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Volumn 17, Issue 3, 1998, Pages 169-184

Phenotypic and biochemical consequences of collagen X mutations in mice and humans

Author keywords

Chondrodysplasia; Collagen X; Hematopoiesis; Human; Hypertrophic cartilage; Mouse; Skeleton; Transgenic

Indexed keywords

COLLAGEN TYPE 10; MUTANT PROTEIN;

EID: 0031879246     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(98)90056-7     Document Type: Review
Times cited : (81)

References (80)
  • 1
    • 0027471504 scopus 로고
    • Characterization of the mouse type X collagen gene
    • Apte, S.S. and Olsen, B.R.: Characterization of the mouse type X collagen gene. Matrix 13: 165-179, 1993.
    • (1993) Matrix , vol.13 , pp. 165-179
    • Apte, S.S.1    Olsen, B.R.2
  • 3
    • 0021352121 scopus 로고
    • Abnormal type I collagen metabolism by cultured fibroblasts in lethal perinatal osteogenesis imperfecta
    • Bateman, J.F., Mascara, T., Chan, D. and Cole, W.G.: Abnormal type I collagen metabolism by cultured fibroblasts in lethal perinatal osteogenesis imperfecta. Biochem. J. 217: 103-115, 1984.
    • (1984) Biochem. J. , vol.217 , pp. 103-115
    • Bateman, J.F.1    Mascara, T.2    Chan, D.3    Cole, W.G.4
  • 4
    • 0029061409 scopus 로고
    • Mutations in three subdomains of the carboxyl-terminal region of collagen type X account for most of the Schmid metaphyseal dysplasias
    • Bonaventure, J., Chaminade, P. and Maroteaux, P.: Mutations in three subdomains of the carboxyl-terminal region of collagen type X account for most of the Schmid metaphyseal dysplasias. Hum. Genet. 96: 58-64, 1995.
    • (1995) Hum. Genet. , vol.96 , pp. 58-64
    • Bonaventure, J.1    Chaminade, P.2    Maroteaux, P.3
  • 5
    • 0026528501 scopus 로고
    • The fibrillar collagens, collagen VIII, collagen X and C1q complement proteins share a similar domain in their C-terminal non-collagenous regions
    • Brass, A., Kadler, K.E., Thomas, J.T., Grant, M.E. and Boot-Handford, R.P.: The fibrillar collagens, collagen VIII, collagen X and C1q complement proteins share a similar domain in their C-terminal non-collagenous regions. FEBS Lett. 303: 126-128, 1992.
    • (1992) FEBS Lett. , vol.303 , pp. 126-128
    • Brass, A.1    Kadler, K.E.2    Thomas, J.T.3    Grant, M.E.4    Boot-Handford, R.P.5
  • 6
    • 0025604727 scopus 로고
    • Cartilage begets bone versus endochondral myelopoiesis
    • Caplan, A.I.: Cartilage begets bone versus endochondral myelopoiesis. Clin. Orthop. Rel. Res. 261: 257-267, 1990.
    • (1990) Clin. Orthop. Rel. Res. , vol.261 , pp. 257-267
    • Caplan, A.I.1
  • 8
    • 0028965555 scopus 로고
    • 618 to Val mutation in the α1(X) NC1 domain resulting in Schmid metaphyseal chondrodysplasia
    • 618 to Val mutation in the α1(X) NC1 domain resulting in Schmid metaphyseal chondrodysplasia. J. Biol. Chem. 270: 4558-4562, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4558-4562
    • Chan, D.1    Cole, W.G.2    Rogers, J.G.3    Bateman, J.F.4
  • 9
    • 0029779729 scopus 로고    scopus 로고
    • Type X collagen NC1 mutations produced by site-directed mutagenesis prevent in vitro assembly
    • Chan, D., Weng, Y.M., Golub, S. and Bateman, J.F.: Type X collagen NC1 mutations produced by site-directed mutagenesis prevent in vitro assembly. Ann. N.Y. Acad. Sci. 785: 231-233, 1996a.
