메뉴 건너뛰기




Volumn 40, Issue 5, 2007, Pages 1343-1351

The post-translational phenotype of collagen synthesized by SAOS-2 osteosarcoma cells

Author keywords

Bone; Lysyl hydroxylase; Osteosarcoma; Protein mass spectrometry; Pyridinoline; Type I collagen; Type V collagen

Indexed keywords

COLLAGEN; COLLAGEN TYPE 1; COLLAGEN TYPE 11; COLLAGEN TYPE 5; LYSINE; LYSYLHYDROXYLASE 1; OXYGENASE; PYRIDINOLINE; UNCLASSIFIED DRUG;

EID: 34047269957     PISSN: 87563282     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bone.2007.01.011     Document Type: Article
Times cited : (25)

References (60)
  • 1
    • 0000159679 scopus 로고    scopus 로고
    • Biochemical basis of collagen metabolites as bone turnover markers
    • Raisz L., Rodin G., and Bilezikian J.P. (Eds), Academic Press, London
    • Eyre D.R. Biochemical basis of collagen metabolites as bone turnover markers. In: Raisz L., Rodin G., and Bilezikian J.P. (Eds). Principles of bone biology (1996), Academic Press, London 43-152
    • (1996) Principles of bone biology , pp. 43-152
    • Eyre, D.R.1
  • 2
    • 33748854428 scopus 로고    scopus 로고
    • Collagen cross-links
    • Eyre D.R., and Wu J.J. Collagen cross-links. Top. Curr. Chem. 247 (2005) 207-229
    • (2005) Top. Curr. Chem. , vol.247 , pp. 207-229
    • Eyre, D.R.1    Wu, J.J.2
  • 3
    • 0023935232 scopus 로고
    • Collagen cross-linking in human bone and articular cartilage. Age-related changes in the content of mature hydroxypyridinium residues
    • Eyre D.R., Dickson I.R., and Van Ness K. Collagen cross-linking in human bone and articular cartilage. Age-related changes in the content of mature hydroxypyridinium residues. Biochem. J. 252 (1988) 495-500
    • (1988) Biochem. J. , vol.252 , pp. 495-500
    • Eyre, D.R.1    Dickson, I.R.2    Van Ness, K.3
  • 4
    • 0020010503 scopus 로고
    • Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes
    • Kivirikko K.I., and Myllyla R. Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes. Methods Enzymol. 82 Pt. A (1982) 245-304
    • (1982) Methods Enzymol. , vol.82 , Issue.PART A , pp. 245-304
    • Kivirikko, K.I.1    Myllyla, R.2
  • 5
    • 0026507897 scopus 로고
    • Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3-p36.2
    • Hautala T., Byers M.G., Eddy R.L., Shows T.B., Kivirikko K.I., and Myllyla R. Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3-p36.2. Genomics 13 (1992) 62-69
    • (1992) Genomics , vol.13 , pp. 62-69
    • Hautala, T.1    Byers, M.G.2    Eddy, R.L.3    Shows, T.B.4    Kivirikko, K.I.5    Myllyla, R.6
  • 6
    • 0030972003 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle
    • Valtavaara M., Papponen H., Pirttila A.M., Hiltunen K., Helander H., and Myllyla R. Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle. J. Biol. Chem. 272 (1997) 6831-6834
    • (1997) J. Biol. Chem. , vol.272 , pp. 6831-6834
    • Valtavaara, M.1    Papponen, H.2    Pirttila, A.M.3    Hiltunen, K.4    Helander, H.5    Myllyla, R.6
  • 7
    • 0032557436 scopus 로고    scopus 로고
    • Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3)
    • Valtavaara M., Szpirer C., Szpirer J., and Myllyla R. Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3). J. Biol. Chem. 273 (1998) 12881-12886
    • (1998) J. Biol. Chem. , vol.273 , pp. 12881-12886
    • Valtavaara, M.1    Szpirer, C.2    Szpirer, J.3    Myllyla, R.4
  • 9
    • 0032940558 scopus 로고    scopus 로고
    • Tissue specificity of a new splice form of the human lysyl hydroxylase 2 gene
