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Volumn 61, Issue 3, 1997, Pages 223-229

Estimation of total collagen and types I and III collagen in canine rotator cuff tendons

Author keywords

Collagen; Hydroxyproline determination; Peptide mapping; Rotator cuff; Tendon

Indexed keywords

COLLAGEN; COLLAGEN TYPE 1; COLLAGEN TYPE 2; COLLAGEN TYPE 3; COLLAGEN TYPE 4; HYDROXYPROLINE;

EID: 0030872247     PISSN: 0171967X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002239900327     Document Type: Article
Times cited : (35)

References (43)
  • 1
    • 0001697085 scopus 로고
    • Biomechanics of the shoulder
    • Rockwood CA Jr. Matsen FA III (eds). WB Saunders, Philadelphia
    • Morrey BF, An K-N (1990) Biomechanics of the shoulder. In: Rockwood CA Jr. Matsen FA III (eds). The shoulder. WB Saunders, Philadelphia, pp 208-245
    • (1990) The Shoulder , pp. 208-245
    • Morrey, B.F.1    An, K.-N.2
  • 2
    • 0018682335 scopus 로고
    • The influence of mechanical forces on the glycosaminoglycan content of the rabbit flexor digitorum profundus tendon
    • Gillard GC, Reilly HC, Bell-Booth PG, Flint MH (1979) The influence of mechanical forces on the glycosaminoglycan content of the rabbit flexor digitorum profundus tendon. Connect Tissue Res 7:27-46
    • (1979) Connect Tissue Res , vol.7 , pp. 27-46
    • Gillard, G.C.1    Reilly, H.C.2    Bell-Booth, P.G.3    Flint, M.H.4
  • 3
    • 0023083361 scopus 로고
    • Site-related variations in glycosaminoglycan content and swelling properties of bovine flexor tendon
    • Koob TJ, Vogel KG (1987) Site-related variations in glycosaminoglycan content and swelling properties of bovine flexor tendon. J Orthop Res 5:414-424
    • (1987) J Orthop Res , vol.5 , pp. 414-424
    • Koob, T.J.1    Vogel, K.G.2
  • 4
    • 0019468685 scopus 로고
    • Bursae, tendons and ligaments
    • Canoso JJ (1981) Bursae, tendons and ligaments. Clin Rheum Dis 7:189-221
    • (1981) Clin Rheum Dis , vol.7 , pp. 189-221
    • Canoso, J.J.1
  • 5
    • 0019729408 scopus 로고
    • Localization of collagen types in tissues
    • Von der Mark K (1981) Localization of collagen types in tissues. Int Rev Connect Tissue Res 9:265-324
    • (1981) Int Rev Connect Tissue Res , vol.9 , pp. 265-324
    • Von Der Mark, K.1
  • 6
    • 0021269042 scopus 로고
    • The distribution of types I and III collagen and fibronectin in the healing equine tendon
    • Williams IF, McCullagh KG, Silver IA (1984) The distribution of types I and III collagen and fibronectin in the healing equine tendon. Conn Tissue Res 12:211-222
    • (1984) Conn Tissue Res , vol.12 , pp. 211-222
    • Williams, I.F.1    McCullagh, K.G.2    Silver, I.A.3
  • 8
    • 0028243182 scopus 로고
    • Tendon degeneration and chronic shoulder pain: Changes in the collagen composition of the human rotator cuff tendons in rotator cuff tendinitis
    • Riley GP, Harrall RL, Constant CR, Chard MD, Cawston TE, Hazleman BL (1994) Tendon degeneration and chronic shoulder pain: changes in the collagen composition of the human rotator cuff tendons in rotator cuff tendinitis. Ann Rheum Dis 53:359-366
    • (1994) Ann Rheum Dis , vol.53 , pp. 359-366
    • Riley, G.P.1    Harrall, R.L.2    Constant, C.R.3    Chard, M.D.4    Cawston, T.E.5    Hazleman, B.L.6
  • 9
    • 0028058831 scopus 로고
    • Immunohistochemical distribution of types I, II and III collagens in the rabbit supraspinatous tendon insertion
    • Kumagai J, Sarkar K, Uhthoff HK, Okawara Y, Ooshima A (1994) Immunohistochemical distribution of types I, II and III collagens in the rabbit supraspinatous tendon insertion. J Anat 185:279-284
    • (1994) J Anat , vol.185 , pp. 279-284
    • Kumagai, J.1    Sarkar, K.2    Uhthoff, H.K.3    Okawara, Y.4    Ooshima, A.5
  • 10
    • 0028003901 scopus 로고
    • The collagen types in the attachment zone of rotator cuff tendons in the elderly: An immunohistochemical study
