메뉴 건너뛰기




Volumn 27, Issue 11, 2012, Pages 1471-1479

Experimental diabetes modulates collagen remodelling of joints in rats

Author keywords

Collagen remodeling; Diabetes; Joint; Streptozotocin

Indexed keywords

COLLAGEN;

EID: 84869429352     PISSN: 02133911     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (41)

References (39)
  • 1
    • 0346734383 scopus 로고    scopus 로고
    • Biochemical markers of types I and III collagen and limited joint mobility in type 1 diabetic patients
    • Arkkila P.E., Koskinen P.J., Kantola I.M., Rönnemaa T., Seppänen E. and Viikari J.S. (2003). Biochemical markers of types I and III collagen and limited joint mobility in type 1 diabetic patients. Acta Diabetol. 40, 151-155.
    • (2003) Acta Diabetol. , vol.40 , pp. 151-155
    • Arkkila, P.E.1    Koskinen, P.J.2    Kantola, I.M.3    Rönnemaa, T.4    Seppänen, E.5    Viikari, J.S.6
  • 2
    • 45149134399 scopus 로고    scopus 로고
    • Which musculoskeletal complications are most frequently seen in type 2 diabetes mellitus?
    • Aydeniz A., Gursoy S. and Guney E. (2008). Which musculoskeletal complications are most frequently seen in type 2 diabetes mellitus? J. Int. Med. Res. 36, 505-511.
    • (2008) J. Int. Med. Res. , vol.36 , pp. 505-511
    • Aydeniz, A.1    Gursoy, S.2    Guney, E.3
  • 4
    • 0036898999 scopus 로고    scopus 로고
    • Genotoxicity of streptozotocin
    • Bolzán A.D. and Bianchi M.S. (2002). Genotoxicity of streptozotocin. Mutat. Res. 512(2-3), 121-134.
    • (2002) Mutat. Res. , vol.512 , Issue.2-3 , pp. 121-134
    • Bolzán, A.D.1    Bianchi, M.S.2
  • 5
    • 0024788007 scopus 로고
    • Changes in solubility, non-enzymatic glycation, and fluorescence of collagen in tail tendons from diabetic rats
    • Brennan M. (1989). Changes in solubility, non-enzymatic glycation, and fluorescence of collagen in tail tendons from diabetic rats. J. Biol. Chem. 264, 20947-20952.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20947-20952
    • Brennan, M.1
  • 7
    • 1942519412 scopus 로고    scopus 로고
    • Insulin-dependent diabetes impairs the inflammatory response and delays angiogenesis following Achilles tendon injury
    • Chbinou N. and Frenette J. (2004). Insulin-dependent diabetes impairs the inflammatory response and delays angiogenesis following Achilles tendon injury. Am. J. Physiol. Regul. Integr. Comp. Physiol. 286, R952-R957.
    • (2004) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.286
    • Chbinou, N.1    Frenette, J.2
  • 8
    • 0024451751 scopus 로고
    • Are the polarization colors of Picrosirius red-stained collagen determined only by the diameter of the fibers?
    • Dayan D., Hiss Y., Hirshberg A., Bubis J.J. and Woiman M. (1989). Are the polarization colors of Picrosirius red-stained collagen determined only by the diameter of the fibers? Histochemistry 93, 27-29.
    • (1989) Histochemistry , vol.93 , pp. 27-29
    • Dayan, D.1    Hiss, Y.2    Hirshberg, A.3    Bubis, J.J.4    Woiman, M.5
  • 9
    • 0028928948 scopus 로고
    • Collagen structure and cartilage matrix integrity
    • Eyre D.R. and Wu J-J. (1995). Collagen structure and cartilage matrix integrity. J. Rheumatol. 22, 82-85.
    • (1995) J. Rheumatol. , vol.22 , pp. 82-85
    • Eyre, D.R.1    Wu, J-J.2
  • 10
    • 70350757829 scopus 로고    scopus 로고
    • Diabetic osteoarthropathy
    • Fujinaka Y. (2009). Diabetic osteoarthropathy. Clin. Calcium 19, 1299-1303.
    • (2009) Clin. Calcium , vol.19 , pp. 1299-1303
    • Fujinaka, Y.1
  • 11
    • 0034646621 scopus 로고    scopus 로고
    • Structural Organization of distinct domains within the non-collagenous N-terminal region of collagen type XI
    • Gregory K., Oxford J.T., Chen Y., (2000). Structural Organization of distinct domains within the non-collagenous N-terminal region of collagen type XI. J. Biol. Chem. 275, 11498-11506.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11498-11506
    • Gregory, K.1    Oxford, J.T.2    Chen, Y.3
  • 14
