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Volumn 15, Issue 1, 2000, Pages 82-94

Different bone growth rates are associated with changes in the expression pattern of types II and X collagens and collagenase 3 in proximal growth plates of the rat tibia

Author keywords

Bone growth; Collagen; Collagenase; Growth plate; Postnatal development

Indexed keywords

COLLAGEN; COLLAGENASE 3;

EID: 0033962948     PISSN: 08840431     EISSN: None     Source Type: Journal    
DOI: 10.1359/jbmr.2000.15.1.82     Document Type: Article
Times cited : (66)

References (67)
  • 1
    • 0028067659 scopus 로고
    • Mechanism of longitudinal bone growth and its regulation by growth plate chondrocytes
    • Hunziker EB 1994 Mechanism of longitudinal bone growth and its regulation by growth plate chondrocytes. Microsc Res Techniq 28:505-519.
    • (1994) Microsc Res Techniq , vol.28 , pp. 505-519
    • Hunziker, E.B.1
  • 3
    • 0028199814 scopus 로고
    • Expression of collagens I, II, III, X and XII and aggrecans mRNAs by bovine growth plate chondrocytes in situ
    • Sandell LJ, Sugai JV, Trippel SB 1994 Expression of collagens I, II, III, X and XII and aggrecans mRNAs by bovine growth plate chondrocytes in situ. J Orthopaed Res 12:1-14.
    • (1994) J Orthopaed Res , vol.12 , pp. 1-14
    • Sandell, L.J.1    Sugai, J.V.2    Trippel, S.B.3
  • 4
    • 0001931432 scopus 로고
    • Type IX or 1, 2, 3 collagen
    • Mayne R and Burgerson RE, (eds) Orlando, FL: Academic
    • Eyre DR, Wu JJ 1987 Type IX or 1, 2, 3 collagen. In: Mayne R and Burgerson RE, (eds) Struture and function of collagen types. Orlando, FL: Academic, pp.261-281.
    • (1987) Struture and Function of Collagen Types , pp. 261-281
    • Eyre, D.R.1    Wu, J.J.2
  • 5
    • 0001786414 scopus 로고
    • The growth plate: Cellular physiology, cartilage assembly, and mineralization
    • Hall B and Newman S (eds) Boca Raton, FL: CRC
    • Poole AR 1991 The growth plate: cellular physiology, cartilage assembly, and mineralization. In: Hall B and Newman S (eds) Cartilage: molecular aspects. Boca Raton, FL: CRC, pp. 179-211.
    • (1991) Cartilage: Molecular Aspects , pp. 179-211
    • Poole, A.R.1
  • 6
    • 0030959592 scopus 로고    scopus 로고
    • Collagen types VIII and X, two non-fibrillar, short-chain collagens. Structure homologies, functions and involvement in pathology
    • Sutmuller M, Bruijn JA, de Heer E 1997 Collagen types VIII and X, two non-fibrillar, short-chain collagens. Structure homologies, functions and involvement in pathology. Histol Histopathol 12:557-566.
    • (1997) Histol Histopathol , vol.12 , pp. 557-566
    • Sutmuller, M.1    Bruijn, J.A.2    De Heer, E.3
  • 7
    • 0029150795 scopus 로고
    • Proteolytic remodeling of extracellular matrix
    • Birkedal-Hansen H 1995 Proteolytic remodeling of extracellular matrix. Curr Opin Cell Biol 7:728-735.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 728-735
    • Birkedal-Hansen, H.1
  • 8
    • 0028322352 scopus 로고
    • Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas
    • Freije JP, Díez-Itza I, Balbín M, Sánchez LM, Blasco R, Tolivia J, López-Otín C 1994 Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas. J Biol Chem 269:16766-16773.
    • (1994) J Biol Chem , vol.269 , pp. 16766-16773
    • Freije, J.P.1    Díez-Itza, I.2    Balbín, M.3    Sánchez, L.M.4    Blasco, R.5    Tolivia, J.6    López-Otín, C.7
  • 12
    • 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-Otín 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. J Biol Chem 272:7608-7616.