    • Yeowell H.N., and Walker L.C. Tissue specificity of a new splice form of the human lysyl hydroxylase 2 gene. Matrix Biol. 18 (1999) 179-187
    • (1999) Matrix Biol. , vol.18 , pp. 179-187
    • Yeowell, H.N.1    Walker, L.C.2
  • 11
    • 33645049315 scopus 로고    scopus 로고
    • Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
    • Ruotsalainen H., Sipila L., Vapola M., Sormunen R., Salo A.M., Uitto L., et al. Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes. J. Cell Sci. 119 (2006) 625-635
    • (2006) J. Cell Sci. , vol.119 , pp. 625-635
    • Ruotsalainen, H.1    Sipila, L.2    Vapola, M.3    Sormunen, R.4    Salo, A.M.5    Uitto, L.6
  • 12
    • 0034680898 scopus 로고    scopus 로고
    • Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity
    • Heikkinen J., Risteli M., Wang C., Latvala J., Rossi M., Valtavaara M., et al. Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity. J. Biol. Chem. 275 (2000) 36158-36163
    • (2000) J. Biol. Chem. , vol.275 , pp. 36158-36163
    • Heikkinen, J.1    Risteli, M.2    Wang, C.3    Latvala, J.4    Rossi, M.5    Valtavaara, M.6
  • 13
    • 20944446258 scopus 로고    scopus 로고
    • A novel mutation in the lysyl hydroxylase 1 gene causes decreased lysyl hydroxylase activity in an Ehlers-Danlos VIA patient
    • Walker L.C., Overstreet M.A., Siddiqui A., De Paepe A., Ceylaner G., Malfait F., et al. A novel mutation in the lysyl hydroxylase 1 gene causes decreased lysyl hydroxylase activity in an Ehlers-Danlos VIA patient. J. Invest. Dermatol. 124 (2005) 914-918
    • (2005) J. Invest. Dermatol. , vol.124 , pp. 914-918
    • Walker, L.C.1    Overstreet, M.A.2    Siddiqui, A.3    De Paepe, A.4    Ceylaner, G.5    Malfait, F.6
  • 14
    • 0032813305 scopus 로고    scopus 로고
    • A patient with Ehlers-Danlos syndrome type VI is homozygous for a premature termination codon in exon 14 of the lysyl hydroxylase 1 gene
    • Walker L.C., Marini J.C., Grange D.K., Filie J., and Yeowell H.N. A patient with Ehlers-Danlos syndrome type VI is homozygous for a premature termination codon in exon 14 of the lysyl hydroxylase 1 gene. Mol. Genet. Metab. 67 (1999) 74-82
    • (1999) Mol. Genet. Metab. , vol.67 , pp. 74-82
    • Walker, L.C.1    Marini, J.C.2    Grange, D.K.3    Filie, J.4    Yeowell, H.N.5
  • 15
    • 0015407865 scopus 로고
    • Lysyl-protocollagen hydroxylase deficiency in fibroblasts from siblings with hydroxylysine-deficient collagen
    • Krane S.M., Pinnell S.R., and Erbe R.W. Lysyl-protocollagen hydroxylase deficiency in fibroblasts from siblings with hydroxylysine-deficient collagen. Proc. Natl. Acad. Sci. U. S. A. 69 (1972) 2899-2903
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 2899-2903
    • Krane, S.M.1    Pinnell, S.R.2    Erbe, R.W.3
  • 16
    • 0028841268 scopus 로고
    • Urinary pyridinoline cross-links in Ehlers-Danlos syndrome type VI
    • Steinmann B., Eyre D.R., and Shao P. Urinary pyridinoline cross-links in Ehlers-Danlos syndrome type VI. Am. J. Hum. Genet. 57 (1995) 1505-1508
    • (1995) Am. J. Hum. Genet. , vol.57 , pp. 1505-1508
    • Steinmann, B.1    Eyre, D.R.2    Shao, P.3
  • 17
    • 0036377858 scopus 로고    scopus 로고
    • The kyphoscoliotic type of Ehlers-Danlos syndrome (type VI): differential effects on the hydroxylation of lysine in collagens I and II revealed by analysis of cross-linked telopeptides from urine
    • Eyre D., Shao P., Weis M.A., and Steinmann B. The kyphoscoliotic type of Ehlers-Danlos syndrome (type VI): differential effects on the hydroxylation of lysine in collagens I and II revealed by analysis of cross-linked telopeptides from urine. Mol. Genet. Metab. 76 (2002) 211-216