    • Kumagai J, Sarkar K, Uhthoff HK (1994) The collagen types in the attachment zone of rotator cuff tendons in the elderly: an immunohistochemical study. J Rheumatol 21:2096-2100
    • (1994) J Rheumatol , vol.21 , pp. 2096-2100
    • Kumagai, J.1    Sarkar, K.2    Uhthoff, H.K.3
  • 11
    • 0015534741 scopus 로고
    • Biochemistry of the hydroxyprolines
    • Kuttan R, Radhakrishnan AN (1973) Biochemistry of the hydroxyprolines. Adv Enzymol 37:273-347
    • (1973) Adv Enzymol , vol.37 , pp. 273-347
    • Kuttan, R.1    Radhakrishnan, A.N.2
  • 12
    • 0018890003 scopus 로고
    • Metabolism of proline and the hydroxyprolines
    • Adams E, Frank L (1980) Metabolism of proline and the hydroxyprolines. Annu Rev Biochem 49:1005-1061
    • (1980) Annu Rev Biochem , vol.49 , pp. 1005-1061
    • Adams, E.1    Frank, L.2
  • 13
    • 76549214686 scopus 로고
    • The determination of collagen and elastin in tissues
    • Newman RE, Logan MA (1950) The determination of collagen and elastin in tissues. J Biol Chem 186:549-556
    • (1950) J Biol Chem , vol.186 , pp. 549-556
    • Newman, R.E.1    Logan, M.A.2
  • 14
    • 0018081898 scopus 로고
    • Characterization of pepsin-solubilized bovine heart-valve collagen
    • Bashey RI, Bashey HM, Jimenez SA (1978) Characterization of pepsin-solubilized bovine heart-valve collagen. Biochem J 173:885-894
    • (1978) Biochem J , vol.173 , pp. 885-894
    • Bashey, R.I.1    Bashey, H.M.2    Jimenez, S.A.3
  • 15
    • 0018933925 scopus 로고
    • Cell morphology and collagen types in equine tendon scar
    • Williams IF, Heaton A, McCullagh KG (1980) Cell morphology and collagen types in equine tendon scar. Res Vet Sci 28:302-310
    • (1980) Res Vet Sci , vol.28 , pp. 302-310
    • Williams, I.F.1    Heaton, A.2    McCullagh, K.G.3
  • 16
    • 0017115666 scopus 로고
    • Collagen fractionation: Separation of native types I, II and III by differential precipitation
    • Trelstad RL, Catanese VM, Rubin DF (1976) Collagen fractionation: separation of native types I, II and III by differential precipitation. Analyt Biochem 71:114-118
    • (1976) Analyt Biochem , vol.71 , pp. 114-118
    • Trelstad, R.L.1    Catanese, V.M.2    Rubin, D.F.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0017756636 scopus 로고
    • Altered relation of two collagen types in osteogenesis imperfecta
    • Sykes B, Francis MJO, Smith R (1977) Altered relation of two collagen types in osteogenesis imperfecta. Biochem Biophys Res Commun 296:1200-1203
    • (1977) Biochem Biophys Res Commun , vol.296 , pp. 1200-1203
    • Sykes, B.1    Francis, M.J.O.2    Smith, R.3
  • 19
    • 0021958346 scopus 로고
    • A method for quantitative analysis of ratio of types I and II collagen in small samples of articular cartilage
    • O'Driscoll SW, Salter RB, Keeley FW (1985) A method for quantitative analysis of ratio of types I and II collagen in small samples of articular cartilage. Analyt Biochem 145:277-285
    • (1985) Analyt Biochem , vol.145 , pp. 277-285
    • O'Driscoll, S.W.1    Salter, R.B.2    Keeley, F.W.3
  • 20
    • 0020010851 scopus 로고
    • Preparation and characterization of the different types of collagen
    • Miller EJ, Rhodes RK (1982) Preparation and characterization of the different types of collagen. Methods Enzymol 82:33-64
    • (1982) Methods Enzymol , vol.82 , pp. 33-64
    • Miller, E.J.1    Rhodes, R.K.2
  • 21
    • 0024046860 scopus 로고
    • UV spectroscopic characterization of type I collagen
    • Na GC (1988) UV spectroscopic characterization of type I collagen. Coll Rel Res 8:315-330
    • (1988) Coll Rel Res , vol.8 , pp. 315-330
    • Na, G.C.1
  • 22
    • 0015228786 scopus 로고
    • Molecular weight heterogeneity of the alpha-chain subunits of collagen