    • 0018361379 scopus 로고
    • A simple and sensitive method for the quantitative estimation of collagen
    • Junqueira L.C.U., Bignolas C. and Brentani R.R. (1979). A simple and sensitive method for the quantitative estimation of collagen. Anal Biochem. 94, 96-99.
    • (1979) Anal Biochem. , vol.94 , pp. 96-99
    • Junqueira, L.C.U.1    Bignolas, C.2    Brentani, R.R.3
  • 15
    • 0020320387 scopus 로고
    • The influence of tissue section thickness on the study of collagen by the picrosirius polarization method
    • Junqueira L.C.U., Montes G.S. and Sanchez E.M. (1982). The influence of tissue section thickness on the study of collagen by the picrosirius polarization method. Histochemistry 74, 153-156.
    • (1982) Histochemistry , vol.74 , pp. 153-156
    • Junqueira, L.C.U.1    Montes, G.S.2    Sanchez, E.M.3
  • 16
    • 68849118986 scopus 로고    scopus 로고
    • The presence of limited joint mobility is significantly associated with multiple digit involvement by stenosing flexor tenosynovitis in diabetics
    • Kameyama M., Meguro S., Funae O., Atsumi Y. and Ikegami H. (2009). The presence of limited joint mobility is significantly associated with multiple digit involvement by stenosing flexor tenosynovitis in diabetics. J. Rheumatol. 36, 1686-1690.
    • (2009) J. Rheumatol. , vol.36 , pp. 1686-1690
    • Kameyama, M.1    Meguro, S.2    Funae, O.3    Atsumi, Y.4    Ikegami, H.5
  • 17
    • 0041829207 scopus 로고    scopus 로고
    • TGF-ß1 causes airway fibrosis and increased collagen I and III mRNA in mice
    • Kenyon N.J., Ward R.W., McGrew G. and Last J.A. (2003). TGF-ß1 causes airway fibrosis and increased collagen I and III mRNA in mice. Thorax 58, 772-777.
    • (2003) Thorax , vol.58 , pp. 772-777
    • Kenyon, N.J.1    Ward, R.W.2    McGrew, G.3    Last, J.A.4
  • 18
    • 0019199299 scopus 로고
    • Sirius red-collagen interaction: A method for the measurement of collagen and bacterial collagenase activity
    • Kuttan R. and Di Ferrante N. (1980). Sirius red-collagen interaction: a method for the measurement of collagen and bacterial collagenase activity. Biochem. Int. 1, 455-462.
    • (1980) Biochem. Int. , vol.1 , pp. 455-462
    • Kuttan, R.1    Di Ferrante, N.2
  • 19
    • 0019831310 scopus 로고
    • Characterization of Nglycosylated type I collagen in streptozotocin-induced diabetes
    • Le Pape A., Muh P. and Bailey A.J. (1981). Characterization of Nglycosylated type I collagen in streptozotocin-induced diabetes. Biochem. J. 197, 405-412.
    • (1981) Biochem. J. , vol.197 , pp. 405-412
    • Le Pape, A.1    Muh, P.2    Bailey, A.J.3
  • 20
    • 0002046471 scopus 로고
    • Collagen
    • In, 2nd ed. Hay E.D. (ed). Plenum Press. New York
    • Linsenmayer T.F. (1991). Collagen. In: Cell biology of extracellular matrix. 2nd ed. Hay E.D. (ed). Plenum Press. New York. pp 7-43.
    • (1991) Cell biology of extracellular matrix , pp. 7-43
    • Linsenmayer, T.F.1
  • 21
    • 0022186671 scopus 로고
    • Sensitive spectophotometer method for the quantitative estimation of collagen
    • Marotta M. and Martino G. (1985). Sensitive spectophotometer method for the quantitative estimation of collagen. Anal. Biochem. 150, 86-90.
    • (1985) Anal. Biochem. , vol.150 , pp. 86-90
    • Marotta, M.1    Martino, G.2
  • 22
    • 77949678912 scopus 로고    scopus 로고
    • The anatomical basis for a novel classification of osteoarthritis and allied disorders
    • McGonagle D., Tan A.L., Carey J. and Benjamin M. (2010). The anatomical basis for a novel classification of osteoarthritis and allied disorders. J. Anat. 216, 279-291.
    • (2010) J. Anat. , vol.216 , pp. 279-291
    • McGonagle, D.1    Tan, A.L.2    Carey, J.3    Benjamin, M.4
  • 23
    • 12544255038 scopus 로고    scopus 로고
    • The increase in denaturation temperature following cross-linking of collagen is caused by dehydration of the fibres