    • (2002) Mol. Genet. Metab. , vol.76 , pp. 211-216
    • Eyre, D.1    Shao, P.2    Weis, M.A.3    Steinmann, B.4
  • 18
    • 0033514449 scopus 로고    scopus 로고
    • Defective collagen crosslinking in bone, but not in ligament or cartilage, in Bruck syndrome: indications for a bone-specific telopeptide lysyl hydroxylase on chromosome 17
    • Bank R.A., Robins S.P., Wijmenga C., Breslau-Siderius L.J., Bardoel A.F., van der Sluijs H.A., et al. Defective collagen crosslinking in bone, but not in ligament or cartilage, in Bruck syndrome: indications for a bone-specific telopeptide lysyl hydroxylase on chromosome 17. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 1054-1058
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 1054-1058
    • Bank, R.A.1    Robins, S.P.2    Wijmenga, C.3    Breslau-Siderius, L.J.4    Bardoel, A.F.5    van der Sluijs, H.A.6
  • 19
    • 0029987370 scopus 로고    scopus 로고
    • Molecular site specificity of pyridinoline and pyrrole cross-links in type I collagen of human bone
    • Hanson D.A., and Eyre D.R. Molecular site specificity of pyridinoline and pyrrole cross-links in type I collagen of human bone. J. Biol. Chem. 271 (1996) 26508-26516
    • (1996) J. Biol. Chem. , vol.271 , pp. 26508-26516
    • Hanson, D.A.1    Eyre, D.R.2
  • 20
    • 0026524229 scopus 로고
    • Lysyl hydroxylation in collagens from hyperplastic callus and embryonic bones
    • Lehmann H.W., Bodo M., Frohn C., Nerlich A., Rimek D., Notbohm H., et al. Lysyl hydroxylation in collagens from hyperplastic callus and embryonic bones. Biochem. J. 282 Pt. 2 (1992) 313-318
    • (1992) Biochem. J. , vol.282 , Issue.PART 2 , pp. 313-318
    • Lehmann, H.W.1    Bodo, M.2    Frohn, C.3    Nerlich, A.4    Rimek, D.5    Notbohm, H.6
  • 21
    • 0020419978 scopus 로고
    • Collagen polymorphism in extracellular matrix of human osteosarcoma
    • Shapiro F.D., and Eyre D.R. Collagen polymorphism in extracellular matrix of human osteosarcoma. J. Natl. Cancer Inst. 69 (1982) 1009-1016
    • (1982) J. Natl. Cancer Inst. , vol.69 , pp. 1009-1016
    • Shapiro, F.D.1    Eyre, D.R.2
  • 22
    • 0029092961 scopus 로고
    • Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias
    • Lehmann H.W., Wolf E., Roser K., Bodo M., Delling G., and Muller P.K. Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias. J. Cancer Res. Clin. Oncol. 121 (1995) 413-418
    • (1995) J. Cancer Res. Clin. Oncol. , vol.121 , pp. 413-418
    • Lehmann, H.W.1    Wolf, E.2    Roser, K.3    Bodo, M.4    Delling, G.5    Muller, P.K.6
  • 23
    • 0026681853 scopus 로고
    • Post-translational modifications in the collagen of human osteoporotic femoral head
    • Bailey A.J., Wotton S.F., Sims T.J., and Thompson P.W. Post-translational modifications in the collagen of human osteoporotic femoral head. Biochem. Biophys. Res. Commun. 185 (1992) 801-805
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 801-805
    • Bailey, A.J.1    Wotton, S.F.2    Sims, T.J.3    Thompson, P.W.4
  • 24
    • 0018863356 scopus 로고
    • Changes in tissue morphology and collagen composition during the repair of cortical bone in the adult chicken
    • Glimcher M.J., Shapiro F., Ellis R.D., and Eyre D.R. Changes in tissue morphology and collagen composition during the repair of cortical bone in the adult chicken. J. Bone Jt. Surg., Am. 62 (1980) 964-973
    • (1980) J. Bone Jt. Surg., Am. , vol.62 , pp. 964-973
    • Glimcher, M.J.1    Shapiro, F.2    Ellis, R.D.3    Eyre, D.R.4