    • (1996) Ann. N.Y. Acad. Sci. , vol.785 , pp. 231-233
    • Chan, D.1    Weng, Y.M.2    Golub, S.3    Bateman, J.F.4
  • 10
    • 0000937043 scopus 로고    scopus 로고
    • A nonsense mutation in the carboxyl-terminal domain of the type X collagen causes haploinsufficiency in Schmid metaphyseal chondrodysplasia
    • in press
    • Chan, D., Weng, Y.M., Graham, H.K., Sillence, D.O. and Bateman, J.F.: A nonsense mutation in the carboxyl-terminal domain of the type X collagen causes haploinsufficiency in Schmid metaphyseal chondrodysplasia. J. Clin. Invest., in press, 1998.
    • (1998) J. Clin. Invest.
    • Chan, D.1    Weng, Y.M.2    Graham, H.K.3    Sillence, D.O.4    Bateman, J.F.5
  • 11
    • 0029946910 scopus 로고    scopus 로고
    • Site-directed mutagenesis of human type X collagen. Expression of α1(X) NC1, NC2, and helical mutations in vitro and in transfected cells
    • Chan, D., Weng, Y.M., Hocking, A.M., Golub, S., McQuillan, D.J. and Bateman, J.F.: Site-directed mutagenesis of human type X collagen. Expression of α1(X) NC1, NC2, and helical mutations in vitro and in transfected cells. J. Biol. Chem. 271: 13566-13572, 1996b.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13566-13572
    • Chan, D.1    Weng, Y.M.2    Hocking, A.M.3    Golub, S.4    McQuillan, D.J.5    Bateman, J.F.6
  • 13
    • 0026514474 scopus 로고
    • Domains of type X collagen: Alteration of cartilage matrix by fibril association and proteoglycan accumulation
    • Chen, Q.A., Linsenmayer, C., Gu, H., Schmid, T.M. and Linsenmayer, TE: Domains of type X collagen: alteration of cartilage matrix by fibril association and proteoglycan accumulation. J. Cell Biol. 137:687-694, 1992.
    • (1992) J. Cell Biol. , vol.137 , pp. 687-694
    • Chen, Q.A.1    Linsenmayer, C.2    Gu, H.3    Schmid, T.M.4    Linsenmayer, T.E.5
  • 14
    • 0027182875 scopus 로고
    • BiP binds type I procollagen pro α-chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta
    • Chessler, S.D. and Byers, P.H.: BiP binds type I procollagen pro α-chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta. J. Biol. Chem. 268: 18226-18233, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18226-18233
    • Chessler, S.D.1    Byers, P.H.2
  • 16
    • 0028265711 scopus 로고
    • Identification of a mutation in type X collagen in a family with Schmid metaphyseal chondrodysplasia
    • Dharmavaram, R.M., Elberson, M.A., Peng, M., Kirson, L.A., Kelley, T.E. and Jimenez, S.A.: Identification of a mutation in type X collagen in a family with Schmid metaphyseal chondrodysplasia. Hum. Mol. Genet. 3: 507-509, 1994.
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 507-509
    • Dharmavaram, R.M.1    Elberson, M.A.2    Peng, M.3    Kirson, L.A.4    Kelley, T.E.5    Jimenez, S.A.6
  • 17
    • 0022998819 scopus 로고
    • Folding of carboxyl domain and assembly of procollagen I
    • Doege, K.J. and Fessier, J.H.: Folding of carboxyl domain and assembly of procollagen I. J. Biol. Chem. 261: 8924-8935, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8924-8935
    • Doege, K.J.1    Fessier, J.H.2
  • 19
    • 0030460933 scopus 로고    scopus 로고
    • Mouse models of human genetic disease: Which mouse is more like a man?
    • Erickson, R.P.: Mouse models of human genetic disease: which mouse is more like a man? BioEssays 18: 993-998, 1996.
