메뉴 건너뛰기




Volumn 65, Issue , 2018, Pages 30-44

Aging-associated modifications of collagen affect its degradation by matrix metalloproteinases

Author keywords

Advanced glycation products; Cathepsins; Collagen; Matrix metalloproteinases; Mineralization; Proteolysis

Indexed keywords

ADVANCED GLYCATION END PRODUCT; CATHEPSIN K; CATHEPSIN V; COLLAGEN; COLLAGENASE 3; CYSTEINE DEPENDENT COLLAGENASE; FIBRILLAR COLLAGEN; GLYCOSAMINOGLYCAN; HYDROXYPROLINE; INTERSTITIAL COLLAGENASE; MATRIX METALLOPROTEINASE; NEUTROPHIL COLLAGENASE; UNCLASSIFIED DRUG; CTSK PROTEIN, MOUSE;

EID: 85021214429     PISSN: 0945053X     EISSN: 15691802     Source Type: Journal    
DOI: 10.1016/j.matbio.2017.06.004     Document Type: Article
Times cited : (125)

References (59)
  • 1
    • 84922333220 scopus 로고    scopus 로고
    • Remodelling the extracellular matrix in development and disease
    • Bonnans, C., Chou, J., Werb, Z., Remodelling the extracellular matrix in development and disease. Nat. Rev. Mol. Cell Biol. 15:12 (2014), 786–801.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , Issue.12 , pp. 786-801
    • Bonnans, C.1    Chou, J.2    Werb, Z.3
  • 2
    • 0037064041 scopus 로고    scopus 로고
    • Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain. The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage
    • Tam, E.M., Wu, Y.I., Butler, G.S., Stack, M.S., Overall, C.M., Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain. The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage. J. Biol. Chem. 277:41 (2002), 39005–39014.
    • (2002) J. Biol. Chem. , vol.277 , Issue.41 , pp. 39005-39014
    • Tam, E.M.1    Wu, Y.I.2    Butler, G.S.3    Stack, M.S.4    Overall, C.M.5
  • 4
    • 12544256661 scopus 로고    scopus 로고
    • Pivotal molecular determinants of peptidic and collagen triple helicase activities reside in the S3' subsite of matrix metalloproteinase 8 (MMP-8): the role of hydrogen bonding potential of ASN188 and TYR189 and the connecting cis bond
    • Pelman, G.R., Morrison, C.J., Overall, C.M., Pivotal molecular determinants of peptidic and collagen triple helicase activities reside in the S3' subsite of matrix metalloproteinase 8 (MMP-8): the role of hydrogen bonding potential of ASN188 and TYR189 and the connecting cis bond. J. Biol. Chem. 280:3 (2005), 2370–2377.
    • (2005) J. Biol. Chem. , vol.280 , Issue.3 , pp. 2370-2377
    • Pelman, G.R.1    Morrison, C.J.2    Overall, C.M.3
  • 5
    • 5744251586 scopus 로고    scopus 로고
    • Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities
    • Tam, E.M., Moore, T.R., Butler, G.S., Overall, C.M., Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities. J. Biol. Chem. 279:41 (2004), 43336–43344.
    • (2004) J. Biol. Chem. , vol.279 , Issue.41 , pp. 43336-43344
    • Tam, E.M.1    Moore, T.R.2    Butler, G.S.3    Overall, C.M.4
  • 6
    • 84867086656 scopus 로고    scopus 로고
    • Assessment of gelatinases (MMP-2 and MMP-9) by gelatin zymography
    • Toth, M., Sohail, A., Fridman, R., Assessment of gelatinases (MMP-2 and MMP-9) by gelatin zymography. Methods Mol. Biol. 878 (2012), 121–135.
    • (2012) Methods Mol. Biol. , vol.878 , pp. 121-135
    • Toth, M.1    Sohail, A.2    Fridman, R.3
  • 7
    • 0033848986 scopus 로고    scopus 로고
    • Matrix metalloproteinases: effectors of development and normal physiology
    • Vu, T.H., Werb, Z., Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev. 14:17 (2000), 2123–2133.