    • (1997) J Biol Chem , vol.272 , pp. 7608-7616
    • Knäuper, V.1    Cowell, S.2    Smith, B.3    López-Otín, C.4    O'Shea, M.5    Morris, H.6    Zardi, L.7    Murphy, G.8
  • 13
    • 0029063214 scopus 로고
    • Expression of interstitial collagenase during skeletal development of the mouse is restricted to osteoblast-like cells and hypertrophic chondrocytes
    • Gack S, Vallon R, Schmidt J, Grigoriadis A, Tuckermann J, Schenkel J, Weiher H, Wagner EF, Angel P 1995 Expression of interstitial collagenase during skeletal development of the mouse is restricted to osteoblast-like cells and hypertrophic chondrocytes. Cell Growth Differ 6:759-767.
    • (1995) Cell Growth Differ , vol.6 , pp. 759-767
    • Gack, S.1    Vallon, R.2    Schmidt, J.3    Grigoriadis, A.4    Tuckermann, J.5    Schenkel, J.6    Weiher, H.7    Wagner, E.F.8    Angel, P.9
  • 17
    • 0039167208 scopus 로고    scopus 로고
    • Collagenase-3 (MMP-13) is expessed during human fetal ossification and re-expressed in postnatal bone remodeling and rheumatoid arthritis
    • Ståhle-Bhckdahl M, Sandstedt B, Bruce K, Lindahl A, Jiménez MJ, Vega JA, López-Otín C 1997 Collagenase-3 (MMP-13) is expessed during human fetal ossification and re-expressed in postnatal bone remodeling and rheumatoid arthritis. Lab Invest 76:717-728.
    • (1997) Lab Invest , vol.76 , pp. 717-728
    • Ståhle-Bhckdahl, M.1    Sandstedt, B.2    Bruce, K.3    Lindahl, A.4    Jiménez, M.J.5    Vega, J.A.6    López-Otín, C.7
  • 19
    • 0024397516 scopus 로고
    • Immunolocalization of metalloproteinases and their inhibitor in the rabbit growth plate
    • Brown CC, Hembry RM, Reynolds JJ 1989 Immunolocalization of metalloproteinases and their inhibitor in the rabbit growth plate. J Bone Joint Surg 71:580-593.
    • (1989) J Bone Joint Surg , vol.71 , pp. 580-593
    • Brown, C.C.1    Hembry, R.M.2    Reynolds, J.J.3
  • 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 9:366-375.
    • (1989) Matrix , vol.9 , pp. 366-375
    • Dean, D.D.1    Muniz, O.E.2    Howell, D.S.3
  • 21
    • 0027457447 scopus 로고
    • Determination of proliferative characteristisc of growth plate chondrocytes by labeling with bromodeoxiuridine
    • Farnum CE, Wilsman NJ 1993 Determination of proliferative characteristisc of growth plate chondrocytes by labeling with bromodeoxiuridine. Calcified Tissue Int 52:110-119.
    • (1993) Calcified Tissue Int , vol.52 , pp. 110-119
    • Farnum, C.E.1    Wilsman, N.J.2
  • 22
    • 0024399588 scopus 로고
    • Physiological mechanisms adopted by chondrocytes in regulating longitudinal bone growth in rats
    • Hunziker EB, Schenk RK 1989 Physiological mechanisms adopted by chondrocytes in regulating longitudinal bone growth in rats. J Physiol 414:55-71.
    • (1989) J Physiol , vol.414 , pp. 55-71
    • Hunziker, E.B.1    Schenk, R.K.2
  • 23
    • 0028331261 scopus 로고
    • Differencial effects of IGF-I and hGH on the various developmental stages of growth plate chondrocytes in vitro
    • Hunziker EB, Wagner J, Zapf J 1994 Differencial effects of IGF-I and hGH on the various developmental stages of growth plate chondrocytes in vitro. J Clin Invest 93:1078-1086.
    • (1994) J Clin Invest , vol.93 , pp. 1078-1086
    • Hunziker, E.B.1    Wagner, J.2    Zapf, J.3
  • 24
    • 0026153593 scopus 로고
    • Linear relationship between the volumen of hypertrophic chondrocytes and the rate of longitudinal bone growth in growth plates
    • Breur GJ, VanEnkevort BA, Farnum CE, Wilsman NJ 1991 Linear relationship between the volumen of hypertrophic chondrocytes and the rate of longitudinal bone growth in growth plates. J Orthopaed Res 9:348-359.
    • (1991) J Orthopaed Res , vol.9 , pp. 348-359
    • Breur, G.J.1    VanEnkevort, B.A.2    Farnum, C.E.3    Wilsman, N.J.4
  • 25
    • 0026718204 scopus 로고
    • Cellular basis of decreased rate of longitudinal growth of bone in pseudoachondroplastic dogs
    • Breur GJ, Farnum CE, Padgett GA, Wilsman NJ 1992 Cellular basis of decreased rate of longitudinal growth of bone in pseudoachondroplastic dogs. J Bone Joint Surg Am 74:516-528.