  • 25
    • 0242329676 scopus 로고    scopus 로고
    • Differential enhancement of collagen crosslink excretion in cases of osteosarcoma and chondrosarcoma
    • Acil Y., Springer I., Behrens P., Ullrich K.P., Hedderich J., and Bruns J. Differential enhancement of collagen crosslink excretion in cases of osteosarcoma and chondrosarcoma. J. Cancer Res. Clin. Oncol. 129 (2003) 583-588
    • (2003) J. Cancer Res. Clin. Oncol. , vol.129 , pp. 583-588
    • Acil, Y.1    Springer, I.2    Behrens, P.3    Ullrich, K.P.4    Hedderich, J.5    Bruns, J.6
  • 27
    • 0023200410 scopus 로고
    • Characterization of a human osteosarcoma cell line (Saos-2) with osteoblastic properties
    • Rodan S.B., Imai Y., Thiede M.A., Wesolowski G., Thompson D., Bar-Shavit Z., et al. Characterization of a human osteosarcoma cell line (Saos-2) with osteoblastic properties. Cancer Res. 47 (1987) 4961-4966
    • (1987) Cancer Res. , vol.47 , pp. 4961-4966
    • Rodan, S.B.1    Imai, Y.2    Thiede, M.A.3    Wesolowski, G.4    Thompson, D.5    Bar-Shavit, Z.6
  • 28
    • 14944376718 scopus 로고    scopus 로고
    • Characterization of osteosarcoma cell lines MG-63, Saos-2 and U-2 OS in comparison to human osteoblasts
    • Pautke C., Schieker M., Tischer T., Kolk A., Neth P., Mutschler W., et al. Characterization of osteosarcoma cell lines MG-63, Saos-2 and U-2 OS in comparison to human osteoblasts. Anticancer Res. 24 (2004) 3743-3748
    • (2004) Anticancer Res. , vol.24 , pp. 3743-3748
    • Pautke, C.1    Schieker, M.2    Tischer, T.3    Kolk, A.4    Neth, P.5    Mutschler, W.6
  • 29
    • 0023358690 scopus 로고
    • Characterization of a human osteoblastic osteosarcoma cell line (SAOS-2) with high bone alkaline phosphatase activity
    • Murray E., Provvedini D., Curran D., Catherwood B., Sussman H., and Manolagas S. Characterization of a human osteoblastic osteosarcoma cell line (SAOS-2) with high bone alkaline phosphatase activity. J. Bone Miner. Res. 2 (1987) 231-238
    • (1987) J. Bone Miner. Res. , vol.2 , pp. 231-238
    • Murray, E.1    Provvedini, D.2    Curran, D.3    Catherwood, B.4    Sussman, H.5    Manolagas, S.6
  • 30
    • 0030671398 scopus 로고    scopus 로고
    • A new action of parathyroid hormone. receptor-mediated stimulation of extracellular acidification in human osteoblast-like SaOS-2 cells
    • Barrett M.G., Belinsky G.S., and Tashjian Jr. A.H. A new action of parathyroid hormone. receptor-mediated stimulation of extracellular acidification in human osteoblast-like SaOS-2 cells. J. Biol. Chem. 272 (1997) 26346-26353
    • (1997) J. Biol. Chem. , vol.272 , pp. 26346-26353
    • Barrett, M.G.1    Belinsky, G.S.2    Tashjian Jr., A.H.3
  • 31
    • 0025895597 scopus 로고
    • Skeletal alkaline phosphatase specific activity is an index of the osteoblastic phenotype in subpopulations of the human osteosarcoma cell line SAOS-2
    • Farley J.R., Hall S.L., Herring S., Tarbaux N.M., Matsuyama T., and Wergedal J.E. Skeletal alkaline phosphatase specific activity is an index of the osteoblastic phenotype in subpopulations of the human osteosarcoma cell line SAOS-2. Metabolism 40 (1991) 664-671
    • (1991) Metabolism , vol.40 , pp. 664-671
    • Farley, J.R.1    Hall, S.L.2    Herring, S.3    Tarbaux, N.M.4    Matsuyama, T.5    Wergedal, J.E.6
  • 33
    • 21844447346 scopus 로고    scopus 로고
    • Calcified matrix production by SAOS-2 cells inside a polyurethane porous scaffold, using a perfusion bioreactor