    • (2000) Genes Dev. , vol.14 , Issue.17 , pp. 2123-2133
    • Vu, T.H.1    Werb, Z.2
  • 8
    • 84930764947 scopus 로고    scopus 로고
    • Matrix remodeling by MMPs during wound repair
    • Rohani, M.G., Parks, W.C., Matrix remodeling by MMPs during wound repair. Matrix Biol. 44–46 (2015), 113–121.
    • (2015) Matrix Biol. , vol.44-46 , pp. 113-121
    • Rohani, M.G.1    Parks, W.C.2
  • 9
    • 58549088530 scopus 로고    scopus 로고
    • Collagens in the progression and complications of atherosclerosis
    • Adiguzel, E., Ahmad, P.J., Franco, C., Bendeck, M.P., Collagens in the progression and complications of atherosclerosis. Vasc. Med. 14:1 (2009), 73–89.
    • (2009) Vasc. Med. , vol.14 , Issue.1 , pp. 73-89
    • Adiguzel, E.1    Ahmad, P.J.2    Franco, C.3    Bendeck, M.P.4
  • 10
    • 82155195873 scopus 로고    scopus 로고
    • Altered matrix metalloproteinases and tissue inhibitors of metalloproteinases in embryos from diabetic rats during early organogenesis
    • Higa, R., Kurtz, M., Capobianco, E., Martinez, N., White, V., Jawerbaum, A., Altered matrix metalloproteinases and tissue inhibitors of metalloproteinases in embryos from diabetic rats during early organogenesis. Reprod. Toxicol. 32:4 (2011), 449–462.
    • (2011) Reprod. Toxicol. , vol.32 , Issue.4 , pp. 449-462
    • Higa, R.1    Kurtz, M.2    Capobianco, E.3    Martinez, N.4    White, V.5    Jawerbaum, A.6
  • 11
    • 0035990901 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumor invasion: role for cell migration
    • Nabeshima, K., Inoue, T., Shimao, Y., Sameshima, T., Matrix metalloproteinases in tumor invasion: role for cell migration. Pathol. Int. 52:4 (2002), 255–264.
    • (2002) Pathol. Int. , vol.52 , Issue.4 , pp. 255-264
    • Nabeshima, K.1    Inoue, T.2    Shimao, Y.3    Sameshima, T.4
  • 12
    • 0029176582 scopus 로고
    • Regulation of type I collagen genes expression
    • Karsenty, G., Park, R.W., Regulation of type I collagen genes expression. Int. Rev. Immunol. 12:2–4 (1995), 177–185.
    • (1995) Int. Rev. Immunol. , vol.12 , Issue.2-4 , pp. 177-185
    • Karsenty, G.1    Park, R.W.2
  • 13
    • 79952340427 scopus 로고    scopus 로고
    • Remodeling and homeostasis of the extracellular matrix: implications for fibrotic diseases and cancer
    • Cox, T.R., Erler, J.T., Remodeling and homeostasis of the extracellular matrix: implications for fibrotic diseases and cancer. Dis. Model. Mech. 4:2 (2011), 165–178.
    • (2011) Dis. Model. Mech. , vol.4 , Issue.2 , pp. 165-178
    • Cox, T.R.1    Erler, J.T.2
  • 14
    • 84555179609 scopus 로고    scopus 로고
    • Extracellular matrix degradation and remodeling in development and disease
    • Lu, P., Takai, K., Weaver, V.M., Werb, Z., Extracellular matrix degradation and remodeling in development and disease. Cold Spring Harb. Perspect. Biol., 3(12), 2011.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , Issue.12
    • Lu, P.1    Takai, K.2    Weaver, V.M.3    Werb, Z.4
  • 15
    • 84907332907 scopus 로고    scopus 로고
    • Intrinsic stiffness of extracellular matrix increases with age in skeletal muscles of mice
    • Wood, L.K., Kayupov, E., Gumucio, J.P., Mendias, C.L., Claflin, D.R., Brooks, S.V., Intrinsic stiffness of extracellular matrix increases with age in skeletal muscles of mice. J. Appl. Physiol. 117:4 (2014), 363–369.