    • (1992) J Bone Joint Surg Am , vol.74 , pp. 516-528
    • Breur, G.J.1    Farnum, C.E.2    Padgett, G.A.3    Wilsman, N.J.4
  • 28
    • 0028242571 scopus 로고
    • Stereological and serial section analysis of chondrocytic enlargement in the proximal tibial growth plate of the rat
    • Breur GJ, Turgai BA, VanEnkevort CE, Farnum CE, Wilsman NJ 1994 Stereological and serial section analysis of chondrocytic enlargement in the proximal tibial growth plate of the rat. Anat Rec 239:255-268.
    • (1994) Anat Rec , vol.239 , pp. 255-268
    • Breur, G.J.1    Turgai, B.A.2    VanEnkevort, C.E.3    Farnum, C.E.4    Wilsman, N.J.5
  • 29
    • 0032055031 scopus 로고    scopus 로고
    • Kinetic studies on epiphyseal growth cartilage in the normal mouse
    • Vanky P, Brockstedt U, Hjerpe A, Wikström B 1998 Kinetic studies on epiphyseal growth cartilage in the normal mouse. Bone 22:331-339.
    • (1998) Bone , vol.22 , pp. 331-339
    • Vanky, P.1    Brockstedt, U.2    Hjerpe, A.3    Wikström, B.4
  • 30
    • 84985217564 scopus 로고
    • Stereology for anisotropic cells: Application to growth cartilage
    • Cruz-Orive LM, Hunziker EB 1986 Stereology for anisotropic cells: application to growth cartilage. J Micros 113:47-80.
    • (1986) J Micros , vol.113 , pp. 47-80
    • Cruz-Orive, L.M.1    Hunziker, E.B.2
  • 32
    • 0025949448 scopus 로고
    • Mouse type II collagen gene. Complete nucleotide sequence, exon structure and alternative splicing
    • Metsäranta M, Toman D, de Crombrugghe B, Vuorio E 1991 Mouse type II collagen gene. Complete nucleotide sequence, exon structure and alternative splicing. J Biol Chem 266:16862-16869.
    • (1991) J Biol Chem , vol.266 , pp. 16862-16869
    • Metsäranta, M.1    Toman, D.2    De Crombrugghe, B.3    Vuorio, E.4
  • 33
    • 0026544785 scopus 로고
    • Cloning of the human and mouse type-X collagen genes and mapping of the mouse type-X collagen gene to chromosome 10
    • Apte SS, Seidin MF, Hayashi M, Olsen BR 1992 Cloning of the human and mouse type-X collagen genes and mapping of the mouse type-X collagen gene to chromosome 10. Eur J Biochem 206:217-224.
    • (1992) Eur J Biochem , vol.206 , pp. 217-224
    • Apte, S.S.1    Seidin, M.F.2    Hayashi, M.3    Olsen, B.R.4
  • 34
    • 0002908409 scopus 로고    scopus 로고
    • A simplified in situ hybridization protocol using non-radioactively labeled probes to detect abundant and rare mRNAs on tissue sections
    • Braissant O, Wahli W 1998 A simplified in situ hybridization protocol using non-radioactively labeled probes to detect abundant and rare mRNAs on tissue sections. Biochemica (Boehringer Mannheim) 1:10-16.
    • (1998) Biochemica (Boehringer Mannheim) , vol.1 , pp. 10-16
    • Braissant, O.1    Wahli, W.2
  • 35
    • 85003152202 scopus 로고
    • Modulation of osteoclast differentiation
    • Suda T, Takahashi N, Martin TJ 1992 Modulation of osteoclast differentiation. Endocr Rev 13:66-80.
    • (1992) Endocr Rev , vol.13 , pp. 66-80
    • Suda, T.1    Takahashi, N.2    Martin, T.J.3
  • 36
    • 0030483252 scopus 로고    scopus 로고
    • Differential growth by growth plates as a function of multiple parameters of chondrocytic kinetics
    • Wilsman NJ, Farnum CE, Leiferman EM, Fry M, Barreto C 1996 Differential growth by growth plates as a function of multiple parameters of chondrocytic kinetics. J Orthopaed Res 14:927-936.