    • (1996) BioEssays , vol.18 , pp. 993-998
    • Erickson, R.P.1
  • 20
    • 0024361393 scopus 로고
    • Cellular turnover at the chondro-osseous junction of growth plate cartilage: Analysis by serial sections at the light microscope level
    • Farnum, C.E. and Wilsman, N.J.: Cellular turnover at the chondro-osseous junction of growth plate cartilage: analysis by serial sections at the light microscope level. J. Orthop. Res. 7: 654-666, 1989a.
    • (1989) J. Orthop. Res. , vol.7 , pp. 654-666
    • Farnum, C.E.1    Wilsman, N.J.2
  • 21
    • 0024457668 scopus 로고
    • Condensation of hypertrophic chondrocytes at the chondro-osseous junction of growth plate cartilage in yucutan swine: Relationship to long bone growth
    • Farnum, C.E. and Wilsman, N.J.: Condensation of hypertrophic chondrocytes at the chondro-osseous junction of growth plate cartilage in yucutan swine: relationship to long bone growth. Am. J. Anat. 186: 346-358, 1989b.
    • (1989) Am. J. Anat. , vol.186 , pp. 346-358
    • Farnum, C.E.1    Wilsman, N.J.2
  • 22
    • 0345210453 scopus 로고
    • Histochemical evidence of DNA fragmentation characteristic of apoptosis in hypertrophic chondrocytes
    • Farnum, C.E. and Wilsman, N.J.: Histochemical evidence of DNA fragmentation characteristic of apoptosis in hypertrophic chondrocytes. 41st Ann. Mtg. Orthop. Res. Soc. 77: 13, 1995.
    • (1995) 41st Ann. Mtg. Orthop. Res. Soc. , vol.77 , pp. 13
    • Farnum, C.E.1    Wilsman, N.J.2
  • 23
    • 0020265138 scopus 로고
    • Effects of matrix macromolecules on chondrocyte gene expression: Synthesis of a low molecular weight collagen species by cells cultured within collagen gels
    • Gibson, G.J., Schor, S.L. and Grant, M.E.: Effects of matrix macromolecules on chondrocyte gene expression: synthesis of a low molecular weight collagen species by cells cultured within collagen gels. J. Cell Biol. 93: 767-774, 1982.
    • (1982) J. Cell Biol. , vol.93 , pp. 767-774
    • Gibson, G.J.1    Schor, S.L.2    Grant, M.E.3
  • 24
    • 0023655428 scopus 로고
    • Type X collagen synthesis during endochondral ossification in fracture repair
    • Grant, W.T., Wang, G.J. and Balian, G.: Type X collagen synthesis during endochondral ossification in fracture repair. J. Biol. Chem. 262: 9844-9849, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9844-9849
    • Grant, W.T.1    Wang, G.J.2    Balian, G.3
  • 25
    • 0020441791 scopus 로고
    • Improved cartilage fixation by ruthenium hexamine trichloride (RHT). A prerequisite for morphometry in growth cartilage
    • Hunziker, E.B., Herrman, W. and Schenk, R.K.: Improved cartilage fixation by ruthenium hexamine trichloride (RHT). A prerequisite for morphometry in growth cartilage. J. Ultrastruct. Res. 81: 1-12, 1982.
    • (1982) J. Ultrastruct. Res. , vol.81 , pp. 1-12
    • Hunziker, E.B.1    Herrman, W.2    Schenk, R.K.3
  • 26
    • 0020604847 scopus 로고
    • Ruthenium hexamine trichloride (RHT)-mediated interaction between plasmalemmal components and pericellular matrix proteoglycans is responsible for the preservation of chondrocytic plasma membranes in situ during cartilage fixation
    • Hunziker, E.B., Herrmann, W. and Schenk, R.K.: Ruthenium hexamine trichloride (RHT)-mediated interaction between plasmalemmal components and pericellular matrix proteoglycans is responsible for the preservation of chondrocytic plasma membranes in situ during cartilage fixation. J. Histochem. Cytochem. 31: 717-727, 1984.