    • (2014) J. Appl. Physiol. , vol.117 , Issue.4 , pp. 363-369
    • Wood, L.K.1    Kayupov, E.2    Gumucio, J.P.3    Mendias, C.L.4    Claflin, D.R.5    Brooks, S.V.6
  • 16
    • 0035157665 scopus 로고    scopus 로고
    • Age-related decrease in susceptibility of human articular cartilage to matrix metalloproteinase-mediated degradation: the role of advanced glycation end products
    • DeGroot, J., Verzijl, N., Wenting-Van Wijk, M.J., Bank, R.A., Lafeber, F.P., Bijlsma, J.W., TeKoppele, J.M., Age-related decrease in susceptibility of human articular cartilage to matrix metalloproteinase-mediated degradation: the role of advanced glycation end products. Arthritis Rheum. 44:11 (2001), 2562–2571.
    • (2001) Arthritis Rheum. , vol.44 , Issue.11 , pp. 2562-2571
    • DeGroot, J.1    Verzijl, N.2    Wenting-Van Wijk, M.J.3    Bank, R.A.4    Lafeber, F.P.5    Bijlsma, J.W.6    TeKoppele, J.M.7
  • 17
    • 33746920337 scopus 로고    scopus 로고
    • Advanced glycation end products: sparking the development of diabetic vascular injury
    • Goldin, A., Beckman, J.A., Schmidt, A.M., Creager, M.A., Advanced glycation end products: sparking the development of diabetic vascular injury. Circulation 114:6 (2006), 597–605.
    • (2006) Circulation , vol.114 , Issue.6 , pp. 597-605
    • Goldin, A.1    Beckman, J.A.2    Schmidt, A.M.3    Creager, M.A.4
  • 18
    • 33750904801 scopus 로고    scopus 로고
    • Vascular calcification: pathobiological mechanisms and clinical implications
    • Johnson, R.C., Leopold, J.A., Loscalzo, J., Vascular calcification: pathobiological mechanisms and clinical implications. Circ. Res. 99:10 (2006), 1044–1059.
    • (2006) Circ. Res. , vol.99 , Issue.10 , pp. 1044-1059
    • Johnson, R.C.1    Leopold, J.A.2    Loscalzo, J.3
  • 19
    • 84991738059 scopus 로고    scopus 로고
    • Calcific aortic valve disease is associated with layer-specific alterations in collagen architecture
    • Hutson, H.N., Marohl, T., Anderson, M., Eliceiri, K., Campagnola, P., Masters, K.S., Calcific aortic valve disease is associated with layer-specific alterations in collagen architecture. PLoS One, 11(9), 2016, e0163858.
    • (2016) PLoS One , vol.11 , Issue.9 , pp. e0163858
    • Hutson, H.N.1    Marohl, T.2    Anderson, M.3    Eliceiri, K.4    Campagnola, P.5    Masters, K.S.6
  • 21
    • 0023927040 scopus 로고
    • Proteoglycan-fibrillar collagen interactions
    • Scott, J.E., Proteoglycan-fibrillar collagen interactions. Biochem. J. 252:2 (1988), 313–323.
    • (1988) Biochem. J. , vol.252 , Issue.2 , pp. 313-323
    • Scott, J.E.1
  • 22
    • 84882794927 scopus 로고    scopus 로고
    • Age-dependent alterations of decorin glycosaminoglycans in human skin
    • Li, Y., Liu, Y., Xia, W., Lei, D., Voorhees, J.J., Fisher, G.J., Age-dependent alterations of decorin glycosaminoglycans in human skin. Sci. Rep., 3, 2013, 2422.
    • (2013) Sci. Rep. , vol.3 , pp. 2422
    • Li, Y.1    Liu, Y.2    Xia, W.3    Lei, D.4    Voorhees, J.J.5    Fisher, G.J.6
  • 23
    • 84991109624 scopus 로고    scopus 로고
    • Glycosaminoglycan and proteoglycan in skin aging
    • Lee, D.H., Oh, J.H., Chung, J.H., Glycosaminoglycan and proteoglycan in skin aging. J. Dermatol. Sci. 83:3 (2016), 174–181.
    • (2016) J. Dermatol. Sci. , vol.83 , Issue.3 , pp. 174-181
    • Lee, D.H.1    Oh, J.H.2    Chung, J.H.3
  • 24
    • 84942867447 scopus 로고    scopus 로고
    • Changes in structural-mechanical properties and degradability of collagen during aging-associated modifications
    • Panwar, P., Lamour, G., Mackenzie, N.C., Yang, H., Ko, F., Li, H., Bromme, D., Changes in structural-mechanical properties and degradability of collagen during aging-associated modifications. J. Biol. Chem. 290:38 (2015), 23291–23306.