    • (1996) J Orthopaed Res , vol.14 , pp. 927-936
    • Wilsman, N.J.1    Farnum, C.E.2    Leiferman, E.M.3    Fry, M.4    Barreto, C.5
  • 38
    • 0031926816 scopus 로고    scopus 로고
    • Bone formation via cartilage models: The "borderline" chondrocyte
    • Bianco P, Cancedda FD, Riminucci M, Cancedda R 1998 Bone formation via cartilage models: the "borderline" chondrocyte. Matrix Biol 17:185-192.
    • (1998) Matrix Biol , vol.17 , pp. 185-192
    • Bianco, P.1    Cancedda, F.D.2    Riminucci, M.3    Cancedda, R.4
  • 40
    • 0000666051 scopus 로고
    • Regulation of cartilage collagen and proteoglycan synthesis by transforming growth factor-beta
    • Sandell LJ, Dudek EJ, Bielaga B, Wight TN 1989 Regulation of cartilage collagen and proteoglycan synthesis by transforming growth factor-beta. Trans Orthop Res Soc 14:280.
    • (1989) Trans Orthop Res Soc , vol.14 , pp. 280
    • Sandell, L.J.1    Dudek, E.J.2    Bielaga, B.3    Wight, T.N.4
  • 41
    • 0025614088 scopus 로고
    • Type X collagen gene expression is transiently up-regulated by retinoic acid treatment in chick chondrocyte cultures
    • Oettinger HF, Pacifici M 1990 Type X collagen gene expression is transiently up-regulated by retinoic acid treatment in chick chondrocyte cultures. Exp Cell Res 191:292-298.
    • (1990) Exp Cell Res , vol.191 , pp. 292-298
    • Oettinger, H.F.1    Pacifici, M.2
  • 42
    • 0027197285 scopus 로고
    • Responsiveness to retinoic acid changes during chondrocyte maturation
    • Iwamoto M, Golden EB, Adams SL, Noji S, Pacifici M 1993 Responsiveness to retinoic acid changes during chondrocyte maturation. Exp Cell Res 205:153-161.
    • (1993) Exp Cell Res , vol.205 , pp. 153-161
    • Iwamoto, M.1    Golden, E.B.2    Adams, S.L.3    Noji, S.4    Pacifici, M.5
  • 43
    • 0030958202 scopus 로고    scopus 로고
    • Retinoic acid stimulates matrix calcification and initiates type I collagen synthesis in primary cultures of avian weight-bearing growth plate chondrocytes
    • Wu LNY, Ishikawa Y, Nie D, Genge BR, Wuthier RE 1997 Retinoic acid stimulates matrix calcification and initiates type I collagen synthesis in primary cultures of avian weight-bearing growth plate chondrocytes. J Cell Biochem 65:209-230.
    • (1997) J Cell Biochem , vol.65 , pp. 209-230
    • Wu, L.N.Y.1    Ishikawa, Y.2    Nie, D.3    Genge, B.R.4    Wuthier, R.E.5
  • 47
    • 0025189848 scopus 로고
    • Is longitudinal bone growth influenced by diurnal variation in the mitotic activity of chondrocytes of the growth plate?
    • Stevenson S, Hunziker EB, Herrmann W, Schenk RK 1990 Is longitudinal bone growth influenced by diurnal variation in the mitotic activity of chondrocytes of the growth plate?. J Orthopaed Res 8:132-135.
    • (1990) J Orthopaed Res , vol.8 , pp. 132-135
    • Stevenson, S.1    Hunziker, E.B.2    Herrmann, W.3    Schenk, R.K.4
  • 48
    • 0024988862 scopus 로고
    • Cell proliferation within the growth plate of long bones assessed by bromodeoxyuridine uptake and its relationship to glucose 6-phosphate dehydrogenase activity
    • Farquharson C, Loveridge N 1990 Cell proliferation within the growth plate of long bones assessed by bromodeoxyuridine uptake and its relationship to glucose 6-phosphate dehydrogenase activity. Bone Miner 10:121-130.
    • (1990) Bone Miner , vol.10 , pp. 121-130
    • Farquharson, C.1    Loveridge, N.2
  • 49
    • 0025166680 scopus 로고
    • Differential susceptibility of type X collagen to cleavage by two mammalian interstitial collagenases and 72-kDa type IV collagenase
    • Welgus HC, Fliszar CJ, Seltzer JL, Schnid TM, Jeffrey JJ 1990 Differential susceptibility of type X collagen to cleavage by two mammalian interstitial collagenases and 72-kDa type IV collagenase. J Biol Chem 265:13521-13527.