    • (1984) J. Histochem. Cytochem. , vol.31 , pp. 717-727
    • Hunziker, E.B.1    Herrmann, W.2    Schenk, R.K.3
  • 27
    • 0024399588 scopus 로고
    • Physiological mechanisms adopted by chondrocytes in regulating longitudinal bone growth in rats
    • Hunziker, E.B. and Schenk, R.K.: Physiological mechanisms adopted by chondrocytes in regulating longitudinal bone growth in rats. J. Physiol. 414: 55-71, 1989.
    • (1989) J. Physiol. , vol.414 , pp. 55-71
    • Hunziker, E.B.1    Schenk, R.K.2
  • 28
    • 13144256295 scopus 로고
    • Type X collagen does not bind to matrix vesicles
    • Inao, S. and Conrad, H.E.: Type X collagen does not bind to matrix vesicles. Hokkaido J. Med. Sci. 86: 214-23, 1993.
    • (1993) Hokkaido J. Med. Sci. , vol.86 , pp. 214-223
    • Inao, S.1    Conrad, H.E.2
  • 29
    • 0029785002 scopus 로고    scopus 로고
    • Skeletal and hematopoietic defects in mice transgenic for collagen X
    • Jacenko, O., Ito, S. and Olsen, B.R.: Skeletal and hematopoietic defects in mice transgenic for collagen X. Ann. N.Y. Acad. Sci. 785: 278-280, 1996.
    • (1996) Ann. N.Y. Acad. Sci. , vol.785 , pp. 278-280
    • Jacenko, O.1    Ito, S.2    Olsen, B.R.3
  • 30
    • 0027488970 scopus 로고
    • Spondylometaphyseal dysplasia in mice carrying a dominant negative mutation in a matrix protein specific for cartilage-to-bone transition
    • Jacenko, O., LuValle, P.A. and Olsen, B.R.: Spondylometaphyseal dysplasia in mice carrying a dominant negative mutation in a matrix protein specific for cartilage-to-bone transition. Nature 365: 56-61, 1993a.
    • (1993) Nature , vol.365 , pp. 56-61
    • Jacenko, O.1    LuValle, P.A.2    Olsen, B.R.3
  • 31
    • 0027727196 scopus 로고
    • A dominant negative mutation in the α1(X) collagen gene produces spondylometaphyseal defects in mice
    • Jacenko, O., LuValle, P., Solum, K. and Olsen, B.R.: A dominant negative mutation in the α1(X) collagen gene produces spondylometaphyseal defects in mice. Prog. Clin. Biol. Res. 383B: 427-436, 1993b.
    • (1993) Prog. Clin. Biol. Res. , vol.383 B , pp. 427-436
    • Jacenko, O.1    LuValle, P.2    Solum, K.3    Olsen, B.R.4
  • 33
    • 0028370499 scopus 로고
    • Of mice and men: Heritable skeletal disorders
    • Jacenko, O., Olsen, B.R. and Warman, M.L.: Of mice and men: heritable skeletal disorders. Am. J. Hum. Genet. 54: 163-168, 1994.
    • (1994) Am. J. Hum. Genet. , vol.54 , pp. 163-168
    • Jacenko, O.1    Olsen, B.R.2    Warman, M.L.3
  • 34
    • 0028047907 scopus 로고
    • Roles of the nucleational core complex and collagens (types II and X) in calcification of growth plate cartilage matrix vesicles
    • published erratum appears in J. Biol. Chem. 269: 25234, 1994
    • Kirsch, T., Ishikawa, Y., Mwale, F. and Wuthier, R.E.: Roles of the nucleational core complex and collagens (types II and X) in calcification of growth plate cartilage matrix vesicles [published erratum appears in J. Biol. Chem. 269: 25234, 1994]. J. Biol. Chem. 269: 20103-20109, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20103-20109
    • Kirsch, T.1    Ishikawa, Y.2    Mwale, F.3    Wuthier, R.E.4
  • 35
    • 0030952278 scopus 로고    scopus 로고
    • Annexin V-medicated calcium influx across membranes is dependent on the lipid composition: Implications for cartilage mineralization
    • Kirsch, T., Nah, H.D., Demuth, D.R., Harrison, G., Golub, E.E., Adams, S.L. and Pacifici, M.: Annexin V-medicated calcium influx across membranes is dependent on the lipid composition: implications for cartilage mineralization. Biochem. 36: 3359-3367, 1997b.