    • (2015) J. Biol. Chem. , vol.290 , Issue.38 , pp. 23291-23306
    • Panwar, P.1    Lamour, G.2    Mackenzie, N.C.3    Yang, H.4    Ko, F.5    Li, H.6    Bromme, D.7
  • 26
    • 44049093740 scopus 로고    scopus 로고
    • Collagen turnover in normal and degenerate human intervertebral discs as determined by the racemization of aspartic acid
    • Sivan, S.S., Wachtel, E., Tsitron, E., Sakkee, N., van der Ham, F., Degroot, J., Roberts, S., Maroudas, A., Collagen turnover in normal and degenerate human intervertebral discs as determined by the racemization of aspartic acid. J. Biol. Chem. 283:14 (2008), 8796–8801.
    • (2008) J. Biol. Chem. , vol.283 , Issue.14 , pp. 8796-8801
    • Sivan, S.S.1    Wachtel, E.2    Tsitron, E.3    Sakkee, N.4    van der Ham, F.5    Degroot, J.6    Roberts, S.7    Maroudas, A.8
  • 27
    • 79851488199 scopus 로고    scopus 로고
    • Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up
    • Gautieri, A., Vesentini, S., Redaelli, A., Buehler, M.J., Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up. Nano Lett. 11:2 (2011), 757–766.
    • (2011) Nano Lett. , vol.11 , Issue.2 , pp. 757-766
    • Gautieri, A.1    Vesentini, S.2    Redaelli, A.3    Buehler, M.J.4
  • 28
    • 77955110336 scopus 로고    scopus 로고
    • Changes in collagen with aging maintain molecular stability after overload: evidence from an in vitro tendon model
    • Willett, T.L., Labow, R.S., Aldous, I.G., Avery, N.C., Lee, J.M., Changes in collagen with aging maintain molecular stability after overload: evidence from an in vitro tendon model. J. Biomech. Eng., 132(3), 2010, 031002.
    • (2010) J. Biomech. Eng. , vol.132 , Issue.3 , pp. 031002
    • Willett, T.L.1    Labow, R.S.2    Aldous, I.G.3    Avery, N.C.4    Lee, J.M.5
  • 29
    • 84940459597 scopus 로고    scopus 로고
    • The role of collagen crosslinks in ageing and diabetes - the good, the bad, and the ugly
    • Snedeker, J.G., Gautieri, A., The role of collagen crosslinks in ageing and diabetes - the good, the bad, and the ugly. Muscles Ligaments Tendons J. 4:3 (2014), 303–308.
    • (2014) Muscles Ligaments Tendons J. , vol.4 , Issue.3 , pp. 303-308
    • Snedeker, J.G.1    Gautieri, A.2
  • 30
    • 84894251266 scopus 로고    scopus 로고
    • Ectopic mineralization disorders of the extracellular matrix of connective tissue: molecular genetics and pathomechanisms of aberrant calcification
    • Li, Q., Jiang, Q., Uitto, J., Ectopic mineralization disorders of the extracellular matrix of connective tissue: molecular genetics and pathomechanisms of aberrant calcification. Matrix Biol. 33 (2014), 23–28.
    • (2014) Matrix Biol. , vol.33 , pp. 23-28
    • Li, Q.1    Jiang, Q.2    Uitto, J.3
  • 31
    • 84895801260 scopus 로고    scopus 로고
    • Vascular effects of advanced glycation endproducts: clinical effects and molecular mechanisms
    • Stirban, A., Gawlowski, T., Roden, M., Vascular effects of advanced glycation endproducts: clinical effects and molecular mechanisms. Mol. Metab. 3:2 (2014), 94–108.
    • (2014) Mol. Metab. , vol.3 , Issue.2 , pp. 94-108
    • Stirban, A.1    Gawlowski, T.2    Roden, M.3
  • 32
    • 84900337704 scopus 로고    scopus 로고
    • Age- and diabetes-related nonenzymatic crosslinks in collagen fibrils: candidate amino acids involved in advanced glycation end-products
    • Gautieri, A., Redaelli, A., Buehler, M.J., Vesentini, S., Age- and diabetes-related nonenzymatic crosslinks in collagen fibrils: candidate amino acids involved in advanced glycation end-products. Matrix Biol. 34 (2014), 89–95.