    • Fassina L., Visai L., Asti L., Benazzo F., Speziale P., Tanzi M.C., et al. Calcified matrix production by SAOS-2 cells inside a polyurethane porous scaffold, using a perfusion bioreactor. Tissue Eng. 11 (2005) 685-700
    • (2005) Tissue Eng. , vol.11 , pp. 685-700
    • Fassina, L.1    Visai, L.2    Asti, L.3    Benazzo, F.4    Speziale, P.5    Tanzi, M.C.6
  • 34
    • 0026521313 scopus 로고
    • Human osteosarcoma cells spontaneously release matrix-vesicle-like structures with the capacity to mineralize
    • Fedde K.N. Human osteosarcoma cells spontaneously release matrix-vesicle-like structures with the capacity to mineralize. Bone Miner. 17 (1992) 145-151
    • (1992) Bone Miner. , vol.17 , pp. 145-151
    • Fedde, K.N.1
  • 35
    • 0029119981 scopus 로고
    • Matrix deposition by a calcifying human osteogenic sarcoma cell line (SAOS-2)
    • McQuillan D.J., Richardson M.D., and Bateman J.F. Matrix deposition by a calcifying human osteogenic sarcoma cell line (SAOS-2). Bone 16 (1995) 415-426
    • (1995) Bone , vol.16 , pp. 415-426
    • McQuillan, D.J.1    Richardson, M.D.2    Bateman, J.F.3
  • 36
    • 1842690566 scopus 로고    scopus 로고
    • Cbfa1/RUNX2 directs specific expression of the sclerosteosis gene (SOST)
    • Sevetson B., Taylor S., and Pan Y. Cbfa1/RUNX2 directs specific expression of the sclerosteosis gene (SOST). J. Biol. Chem. 279 (2004) 13849-13858
    • (2004) J. Biol. Chem. , vol.279 , pp. 13849-13858
    • Sevetson, B.1    Taylor, S.2    Pan, Y.3
  • 38
    • 1942454714 scopus 로고    scopus 로고
    • Alendronate regulates cell invasion and MMP-2 secretion in human osteosarcoma cell lines
    • Cheng Y.Y., Huang L., Lee K.M., Li K., and Kumta S.M. Alendronate regulates cell invasion and MMP-2 secretion in human osteosarcoma cell lines. Pediatr. Blood Cancer 42 (2004) 410-415
    • (2004) Pediatr. Blood Cancer , vol.42 , pp. 410-415
    • Cheng, Y.Y.1    Huang, L.2    Lee, K.M.3    Li, K.4    Kumta, S.M.5
  • 39
    • 0030199395 scopus 로고    scopus 로고
    • Osteoinductive ability of confluent Saos-2 cell correlates with enhanced expression of bone morphogenetic proteins
    • Raval P., Hsu H.H., and Anderson H.C. Osteoinductive ability of confluent Saos-2 cell correlates with enhanced expression of bone morphogenetic proteins. J. Orthop. Res. 14 (1996) 605-610
    • (1996) J. Orthop. Res. , vol.14 , pp. 605-610
    • Raval, P.1    Hsu, H.H.2    Anderson, H.C.3
  • 40
    • 0030053633 scopus 로고    scopus 로고
    • Healing of a segmental defect in the rat femur with use of an extract from a cultured human osteosarcoma cell-line (Saos-2). A preliminary report
    • Hunt T.R., Schwappach J.R., and Anderson H.C. Healing of a segmental defect in the rat femur with use of an extract from a cultured human osteosarcoma cell-line (Saos-2). A preliminary report. J. Bone Jt. Surg., Am. 78 (1996) 41-48
    • (1996) J. Bone Jt. Surg., Am. , vol.78 , pp. 41-48
    • Hunt, T.R.1    Schwappach, J.R.2    Anderson, H.C.3
  • 41
    • 33646248065 scopus 로고    scopus 로고
    • Sp1 family of transcription factors regulates the human alpha2 (XI) collagen gene (COL11A2) in Saos-2 osteoblastic cells
    • Goto T., Matsui Y., Fernandes R.J., Hanson D.A., Kubo T., Yukata K., et al. Sp1 family of transcription factors regulates the human alpha2 (XI) collagen gene (COL11A2) in Saos-2 osteoblastic cells. J. Bone Miner. Res. 21 (2006) 661-673
    • (2006) J. Bone Miner. Res. , vol.21 , pp. 661-673
    • Goto, T.1    Matsui, Y.2    Fernandes, R.J.3    Hanson, D.A.4    Kubo, T.5    Yukata, K.6
  • 42
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 0028140546 scopus 로고