    • (1990) J Biol Chem , vol.265 , pp. 13521-13527
    • Welgus, H.C.1    Fliszar, C.J.2    Seltzer, J.L.3    Schnid, T.M.4    Jeffrey, J.J.5
  • 50
    • 0028956323 scopus 로고
    • Complete degradation of type X collagen requires the combined action of interstitial collagenase and osteoclasts-derived cathepsin-B
    • Sires UI, Schmid TM, Fliszar CJ, Wang ZQ, Gluck SL, Welgus HG 1995 Complete degradation of type X collagen requires the combined action of interstitial collagenase and osteoclasts-derived cathepsin-B. J Clin Invest 95:2089-2095.
    • (1995) J Clin Invest , vol.95 , pp. 2089-2095
    • Sires, U.I.1    Schmid, T.M.2    Fliszar, C.J.3    Wang, Z.Q.4    Gluck, S.L.5    Welgus, H.G.6
  • 51
    • 0031659890 scopus 로고    scopus 로고
    • Cysteine proteinases and matrix metalloproteinases play distinct roles in the subosteoclastic resorption zone
    • Everts V, Delaissé JM, Korper W, Beertsen W 1998 Cysteine proteinases and matrix metalloproteinases play distinct roles in the subosteoclastic resorption zone. J Bone Miner Res 13:1420-1430.
    • (1998) J Bone Miner Res , vol.13 , pp. 1420-1430
    • Everts, V.1    Delaissé, J.M.2    Korper, W.3    Beertsen, W.4
  • 52
    • 0029876376 scopus 로고    scopus 로고
    • The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases
    • Whitelock JM, Murdoch AD, Iozzo RV, Underwood PA 1996 The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases. J Biol Chem 271:10079-10086.
    • (1996) J Biol Chem , vol.271 , pp. 10079-10086
    • Whitelock, J.M.1    Murdoch, A.D.2    Iozzo, R.V.3    Underwood, P.A.4
  • 53
    • 0028958031 scopus 로고
    • Insulin-like growth factors and their binding proteins: Biological actions
    • Jones JI, Clemmons DR 1995 Insulin-like growth factors and their binding proteins: biological actions. Endocr Rev 16:3-34.
    • (1995) Endocr Rev , vol.16 , pp. 3-34
    • Jones, J.I.1    Clemmons, D.R.2
  • 54
    • 0029121178 scopus 로고
    • Characterization of insulin-like growth factor-binding protein 5-degrading proteases produced throughout murine osteoblast differentiation
    • Thrailkill KM, Quarles LD, Nagase H, Suzuki K, Serra DM, Fowlkes JL 1995 Characterization of insulin-like growth factor-binding protein 5-degrading proteases produced throughout murine osteoblast differentiation. Endocrinology 136:3527-3533.
    • (1995) Endocrinology , vol.136 , pp. 3527-3533
    • Thrailkill, K.M.1    Quarles, L.D.2    Nagase, H.3    Suzuki, K.4    Serra, D.M.5    Fowlkes, J.L.6
  • 55
    • 0029047468 scopus 로고
    • The synthesis of collagenase, gelatinase a (72 kDa) and -B (95 kDa), and TIMP-1 and -2 by human osteoblasts from normal and arthritic bone
    • Meikle MC, Bord S, Hembry RM, Reynolds JJ 1995 The synthesis of collagenase, gelatinase A (72 kDa) and -B (95 kDa), and TIMP-1 and -2 by human osteoblasts from normal and arthritic bone. Bone 17:255-260.
    • (1995) Bone , vol.17 , pp. 255-260
    • Meikle, M.C.1    Bord, S.2    Hembry, R.M.3    Reynolds, J.J.4
  • 56
    • 0031869035 scopus 로고    scopus 로고
    • Stromelysin-1 (MMP-3) and stromelysin-2 (MMP-10) expression in developing human bone: Potential roles in skeletal development
    • Bord S, Horner A, Hembry RM, Compston JE 1998 Stromelysin-1 (MMP-3) and stromelysin-2 (MMP-10) expression in developing human bone: potential roles in skeletal development. Bone 23:7-12.
    • (1998) Bone , vol.23 , pp. 7-12
    • Bord, S.1    Horner, A.2    Hembry, R.M.3    Compston, J.E.4
  • 57
    • 0028223234 scopus 로고
    • High expression of 92-kD type IV collagenase (gelatinase B) in osteoclast lineage during mouse development
    • Reponen P, Sahlberg C, Munaut C, Thesleff I, Tryggvason K 1994 High expression of 92-kD type IV collagenase (gelatinase B) in osteoclast lineage during mouse development. J Cell Biol 124:1091-1102.