    • Sykes BC, Bailey AJ (1971) Molecular weight heterogeneity of the alpha-chain subunits of collagen. Biochem Biophys Res Commun 43:340-345
    • (1971) Biochem Biophys Res Commun , vol.43 , pp. 340-345
    • Sykes, B.C.1    Bailey, A.J.2
  • 23
    • 0015209390 scopus 로고
    • Isolation and characterization of the cyanogen bromide peptides from the α1(II) chain of chick cartilage collagen
    • Miller EJ (1971) Isolation and characterization of the cyanogen bromide peptides from the α1(II) chain of chick cartilage collagen. Biochemistry 10:3030-3035
    • (1971) Biochemistry , vol.10 , pp. 3030-3035
    • Miller, E.J.1
  • 24
    • 0020599036 scopus 로고
    • The presence of intermolecular disulfide cross-links in type III collagen
    • Cheung DT, DiCesare P, Benya PD, Libaw E, Nimni ME (1983) The presence of intermolecular disulfide cross-links in type III collagen. J Biol Chem 258:7774-7778
    • (1983) J Biol Chem , vol.258 , pp. 7774-7778
    • Cheung, D.T.1    Dicesare, P.2    Benya, P.D.3    Libaw, E.4    Nimni, M.E.5
  • 26
    • 0021330969 scopus 로고
    • Tendons and ligaments: A morphological and biochemical comparison
    • Amiel D, Frank CB, Harwood FL, Fronek J, Akeson WH (1984) Tendons and ligaments: a morphological and biochemical comparison. J Orthop Res 1(3):257-265
    • (1984) J Orthop Res , vol.1 , Issue.3 , pp. 257-265
    • Amiel, D.1    Frank, C.B.2    Harwood, F.L.3    Fronek, J.4    Akeson, W.H.5
  • 27
    • 0023075941 scopus 로고
    • Collagen cross-linking amino acids
    • Eyre DR (1987) Collagen cross-linking amino acids. Methods Enzymol 144:115-139
    • (1987) Methods Enzymol , vol.144 , pp. 115-139
    • Eyre, D.R.1
  • 29
    • 0017355018 scopus 로고
    • The progeny of rabbit articular chondrocytes synthesize collagen types I and III and type I trimer, but not type II: Verifications by cyanogen bromide peptide analysis
    • Benya PD, Padilla SR, Nimni ME (1977) The progeny of rabbit articular chondrocytes synthesize collagen types I and III and type I trimer, but not type II: verifications by cyanogen bromide peptide analysis. Biochemistry 16:865-872
    • (1977) Biochemistry , vol.16 , pp. 865-872
    • Benya, P.D.1    Padilla, S.R.2    Nimni, M.E.3
  • 30
    • 0020486206 scopus 로고
    • Estimation of types I and III collagens in whole tissue by quantitation of CNBr peptides on SDS-polyacrylamide gels
    • Light ND (1982) Estimation of types I and III collagens in whole tissue by quantitation of CNBr peptides on SDS-polyacrylamide gels. Biochim Biophys Acta 702:30-36
    • (1982) Biochim Biophys Acta , vol.702 , pp. 30-36
    • Light, N.D.1
  • 31
    • 0019796206 scopus 로고
    • A simplified method for quantitation of the relative amounts of type I and type III collagen in small tissue samples
    • Laurent GJ, Cockerill P, McAnulty RJ, Hastings JRB (1981) A simplified method for quantitation of the relative amounts of type I and type III collagen in small tissue samples. Analyt Biochem 113:301-312
    • (1981) Analyt Biochem , vol.113 , pp. 301-312
    • Laurent, G.J.1    Cockerill, P.2    McAnulty, R.J.3    Hastings, J.R.B.4
  • 32
    • 0020615381 scopus 로고
    • Quantitation of type I to type III collagen ratios in small samples of human tendon, blood vessels, and atherosclerotic plaque
    • Hanson AN, Bentley JP (1983) Quantitation of type I to type III collagen ratios in small samples of human tendon, blood vessels, and atherosclerotic plaque. Analyt Biochem 130:32-40
    • (1983) Analyt Biochem , vol.130 , pp. 32-40
    • Hanson, A.N.1    Bentley, J.P.2
  • 33
    • 0021227948 scopus 로고
    • Quantitation of types I and III collagens using electrophoresis of alpha chains and cyanogen bromide peptides
    • Chan D, Cole WG (1984) Quantitation of types I and III collagens using electrophoresis of alpha chains and cyanogen bromide peptides. Analyt Biochem 139:322-328
    • (1984) Analyt Biochem , vol.139 , pp. 322-328