    • Phenotypic stability of bovine articular chondrocytes after long-term culture in alginate beads
    • Hauselmann H.J., Fernandes R.J., Mok S.S., Schmid T.M., Block J.A., Aydelotte M.B., et al. Phenotypic stability of bovine articular chondrocytes after long-term culture in alginate beads. J. Cell Sci. 107 Pt. 1 (1994) 17-27
    • (1994) J. Cell Sci. , vol.107 , Issue.PART 1 , pp. 17-27
    • Hauselmann, H.J.1    Fernandes, R.J.2    Mok, S.S.3    Schmid, T.M.4    Block, J.A.5    Aydelotte, M.B.6
  • 44
    • 0021191703 scopus 로고
    • Quantitation of hydroxypyridinium crosslinks in collagen by high-performance liquid chromatography
    • Eyre D.R., Koob T.J., and Van Ness K.P. Quantitation of hydroxypyridinium crosslinks in collagen by high-performance liquid chromatography. Anal. Biochem. 137 (1984) 380-388
    • (1984) Anal. Biochem. , vol.137 , pp. 380-388
    • Eyre, D.R.1    Koob, T.J.2    Van Ness, K.P.3
  • 45
    • 0042769370 scopus 로고    scopus 로고
    • Assembly of collagen types II, IX and XI into nascent hetero-fibrils by a rat chondrocyte cell line
    • Fernandes R.J., Schmid T.M., and Eyre D.R. Assembly of collagen types II, IX and XI into nascent hetero-fibrils by a rat chondrocyte cell line. Eur. J. Biochem. 270 (2003) 3243-3250
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3243-3250
    • Fernandes, R.J.1    Schmid, T.M.2    Eyre, D.R.3
  • 46
    • 70449218338 scopus 로고
    • Microdetermination of hydroxyproline with chloramine-T and p-dimethylaminobenzaldehyde
    • Stegemann H. Microdetermination of hydroxyproline with chloramine-T and p-dimethylaminobenzaldehyde. Hoppe-Seyler's Z. Physiol. Chem. 311 (1958) 41-45
    • (1958) Hoppe-Seyler's Z. Physiol. Chem. , vol.311 , pp. 41-45
    • Stegemann, H.1
  • 47
    • 0030743295 scopus 로고    scopus 로고
    • Incomplete processing of type II procollagen by a rat chondrosarcoma cell line
    • Fernandes R.J., Schmid T.M., Harkey M.A., and Eyre D.R. Incomplete processing of type II procollagen by a rat chondrosarcoma cell line. Eur. J. Biochem. 247 (1997) 620-624
    • (1997) Eur. J. Biochem. , vol.247 , pp. 620-624
    • Fernandes, R.J.1    Schmid, T.M.2    Harkey, M.A.3    Eyre, D.R.4
  • 49
    • 0033791689 scopus 로고    scopus 로고
    • Immortalized human adult articular chondrocytes maintain cartilage-specific phenotype and responses to interleukin-1beta
    • Robbins J.R., Thomas B., Tan L., Choy B., Arbiser J.L., Berenbaum F., et al. Immortalized human adult articular chondrocytes maintain cartilage-specific phenotype and responses to interleukin-1beta. Arthritis Rheum. 43 (2000) 2189-2201
    • (2000) Arthritis Rheum. , vol.43 , pp. 2189-2201
    • Robbins, J.R.1    Thomas, B.2    Tan, L.3    Choy, B.4    Arbiser, J.L.5    Berenbaum, F.6
  • 50
    • 0029825396 scopus 로고    scopus 로고
    • Quantification of aggrecan and link-protein mRNA in human articular cartilage of different ages by competitive reverse transcriptase-PCR
    • Bolton M.C., Dudhia J., and Bayliss M.T. Quantification of aggrecan and link-protein mRNA in human articular cartilage of different ages by competitive reverse transcriptase-PCR. Biochem. J. 319 Pt. 2 (1996) 489-498
    • (1996) Biochem. J. , vol.319 , Issue.PART 2 , pp. 489-498
    • Bolton, M.C.1    Dudhia, J.2    Bayliss, M.T.3
  • 51
    • 32244433195 scopus 로고    scopus 로고
    • Loss of one HuD allele on chromosome #1p selects for amplification of the N-myc proto-oncogene in human neuroblastoma cells