    • (2014) Matrix Biol. , vol.34 , pp. 89-95
    • Gautieri, A.1    Redaelli, A.2    Buehler, M.J.3    Vesentini, S.4
  • 33
    • 84874300261 scopus 로고    scopus 로고
    • Effects of cysteine proteases on the structural and mechanical properties of collagen fibers
    • Panwar, P., Du, X., Sharma, V., Lamour, G., Castro, M., Li, H., Bromme, D., Effects of cysteine proteases on the structural and mechanical properties of collagen fibers. J. Biol. Chem. 288:8 (2013), 5940–5950.
    • (2013) J. Biol. Chem. , vol.288 , Issue.8 , pp. 5940-5950
    • Panwar, P.1    Du, X.2    Sharma, V.3    Lamour, G.4    Castro, M.5    Li, H.6    Bromme, D.7
  • 34
    • 67649628133 scopus 로고    scopus 로고
    • Cathepsin K inhibitors for osteoporosis and potential off-target effects
    • Bromme, D., Lecaille, F., Cathepsin K inhibitors for osteoporosis and potential off-target effects. Expert Opin. Investig. Drugs 18:5 (2009), 585–600.
    • (2009) Expert Opin. Investig. Drugs , vol.18 , Issue.5 , pp. 585-600
    • Bromme, D.1    Lecaille, F.2
  • 35
    • 35248897299 scopus 로고    scopus 로고
    • Cathepsin cysteine proteases in cardiovascular disease
    • Lutgens, S.P., Cleutjens, K.B., Daemen, M.J., Heeneman, S., Cathepsin cysteine proteases in cardiovascular disease. FASEB J. 21:12 (2007), 3029–3041.
    • (2007) FASEB J. , vol.21 , Issue.12 , pp. 3029-3041
    • Lutgens, S.P.1    Cleutjens, K.B.2    Daemen, M.J.3    Heeneman, S.4
  • 36
    • 77953442640 scopus 로고    scopus 로고
    • Future of anticathepsin K drugs: dual therapy for skeletal disease and atherosclerosis?
    • Podgorski, I., Future of anticathepsin K drugs: dual therapy for skeletal disease and atherosclerosis?. Future Med. Chem. 1:1 (2009), 21–34.
    • (2009) Future Med. Chem. , vol.1 , Issue.1 , pp. 21-34
    • Podgorski, I.1
  • 38
    • 79957650183 scopus 로고    scopus 로고
    • The effect of cathepsin K deficiency on airway development and TGF-beta1 degradation
    • Zhang, D., Leung, N., Weber, E., Saftig, P., Bromme, D., The effect of cathepsin K deficiency on airway development and TGF-beta1 degradation. Respir. Res., 12, 2011, 72.
    • (2011) Respir. Res. , vol.12 , pp. 72
    • Zhang, D.1    Leung, N.2    Weber, E.3    Saftig, P.4    Bromme, D.5
  • 39
    • 49749135546 scopus 로고    scopus 로고
    • Role of cathepsin K in structural changes in brachiocephalic artery during progression of atherosclerosis in apoE-deficient mice
    • Samokhin, A.O., Wong, A., Saftig, P., Bromme, D., Role of cathepsin K in structural changes in brachiocephalic artery during progression of atherosclerosis in apoE-deficient mice. Atherosclerosis 200:1 (2008), 58–68.
    • (2008) Atherosclerosis , vol.200 , Issue.1 , pp. 58-68
    • Samokhin, A.O.1    Wong, A.2    Saftig, P.3    Bromme, D.4
  • 41
    • 0031931187 scopus 로고    scopus 로고
    • Arterial calcification and not lumen stenosis is highly correlated with atherosclerotic plaque burden in humans: a histologic study of 723 coronary artery segments using nondecalcifying methodology
    • Sangiorgi, G., Rumberger, J.A., Severson, A., Edwards, W.D., Gregoire, J., Fitzpatrick, L.A., Schwartz, R.S., Arterial calcification and not lumen stenosis is highly correlated with atherosclerotic plaque burden in humans: a histologic study of 723 coronary artery segments using nondecalcifying methodology. J. Am. Coll. Cardiol. 31:1 (1998), 126–133.
