P.1    Korostoff, J.2    D'Angelo, M.3    Polson, A.M.4    Feldman, R.S.5    Billings, P.C.6
  • 52
    • 0029891977 scopus 로고    scopus 로고
    • Chondrocyte cultures express matrix metalloproteinase mrna and immunoreactive protein; stromelysin-1 and 72 kda gelatinase are localized in extracellular matrix vesicles
    • Schmitz JP, Dean DD, Schwartz Z, Cochran DL, Grant GM, Klebe RJ, Nakaya H, Boyan BD. 1996. Chondrocyte cultures express matrix metalloproteinase mRNA and immunoreactive protein; stromelysin-1 and 72 kDa gelatinase are localized in extracellular matrix vesicles. Cell Biochem 61:375-391.
    • (1996) Cell Biochem , vol.61 , pp. 375-391
    • Schmitz, J.P.1    Dean, D.D.2    Schwartz, Z.3    Cochran, D.L.4    Grant, G.M.5    Klebe, R.J.6    Nakaya, H.7    Boyan, B.D.8
  • 54
    • 0039167208 scopus 로고    scopus 로고
    • Collagenase-3 (MMP-13) is expressed during human fetal ossification and re-expressed in postnatal bone remodeling and in rheumatoid arthritis
    • Ståhle-Bäckdahl M, Sandstedt B, Bruce K, Lindahl A, Jimenez MG, Vega JA, López-Otín C. 1997. Collagenase-3 (MMP-13) is expressed during human fetal ossification and re-expressed in postnatal bone remodeling and in rheumatoid arthritis. Lab Invest 76:717-728.
    • (1997) Lab Invest , vol.76 , pp. 717-728
    • Ståhle-Bäckdahl, M.1    Sandstedt, B.2    Bruce, K.3    Lindahl, A.4    Jimenez, M.G.5    Vega, J.A.6    López-Otín, C.7
  • 55
    • 0023158228 scopus 로고
    • Chondroitin sulfate inhibits calcification of bone formed in vitro
    • Tenenbaum HC, Hunter GK. 1993. Chondroitin sulfate inhibits calcification of bone formed in vitro. Bone Mineral 2, 43-51.
    • (1993) Bone Mineral , vol.2 , pp. 43-51
    • Tenenbaum, H.C.1    Hunter, G.K.2
  • 56
    • 0031938965 scopus 로고    scopus 로고
    • Modulation of chondrocyte proliferation by ascorbic acid and BMP-2
    • Venezian RA, Shenker BJ, Datar S, Leboy PS. 1998. Modulation of chondrocyte proliferation by ascorbic acid and BMP-2. J Cell Physiol 194:331-341.
    • (1998) J Cell Physiol , vol.194 , pp. 331-341
    • Venezian, R.A.1    Shenker, B.J.2    Datar, S.3    Leboy, P.S.4
  • 58
    • 0030011680 scopus 로고    scopus 로고
    • Collagen expression in chicken tibial dyschondroplasia
    • Wardale RJ, Duance VC. 1996. Collagen expression in chicken tibial dyschondroplasia. Cell Sci 109:1119-1131.
    • (1996) Cell Sci , vol.109 , pp. 1119-1131
    • Wardale, R.J.1    Duance, V.C.2
  • 59
    • 0027442510 scopus 로고
    • Matrix metalloproteinase-3 (stromelysin-1). Identification as the cartilage acid metalloprotease and effect of ph on catalytic properties and calcium affinity
    • Wilhelm SM, Shao Z-H, Housley TJ, Seperack PK, Baumann AP, Gunja-Smith Z, Woessner JF. 1993. Matrix metalloproteinase-3 (stromelysin-1). Identification as the cartilage acid metalloprotease and effect of pH on catalytic properties and calcium affinity. Biol Chem 268: 21906-21913.
    • (1993) Biol Chem , vol.268 , pp. 21906-21913
    • Wilhelm, S.M.1    Shao, Z.-H.2    Housley, T.J.3    Seperack, P.K.4    Baumann, A.P.5    Gunja-Smith, Z.6    Woessner, J.F.7
  • 60
    • 0001796893 scopus 로고    scopus 로고
    • The matrix metalloproteinase family
    • Parks WC, Meecham RP. San Diego: Academic Press
    • Woessner JF. 1998. The matrix metalloproteinase family. In: Parks WC, Meecham RP. Matrix metalloproteinases. San Diego: Academic Press. p 1-14.
    • (1998) Matrix Metalloproteinases , pp. 1-14
    • Woessner, J.F.1
  • 61
    • 0343447576 scopus 로고    scopus 로고
    • MMP-13 but not MMP-1 is synthesized in fetal bovine growth plate chondrocytes
    • Wu CW, Hasty KA, Poole AR. 1997. MMP-13 but not MMP-1 is synthesized in fetal bovine growth plate chondrocytes. Trans Orthop Res Soc 22:618.
    • (1997) Trans Orthop Res Soc , vol.22 , pp. 618
    • Wu, C.W.1    Hasty, K.A.2    Poole, A.R.3
  • 62
    • 0029160171 scopus 로고
    • M-calpain in rat growth plate chondrocyte cultures: Its involvement in the matrix mineralization process
    • Yasuda T, Shimizu K, Nakagawa Y, Yamamoto S, Niibayashi H, Yamamuro T. 1995. m-Calpain in rat growth plate chondrocyte cultures: its involvement in the matrix mineralization process. Dev Biol 170:159-168.
    • (1995) Dev Biol , vol.170 , pp. 159-168
    • Yasuda, T.1    Shimizu, K.2    Nakagawa, Y.3    Yamamoto, S.4    Niibayashi, H.5    Yamamuro, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.