    • (1997) Biochem. , vol.36 , pp. 3359-3367
    • Kirsch, T.1    Nah, H.D.2    Demuth, D.R.3    Harrison, G.4    Golub, E.E.5    Adams, S.L.6    Pacifici, M.7
  • 36
    • 0030940202 scopus 로고    scopus 로고
    • Regulated production of mineralization-competent matrix vesicles in hypertrophic chondrocytes
    • Kirsch, T., Nah, H.D., Shapiro, I.M. and Pacifici, M.: Regulated production of mineralization-competent matrix vesicles in hypertrophic chondrocytes. J. Cell Biol. 137: 1149-60, 1997a.
    • (1997) J. Cell Biol. , vol.137 , pp. 1149-1160
    • Kirsch, T.1    Nah, H.D.2    Shapiro, I.M.3    Pacifici, M.4
  • 37
    • 0026414453 scopus 로고
    • 2+ binding properties of type X collagen
    • 2+ binding properties of type X collagen. FEBS Lett. 294: 149-152, 1991.
    • (1991) FEBS Lett. , vol.294 , pp. 149-152
    • Kirsch, T.1    Von Der Mark, K.2
  • 39
    • 0025826879 scopus 로고
    • Macromolecular organization of chicken type X collagen in vitro
    • Kwan, A.P.L., Cummings, C.E., Chapman, J.A. and Grant, M.E.: Macromolecular organization of chicken type X collagen in vitro. J. Cell Biol. 114: 597-604, 1991.
    • (1991) J. Cell Biol. , vol.114 , pp. 597-604
    • Kwan, A.P.L.1    Cummings, C.E.2    Chapman, J.A.3    Grant, M.E.4
  • 41
    • 0023881159 scopus 로고
    • Metaphyseal chondrodysplasia, Schmid type. Clinical and radiographic delineation with a review of the literature
    • Lachman, R.S., Rimoin, D.L. and Spranger, J.: Metaphyseal chondrodysplasia, Schmid type. Clinical and radiographic delineation with a review of the literature. Pediat. Radiol. 18: 93-102, 1988.
    • (1988) Pediat. Radiol. , vol.18 , pp. 93-102
    • Lachman, R.S.1    Rimoin, D.L.2    Spranger, J.3
  • 42
    • 0029021323 scopus 로고
    • The type I collagen pro-α1(I) COOH-terminal propeptide N-linked oligosaccharide. Functional analysis by site-directed mutagenesis
    • Lamande, S.R. and Bateman, J.E: The type I collagen pro-α1(I) COOH-terminal propeptide N-linked oligosaccharide. Functional analysis by site-directed mutagenesis. J. Biol. Chem. 270: 17858-17865, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17858-17865
    • Lamande, S.R.1    Bateman, J.E.2
  • 43
    • 0022773514 scopus 로고
    • Intracellular avian type X collagen in situ and determination of its thermal stability using a conformation dependent monoclonal antibody
    • Linsenmayer, T.F., Gibney, E. and Schmid, T.M.: Intracellular avian type X collagen in situ and determination of its thermal stability using a conformation dependent monoclonal antibody. Exp. Cell Res. 166: 15-20, 1986.