    • Grandinetti K.B., Spengler B.A., Priedler J.L., and Ross R.A. Loss of one HuD allele on chromosome #1p selects for amplification of the N-myc proto-oncogene in human neuroblastoma cells. Oncogene 25 (2006) 706-712
    • (2006) Oncogene , vol.25 , pp. 706-712
    • Grandinetti, K.B.1    Spengler, B.A.2    Priedler, J.L.3    Ross, R.A.4
  • 52
    • 0024561039 scopus 로고
    • Identification of the cartilage alpha 1(XI) chain in type V collagen from bovine bone
    • Niyibizi C., and Eyre D.R. Identification of the cartilage alpha 1(XI) chain in type V collagen from bovine bone. FEBS Lett. 242 (1989) 314-318
    • (1989) FEBS Lett. , vol.242 , pp. 314-318
    • Niyibizi, C.1    Eyre, D.R.2
  • 53
    • 0024809327 scopus 로고
    • Bone type V collagen: chain composition and location of a trypsin cleavage site
    • Niyibizi C., and Eyre D.R. Bone type V collagen: chain composition and location of a trypsin cleavage site. Connect. Tissue Res. 20 (1989) 247-250
    • (1989) Connect. Tissue Res. , vol.20 , pp. 247-250
    • Niyibizi, C.1    Eyre, D.R.2
  • 54
    • 0026071008 scopus 로고
    • Human bone contains type III collagen, type VI collagen, and fibrillin: type III collagen is present on specific fibers that may mediate attachment of tendons, ligaments, and periosteum to calcified bone cortex
    • Keene D.R., Sakai L.Y., and Burgeson R.E. Human bone contains type III collagen, type VI collagen, and fibrillin: type III collagen is present on specific fibers that may mediate attachment of tendons, ligaments, and periosteum to calcified bone cortex. J. Histochem. Cytochem. 39 (1991) 59-69
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 59-69
    • Keene, D.R.1    Sakai, L.Y.2    Burgeson, R.E.3
  • 55
    • 7144223393 scopus 로고    scopus 로고
    • Differential in situ expression of alpha2(XI) collagen mRNA isoforms in the developing mouse
    • Sugimoto M., Kimura T., Tsumaki N., Matsui Y., Nakata K., Kawahata H., et al. Differential in situ expression of alpha2(XI) collagen mRNA isoforms in the developing mouse. Cell Tissue Res. 292 (1998) 325-332
    • (1998) Cell Tissue Res. , vol.292 , pp. 325-332
    • Sugimoto, M.1    Kimura, T.2    Tsumaki, N.3    Matsui, Y.4    Nakata, K.5    Kawahata, H.6
  • 56
    • 0032570638 scopus 로고    scopus 로고
    • Splicing patterns of type XI collagen transcripts act as molecular markers for osteochondrogenic tumors
    • Matsui Y., Kimura T., Tsumaki N., Nakata K., Yasui N., Araki N., et al. Splicing patterns of type XI collagen transcripts act as molecular markers for osteochondrogenic tumors. Cancer Lett. 124 (1998) 143-148
    • (1998) Cancer Lett. , vol.124 , pp. 143-148
    • Matsui, Y.1    Kimura, T.2    Tsumaki, N.3    Nakata, K.4    Yasui, N.5    Araki, N.6
  • 57
    • 15444370111 scopus 로고    scopus 로고
    • Collagen overglycosylation: a biochemical feature that may contribute to bone quality
    • Dominguez L.J., Barbagallo M., and Moro L. Collagen overglycosylation: a biochemical feature that may contribute to bone quality. Biochem. Biophys. Res. Commun. 330 (2005) 1-4
    • (2005) Biochem. Biophys. Res. Commun. , vol.330 , pp. 1-4
    • Dominguez, L.J.1    Barbagallo, M.2    Moro, L.3
  • 60
    • 33747152561 scopus 로고    scopus 로고
    • Matrix elasticity directs stem cell lineage specification
    • Engler A.J., Sen S., Sweeny H.L., and Discher D.E. Matrix elasticity directs stem cell lineage specification. Cell 126 (2006) 677-689
    • (2006) Cell , vol.126 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeny, H.L.3    Discher, D.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.