    • (1998) J. Am. Coll. Cardiol. , vol.31 , Issue.1 , pp. 126-133
    • Sangiorgi, G.1    Rumberger, J.A.2    Severson, A.3    Edwards, W.D.4    Gregoire, J.5    Fitzpatrick, L.A.6    Schwartz, R.S.7
  • 42
    • 0037388822 scopus 로고    scopus 로고
    • Multiple risk factor intervention reduces cardiovascular risk in hypertensive patients with echolucent plaques in the carotid artery
    • Schmidt, C., Fagerberg, B., Wikstrand, J., Hulthe, J., R.I.S.S. Group, Multiple risk factor intervention reduces cardiovascular risk in hypertensive patients with echolucent plaques in the carotid artery. J. Intern. Med. 253:4 (2003), 430–438.
    • (2003) J. Intern. Med. , vol.253 , Issue.4 , pp. 430-438
    • Schmidt, C.1    Fagerberg, B.2    Wikstrand, J.3    Hulthe, J.4    R.I.S.S. Group5
  • 43
    • 33947512363 scopus 로고    scopus 로고
    • Composition of the stable carotid plaque: insights from a multidetector computed tomography study of plaque volume
    • Nandalur, K.R., Hardie, A.D., Raghavan, P., Schipper, M.J., Baskurt, E., Kramer, C.M., Composition of the stable carotid plaque: insights from a multidetector computed tomography study of plaque volume. Stroke 38:3 (2007), 935–940.
    • (2007) Stroke , vol.38 , Issue.3 , pp. 935-940
    • Nandalur, K.R.1    Hardie, A.D.2    Raghavan, P.3    Schipper, M.J.4    Baskurt, E.5    Kramer, C.M.6
  • 44
    • 84856988081 scopus 로고    scopus 로고
    • Effect of calcification on the mechanical stability of plaque based on a three-dimensional carotid bifurcation model
    • Wong, K.K., Thavornpattanapong, P., Cheung, S.C., Sun, Z., Tu, J., Effect of calcification on the mechanical stability of plaque based on a three-dimensional carotid bifurcation model. BMC Cardiovasc. Disord., 12, 2012, 7.
    • (2012) BMC Cardiovasc. Disord. , vol.12 , pp. 7
    • Wong, K.K.1    Thavornpattanapong, P.2    Cheung, S.C.3    Sun, Z.4    Tu, J.5
  • 46
    • 0037047275 scopus 로고    scopus 로고
    • Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate
    • Li, Z., Hou, W.S., Escalante-Torres, C.R., Gelb, B.D., Bromme, D., Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate. J. Biol. Chem. 277:32 (2002), 28669–28676.
    • (2002) J. Biol. Chem. , vol.277 , Issue.32 , pp. 28669-28676
    • Li, Z.1    Hou, W.S.2    Escalante-Torres, C.R.3    Gelb, B.D.4    Bromme, D.5
  • 47
    • 1242294466 scopus 로고    scopus 로고
    • Regulation of collagenase activities of human cathepsins by glycosaminoglycans
    • Li, Z., Yasuda, Y., Li, W., Bogyo, M., Katz, N., Gordon, R.E., Fields, G.B., Bromme, D., Regulation of collagenase activities of human cathepsins by glycosaminoglycans. J. Biol. Chem. 279:7 (2004), 5470–5479.
    • (2004) J. Biol. Chem. , vol.279 , Issue.7 , pp. 5470-5479
    • Li, Z.1    Yasuda, Y.2    Li, W.3    Bogyo, M.4    Katz, N.5    Gordon, R.E.6    Fields, G.B.7    Bromme, D.8
  • 49
    • 0017664230 scopus 로고
    • The degradation of cartilage proteoglycans by tissue proteinases. Proteoglycan structure and its susceptibility to proteolysis
    • Roughley, P.J., Barrett, A.J., The degradation of cartilage proteoglycans by tissue proteinases. Proteoglycan structure and its susceptibility to proteolysis. Biochem. J. 167:3 (1977), 629–637.
    • (1977) Biochem. J. , vol.167 , Issue.3 , pp. 629-637
    • Roughley, P.J.1    Barrett, A.J.2
  • 50
    • 0024262415 scopus 로고
    • Degradation of the proteoglycans of human articular cartilage by reactive oxygen metabolites
    • Roberts, C.R., Mort, J.S., Roughley, P.J., Degradation of the proteoglycans of human articular cartilage by reactive oxygen metabolites. Basic Life Sci. 49 (1988), 353–356.