    • (1986) Exp. Cell Res. , vol.166 , pp. 15-20
    • Linsenmayer, T.F.1    Gibney, E.2    Schmid, T.M.3
  • 44
    • 0026621518 scopus 로고
    • Type X collagen is transcriptionally activated and specifically localized during sternal cartilage maturation
    • LuValle, P.A., Daniels, K., Hay, E.D. and Olsen, B.R.: Type X collagen is transcriptionally activated and specifically localized during sternal cartilage maturation. Matrix 12: 404-413, 1992.
    • (1992) Matrix , vol.12 , pp. 404-413
    • LuValle, P.A.1    Daniels, K.2    Hay, E.D.3    Olsen, B.R.4
  • 45
    • 0027312084 scopus 로고
    • Multiple negative elements in a gene that encodes for an extracellular matrix protein, collagen X, restrict expression to hypertrophic chondrocytes
    • LuValle, P., Iwamoto, M., Fanning, P., Pacifici, M. and Olsen, B.R.: Multiple negative elements in a gene that encodes for an extracellular matrix protein, collagen X, restrict expression to hypertrophic chondrocytes. J. Cell Biol. 121: 1173-1179, 1993a.
    • (1993) J. Cell Biol. , vol.121 , pp. 1173-1179
    • LuValle, P.1    Iwamoto, M.2    Fanning, P.3    Pacifici, M.4    Olsen, B.R.5
  • 46
    • 13144249766 scopus 로고
    • From cartilage to bone - The role of collagenous proteins
    • ed. by Bernfield, M., Wiley/Liss, New York
    • LuValle, P., Jacenko, O., Iwamoto, M., Pacifici, M. and Olsen, B.R.: From cartilage to bone - the role of collagenous proteins. In: Molecular Basis of Morphogenesis, ed. by Bernfield, M., Wiley/Liss, New York, 1993b, pp. 189-205.
    • (1993) Molecular Basis of Morphogenesis , pp. 189-205
    • LuValle, P.1    Jacenko, O.2    Iwamoto, M.3    Pacifici, M.4    Olsen, B.R.5
  • 47
    • 0024267226 scopus 로고
    • The type X collagen gene: Intron sequences split the 5'-untranslated region and separate the coding regions for the noncollagenous amino-terminal and triple-helical domains
    • LuValle, P.A., Ninomiya, Y., Rosenblum, N.D. and Olsen, B.R.: The type X collagen gene: Intron sequences split the 5'-untranslated region and separate the coding regions for the noncollagenous amino-terminal and triple-helical domains. J. Biol. Chem. 263: 18378-18385, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18378-18385
    • LuValle, P.A.1    Ninomiya, Y.2    Rosenblum, N.D.3    Olsen, B.R.4
  • 48
    • 0029330286 scopus 로고
    • When cells stop making sense: Effects of nonsense codons on RNA metabolism in vertebrate cells
    • Maquat, L.E.: When cells stop making sense: effects of nonsense codons on RNA metabolism in vertebrate cells. RNA 1: 453-465, 1995.
    • (1995) RNA , vol.1 , pp. 453-465
    • Maquat, L.E.1
  • 49
    • 0029906544 scopus 로고    scopus 로고
    • A recurrent 1992delCT mutation of the type X collagen gene in a Japanese patient with Schmid metaphyseal chondrodysplasia
    • Matsui, Y., Kimura, T., Tsumaki, N., Yasui, N. and Ochi, T.: A recurrent 1992delCT mutation of the type X collagen gene in a Japanese patient with Schmid metaphyseal chondrodysplasia. Jap. J. Hum. Genet. 41: 339-342, 1996.
    • (1996) Jap. J. Hum. Genet. , vol.41 , pp. 339-342
    • Matsui, Y.1    Kimura, T.2    Tsumaki, N.3    Yasui, N.4    Ochi, T.5
  • 50
    • 0028961999 scopus 로고
    • Concentration of mutations causing Schmid metaphyseal chondrodysplasia in the C-terminal noncollagenous domain of type X collagen
    • McIntosh, I., Abbott, M.H. and Francomano, C.A.: Concentration of mutations causing Schmid metaphyseal chondrodysplasia in the C-terminal noncollagenous domain of type X collagen. Hum. Mutation 5:121-125, 1995.