    • Miles C.A., Avery N.C., Rodin V.V. and Bailey A.J. (2005). The increase in denaturation temperature following cross-linking of collagen is caused by dehydration of the fibres. J. Mol. Biol. 346, 551-556.
    • (2005) J. Mol. Biol. , vol.346 , pp. 551-556
    • Miles, C.A.1    Avery, N.C.2    Rodin, V.V.3    Bailey, A.J.4
  • 24
    • 0033739702 scopus 로고    scopus 로고
    • Architectural remodelling in acute and chronic interstitial lung disease: Fibrosis or fibroelastosis?
    • Negri E.M., Montes G.S., Saldiva P.H. and Capelozzi V.L. (2000). Architectural remodelling in acute and chronic interstitial lung disease: fibrosis or fibroelastosis? Histopathology 37, 393-401.
    • (2000) Histopathology , vol.37 , pp. 393-401
    • Negri, E.M.1    Montes, G.S.2    Saldiva, P.H.3    Capelozzi, V.L.4
  • 28
    • 0024318692 scopus 로고
    • Histochemical evaluation of lung collagen content in acute and chronic interstitial diseases
    • Saldiva P.H., Delmonte V.C., Carvalho C.R., Kairalla R.A. and Auler Júnior J.O. (1989). Histochemical evaluation of lung collagen content in acute and chronic interstitial diseases. Chest 95, 953-957.
    • (1989) Chest , vol.95 , pp. 953-957
    • Saldiva, P.H.1    Delmonte, V.C.2    Carvalho, C.R.3    Kairalla, R.A.4    Auler Júnior, J.O.5
  • 30
    • 40749116413 scopus 로고    scopus 로고
    • Changes in histoanatomical distribution of types I, III and V collagen promote adaptative remodeling in posterior tibial tendon rupture
    • Satomi E., Teodoro W.R., Parra E.R., Fernandes T.D., Velosa A.P., Capelozzi V.L. and and Yoshinari N.H. (2008). Changes in histoanatomical distribution of types I, III and V collagen promote adaptative remodeling in posterior tibial tendon rupture. Clinics 63, 9-14.
    • (2008) Clinics , vol.63 , pp. 9-14
    • Satomi, E.1    Teodoro, W.R.2    Parra, E.R.3    Fernandes, T.D.4    Velosa, A.P.5    Capelozzi, V.L.6    Yoshinari, N.H.7
  • 31
    • 76449097123 scopus 로고    scopus 로고
    • Relationship of an advanced glycation end product, plasma carboxymethyl-lysine, with slow walking speed in older adults: The In CHIANTI study
    • Semba R.D., Bandinelli S., Sun K., Guralnik J.M. and Ferrucci L. (2010). Relationship of an advanced glycation end product, plasma carboxymethyl-lysine, with slow walking speed in older adults: the In CHIANTI study. Eur. J. Appl. Physiol. 108, 191-195.
    • (2010) Eur. J. Appl. Physiol. , vol.108 , pp. 191-195
    • Semba, R.D.1    Bandinelli, S.2    Sun, K.3    Guralnik, J.M.4    Ferrucci, L.5
  • 32
    • 0023888603 scopus 로고
    • Decreased collagen production in diabetic rats
    • Spanheimer R.G., Umpierrez G.E. and Stumpf V. (1988). Decreased collagen production in diabetic rats. Diabetes 37, 371-376.
    • (1988) Diabetes , vol.37 , pp. 371-376
    • Spanheimer, R.G.1    Umpierrez, G.E.2    Stumpf, V.3
  • 33
    • 0034670138 scopus 로고    scopus 로고
    • p-Dimethylaminobenzaldehyde-reactive substances in tail tendon collagen of streptozotocin-diabetic rats: Temporal relation to biomechanical properties and advanced glycation endproduct (AGE)-related fluorescence
    • Stefek M., Gajdosik A., Gajdosikova A. and Krizanova L. (2000). p-Dimethylaminobenzaldehyde-reactive substances in tail tendon collagen of streptozotocin-diabetic rats: temporal relation to biomechanical properties and advanced glycation endproduct (AGE)-related fluorescence. Biochim. Biophys. Acta 1502, 398-404.
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 398-404
    • Stefek, M.1    Gajdosik, A.2    Gajdosikova, A.3    Krizanova, L.4
  • 37
    • 0024823327 scopus 로고
    • Nutritional and hormonal regulation of articular collagen production in diabetic animals
    • Umpierrez G.E., Goldstein S., Phillips L.S. and Spanheimer R.G. (1989). Nutritional and hormonal regulation of articular collagen production in diabetic animals. Diabetes 38, 758-63.
    • (1989) Diabetes , vol.38 , pp. 758-763
    • Umpierrez, G.E.1    Goldstein, S.2    Phillips, L.S.3    Spanheimer, R.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.