    • (1988) Basic Life Sci. , vol.49 , pp. 353-356
    • Roberts, C.R.1    Mort, J.S.2    Roughley, P.J.3
  • 51
    • 17644443643 scopus 로고    scopus 로고
    • Age-dependent changes in glycosaminoglycan content in the skin of fasted rats. A possible mechanism
    • Cechowska-Pasko, M., Palka, J., Age-dependent changes in glycosaminoglycan content in the skin of fasted rats. A possible mechanism. Exp. Toxicol. Pathol. 52:2 (2000), 127–131.
    • (2000) Exp. Toxicol. Pathol. , vol.52 , Issue.2 , pp. 127-131
    • Cechowska-Pasko, M.1    Palka, J.2
  • 52
    • 0036674029 scopus 로고    scopus 로고
    • The effects of age and sex on chondroitin sulfates in normal synovial fluid
    • Nakayama, Y., Narita, T., Mori, A., Uesaka, S., Miyazaki, K., Ito, H., The effects of age and sex on chondroitin sulfates in normal synovial fluid. Arthritis Rheum. 46:8 (2002), 2105–2108.
    • (2002) Arthritis Rheum. , vol.46 , Issue.8 , pp. 2105-2108
    • Nakayama, Y.1    Narita, T.2    Mori, A.3    Uesaka, S.4    Miyazaki, K.5    Ito, H.6
  • 53
    • 0018870303 scopus 로고
    • Age-related changes in the structure of the proteoglycan subunits from human articular cartilage
    • Roughley, P.J., White, R.J., Age-related changes in the structure of the proteoglycan subunits from human articular cartilage. J. Biol. Chem. 255:1 (1980), 217–224.
    • (1980) J. Biol. Chem. , vol.255 , Issue.1 , pp. 217-224
    • Roughley, P.J.1    White, R.J.2
  • 54
    • 0032522487 scopus 로고    scopus 로고
    • Critical roles of glycosaminoglycan side chains of cartilage proteoglycan (aggrecan) in antigen recognition and presentation
    • Glant, T.T., Buzas, E.I., Finnegan, A., Negroiu, G., Cs-Szabo, G., Mikecz, K., Critical roles of glycosaminoglycan side chains of cartilage proteoglycan (aggrecan) in antigen recognition and presentation. J. Immunol. 160:8 (1998), 3812–3819.
    • (1998) J. Immunol. , vol.160 , Issue.8 , pp. 3812-3819
    • Glant, T.T.1    Buzas, E.I.2    Finnegan, A.3    Negroiu, G.4    Cs-Szabo, G.5    Mikecz, K.6
  • 55
    • 0023377518 scopus 로고
    • Initial characterization of a neutral metallo-endoproteinase, active on native 3/4-collagen fragments, synthesized by ROS 17/2.8 osteoblastic cells, periodontal fibroblasts and identified in gingival crevicular fluid
    • Overal, C.M., Sodek, J., Initial characterization of a neutral metallo-endoproteinase, active on native 3/4-collagen fragments, synthesized by ROS 17/2.8 osteoblastic cells, periodontal fibroblasts and identified in gingival crevicular fluid. J. Dent. Res. 66 (1987), 1271–1281.
    • (1987) J. Dent. Res. , vol.66 , pp. 1271-1281
    • Overal, C.M.1    Sodek, J.2
  • 58
    • 0038687865 scopus 로고    scopus 로고
    • Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization
    • Brömme, D., Li, Z., Barnes, M., Mehler, E., Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry 38 (1999), 2377–2385.
    • (1999) Biochemistry , vol.38 , pp. 2377-2385
    • Brömme, D.1    Li, Z.2    Barnes, M.3    Mehler, E.4
  • 59
    • 7444234178 scopus 로고    scopus 로고
    • Tensile testing of a single ultrafine polymeric fiber
    • Tan, E.P., Ng, S.Y., Lim, C.T., Tensile testing of a single ultrafine polymeric fiber. Biomaterials 26:13 (2005), 1453–1456.
    • (2005) Biomaterials , vol.26 , Issue.13 , pp. 1453-1456
    • Tan, E.P.1    Ng, S.Y.2    Lim, C.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.