    • (1995) Hum. Mutation , vol.5 , pp. 121-125
    • McIntosh, I.1    Abbott, M.H.2    Francomano, C.A.3
  • 51
    • 0027976169 scopus 로고
    • Additional mutations of type X collagen confirm COL10A1 as the Schmid metaphyseal chondrodysplasia locus
    • McIntosh, I., Abbott, M.H., Warman, M.L., Olsen, B.R. and Francomano, C.A.: Additional mutations of type X collagen confirm COL10A1 as the Schmid metaphyseal chondrodysplasia locus. Hum. Molec. Genet. 3: 303-307, 1994.
    • (1994) Hum. Molec. Genet. , vol.3 , pp. 303-307
    • McIntosh, I.1    Abbott, M.H.2    Warman, M.L.3    Olsen, B.R.4    Francomano, C.A.5
  • 52
    • 0026605976 scopus 로고
    • Immunochemical and immunocytochemical identification of matrix vesicle proteins
    • Morris, D.C., Moylan, P.E. and Anderson, H.C.: Immunochemical and immunocytochemical identification of matrix vesicle proteins. Bone Miner. 17: 209-213, 1992.
    • (1992) Bone Miner. , vol.17 , pp. 209-213
    • Morris, D.C.1    Moylan, P.E.2    Anderson, H.C.3
  • 53
    • 0025887138 scopus 로고
    • The α2(VIII) collagen gene - A member of the short-chain family, located on chromosome 1
    • Muragaki, Y., Jacenko, O., Apte, S.A., Mattei, M.-G., Ninomiya, Y. and Olsen, B.R.: The α2(VIII) collagen gene - a member of the short-chain family, located on chromosome 1. J. Biol. Chem. 266: 7721-7727, 1992.
    • (1992) J. Biol. Chem. , vol.266 , pp. 7721-7727
    • Muragaki, Y.1    Jacenko, O.2    Apte, S.A.3    Mattei, M.-G.4    Ninomiya, Y.5    Olsen, B.R.6
  • 54
    • 0030005878 scopus 로고    scopus 로고
    • Type X collagen isolated from the hypertrophic cartilage of embryonic chick tibiae contains both hydroxylysyl- and lysylpyridinoline cross-links
    • Orth, M.W., Luchene, L.J. and Schmid, T.M.: Type X collagen isolated from the hypertrophic cartilage of embryonic chick tibiae contains both hydroxylysyl- and lysylpyridinoline cross-links. Biochem. Biophys. Res. Commun. 219: 301-305, 1996.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 301-305
    • Orth, M.W.1    Luchene, L.J.2    Schmid, T.M.3
  • 55
    • 0030220113 scopus 로고    scopus 로고
    • FT-IR microscopic analysis identifies alterations in mineral properties in bones from mice transgenic for collagen X
    • Paschalis, E.P., Jacenko, O., Olsen, B.R., Mendelsohn, R. and Boskey, A.L.: FT-IR microscopic analysis identifies alterations in mineral properties in bones from mice transgenic for collagen X. Bone 19: 151-156, 1996.