    • (1994) J Cell Biol , vol.124 , pp. 1091-1102
    • Reponen, P.1    Sahlberg, C.2    Munaut, C.3    Thesleff, I.4    Tryggvason, K.5
  • 60
    • 0030884231 scopus 로고    scopus 로고
    • Unaltered secretion of beta-amyloid precursor protein in gelatinase a (matrix metalloproteinase 2)-deficient mice
    • Itoh T, Ikeda T, Gomi H, Nakao S, Suzuki T, Itohara S 1997 Unaltered secretion of beta-amyloid precursor protein in gelatinase A (matrix metalloproteinase 2)-deficient mice. J Biol Chem 272:22389-22392.
    • (1997) J Biol Chem , vol.272 , pp. 22389-22392
    • Itoh, T.1    Ikeda, T.2    Gomi, H.3    Nakao, S.4    Suzuki, T.5    Itohara, S.6
  • 61
    • 0029910358 scopus 로고    scopus 로고
    • Membrane type matrix metalloproteinase 1 activates progelatinase a without furin cleavage of the N-terminal domain
    • Cao J, Rehemtulla A, Bahou W, Zucker S 1996 Membrane type matrix metalloproteinase 1 activates progelatinase A without furin cleavage of the N-terminal domain. J Biol Chem 217: 30174-30180.
    • (1996) J Biol Chem , vol.217 , pp. 30174-30180
    • Cao, J.1    Rehemtulla, A.2    Bahou, W.3    Zucker, S.4
  • 62
    • 0029885707 scopus 로고    scopus 로고
    • Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase a and express intrinsic matrix-degrading activity
    • Pei DQ, Weiss SJ 1996 Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J Biol Chem 271:9135-9140.
    • (1996) J Biol Chem , vol.271 , pp. 9135-9140
    • Pei, D.Q.1    Weiss, S.J.2
  • 63
    • 0029034457 scopus 로고
    • Activation of progelatinase B (MMP-9) by gelatinase a (MMP-2)
    • Fridman R, Toth M, Peña D, Mobashery S 1995 Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2). Cancer Res 55:2548-1555.
    • (1995) Cancer Res , vol.55 , pp. 2548-11555
    • Fridman, R.1    Toth, M.2    Peña, D.3    Mobashery, S.4
  • 64
    • 0030037395 scopus 로고    scopus 로고
    • Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme
    • Knauper V, Will H, Lopez-Otin C, Smith B, Atkinson SJ, Stanton H, Hembry RM, Murphy G 1996 Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme. J Biol Chem 271:17124-31.
    • (1996) J Biol Chem , vol.271 , pp. 17124-17131
    • Knauper, V.1    Will, H.2    Lopez-Otin, C.3    Smith, B.4    Atkinson, S.J.5    Stanton, H.6    Hembry, R.M.7    Murphy, G.8
  • 65
    • 0030886122 scopus 로고    scopus 로고
    • Activation of progelatinase B (proMMP-9) by active collagenase-3 (MMP-13)
    • Knäuper V, Smith B, Lopéz-Otìn C, Murphy G 1997 Activation of progelatinase B (proMMP-9) by active collagenase-3 (MMP-13). Eur J Biochem 248:369-373.
    • (1997) Eur J Biochem , vol.248 , pp. 369-373
    • Knäuper, V.1    Smith, B.2    Lopéz-Otìn, C.3    Murphy, G.4
  • 66
    • 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, Knauper V, Stewart ML, D'Ortho MP, Stanton H, Hembry RM, Lopez-Otin 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 15:453-458.
    • (1998) Biochem J , vol.15 , pp. 453-458
    • Cowell, S.1    Knauper, V.2    Stewart, M.L.3    D'Ortho, M.P.4    Stanton, H.5    Hembry, R.M.6    Lopez-Otin, C.7    Reynolds, J.J.8    Murphy, G.9
  • 67
    • 0032168205 scopus 로고    scopus 로고
    • Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface
    • Lehti K, Lohi J, Valtanen H, Keski-Oja J 1998 Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface. Biochem J 334:345-353.
    • (1998) Biochem J , vol.334 , pp. 345-353
    • Lehti, K.1    Lohi, J.2    Valtanen, H.3    Keski-Oja, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.