    • Chan, D.1    Cole, W.G.2
  • 34
    • 0022250271 scopus 로고
    • Quantification and specific detection of collagenous proteins using an enzyme-linked immunosorbent assay and an immunoblotting for cyanogen bromide peptides
    • Bellon G (1985) Quantification and specific detection of collagenous proteins using an enzyme-linked immunosorbent assay and an immunoblotting for cyanogen bromide peptides. Analyt Biochem 150:188-202
    • (1985) Analyt Biochem , vol.150 , pp. 188-202
    • Bellon, G.1
  • 35
    • 0024266301 scopus 로고
    • Quantitative evaluation of collagen fractions separated by acrylamide gel electrophoresis: Its application for collagen typing in normal and pathological tissues
    • Bellon G, Borel JP (1988) Quantitative evaluation of collagen fractions separated by acrylamide gel electrophoresis: its application for collagen typing in normal and pathological tissues. J Chromatog 433:S1-94
    • (1988) J Chromatog , vol.433
    • Bellon, G.1    Borel, J.P.2
  • 37
    • 0017114645 scopus 로고
    • Production and specificity of antibodies against the aminoterminal region in type III collagen
    • Becker U, Nowack H, Gay S, Timpl R (1976) Production and specificity of antibodies against the aminoterminal region in type III collagen. Immunology 31:57-65
    • (1976) Immunology , vol.31 , pp. 57-65
    • Becker, U.1    Nowack, H.2    Gay, S.3    Timpl, R.4
  • 38
    • 0024727606 scopus 로고
    • Location of intergrin complex and extracellular matrix molecule at the chicken myotendinous junction
    • Swasdison S, Mayne R (1989) Location of intergrin complex and extracellular matrix molecule at the chicken myotendinous junction. Cell Tissue Res 257:537-543
    • (1989) Cell Tissue Res , vol.257 , pp. 537-543
    • Swasdison, S.1    Mayne, R.2
  • 39
    • 0019200199 scopus 로고
    • Synthesis of types I, III and AB2 collagen by chick tendon fibroblasts in vitro
    • Herrmann H, Dessau W, Fessier LI, Vor der mark K (1980) Synthesis of types I, III and AB2 collagen by chick tendon fibroblasts in vitro. Eur J Biochem 105:63-74
    • (1980) Eur J Biochem , vol.105 , pp. 63-74
    • Herrmann, H.1    Dessau, W.2    Fessier, L.I.3    Vor Der Mark, K.4
  • 40
    • 0020466668 scopus 로고
    • The biosynthesis of glycoproteins by cultured bovine tendon fibroblasts
    • Taylor CM, Qelbaum RS, Grant ME (1982) The biosynthesis of glycoproteins by cultured bovine tendon fibroblasts. Connect Tissue Res 10:319-331
    • (1982) Connect Tissue Res , vol.10 , pp. 319-331
    • Taylor, C.M.1    Qelbaum, R.S.2    Grant, M.E.3
  • 41
    • 0027355493 scopus 로고
    • Tendon collagens: Extracellular matrix composition in shear stress and tensile components of flexor tendons
    • Tsuzaki M, Yamauchi M, Banes AJ (1993) Tendon collagens: extracellular matrix composition in shear stress and tensile components of flexor tendons. Connect Tissue Res 29:141-152
    • (1993) Connect Tissue Res , vol.29 , pp. 141-152
    • Tsuzaki, M.1    Yamauchi, M.2    Banes, A.J.3
  • 42
    • 0027353094 scopus 로고
    • The post-translational chemistry and molecular packing of mineralizing tendon collagens
    • Yamauchi M, Katz EP (1993) The post-translational chemistry and molecular packing of mineralizing tendon collagens. Connect Tissue Res 29:81-98
    • (1993) Connect Tissue Res , vol.29 , pp. 81-98
    • Yamauchi, M.1    Katz, E.P.2
  • 43
    • 0026446483 scopus 로고
    • Correlation of structure and viscoelastic properties in the pericardia of four mammalian species
    • Naimark WA, Lee JM, Limeback H, Cheung DJ (1992) Correlation of structure and viscoelastic properties in the pericardia of four mammalian species. Am J Physiol 263:H1095-1106
    • (1992) Am J Physiol , vol.263
    • Naimark, W.A.1    Lee, J.M.2    Limeback, H.3    Cheung, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.