    • (1996) Bone , vol.19 , pp. 151-156
    • Paschalis, E.P.1    Jacenko, O.2    Olsen, B.R.3    Mendelsohn, R.4    Boskey, A.L.5
  • 56
    • 0029563235 scopus 로고
    • A novel mutation substituting tryptophan with arginine in the carboxyl-terminal, non-collagenous domain of collagen X in a case of Schmid metaphyseal chondrodysplasia
    • Pokharel, R.K., Alimsardjono, H., Uno, K., Fujii, S., Shiba, R. and Matsuo, M.: A novel mutation substituting tryptophan with arginine in the carboxyl-terminal, non-collagenous domain of collagen X in a case of Schmid metaphyseal chondrodysplasia. Biochem. Biophys. Res. Commun. 217: 1157-1162, 1995.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 1157-1162
    • Pokharel, R.K.1    Alimsardjono, H.2    Uno, K.3    Fujii, S.4    Shiba, R.5    Matsuo, M.6
  • 57
    • 0024451613 scopus 로고
    • Immunoelectron microscopic studies of type X collagen in endochondral ossification
    • Poole, A.R. and Pidoux, I.: Immunoelectron microscopic studies of type X collagen in endochondral ossification. J. Cell Biol. 309: 2547-2554, 1989.
    • (1989) J. Cell Biol. , vol.309 , pp. 2547-2554
    • Poole, A.R.1    Pidoux, I.2
  • 58
    • 0021638244 scopus 로고
    • Osteogenesis imperfecta: Phenotypic heterogeneity, protein suicide, short and long collagen
    • Prockop, D.J.: Osteogenesis imperfecta: phenotypic heterogeneity, protein suicide, short and long collagen. Am. J. Hum. Genet. 36: 499-505, 1984.
    • (1984) Am. J. Hum. Genet. , vol.36 , pp. 499-505
    • Prockop, D.J.1
  • 59
    • 0027744510 scopus 로고
    • Calcium deficiency and type X collagen synthesis in chick embryonic sterna
    • Reginato, A.M., Tuan, R.S., Ono, T., Jimenez, S. and Jacenko. O.: Calcium deficiency and type X collagen synthesis in chick embryonic sterna. Develop. Dynam. 198: 284-295, 1994.
    • (1994) Develop. Dynam. , vol.198 , pp. 284-295
    • Reginato, A.M.1    Tuan, R.S.2    Ono, T.3    Jimenez, S.4    Jacenko, O.5
  • 60
    • 0026323132 scopus 로고
    • In situ hybridization studies on the expression of type X collagen in fetal human cartilage
    • Reichenberger, E., Aigner, T., von der Mark, K., Stoss, H. and Bertling, W.: In situ hybridization studies on the expression of type X collagen in fetal human cartilage. Dev. Biol. 148: 562-572, 1991.
    • (1991) Dev. Biol. , vol.148 , pp. 562-572
    • Reichenberger, E.1    Aigner, T.2    Von Der Mark, K.3    Stoss, H.4    Bertling, W.5
  • 62
    • 0030199446 scopus 로고    scopus 로고
    • Identification of lysine-derived crosslinks in porcine collagen type X from growth plate and newly mineralized bone
    • Rucklidge, G.J., Milne, G. and Robins, S.P.: Identification of lysine-derived crosslinks in porcine collagen type X from growth plate and newly mineralized bone. Matrix Biol. 15: 73-80, 1996.
    • (1996) Matrix Biol. , vol.15 , pp. 73-80
    • Rucklidge, G.J.1    Milne, G.2    Robins, S.P.3
  • 63
    • 0025117435 scopus 로고
    • Characterization of the collagen in the hexagonal lattice of Descemet's membrane: Its relation to type VIII collagen
    • Sawada, H., Konomi, H. and Hirosawa, K.: Characterization of the collagen in the hexagonal lattice of Descemet's membrane: Its relation to type VIII collagen. J. Cell Biol. 110: 219-227, 1990.
    • (1990) J. Cell Biol. , vol.110 , pp. 219-227
    • Sawada, H.1    Konomi, H.2    Hirosawa, K.3
  • 64
    • 0025840204 scopus 로고
    • Late events in chondrocyte differentiation: Hypertrophy, type X collagen synthesis and matrix calcification
    • Schmid, T.M., Bonen, D.K., Luchene, L. and Linsenmayer, T.F.: Late events in chondrocyte differentiation: hypertrophy, type X collagen synthesis and matrix calcification. In Vivo, 5: 533-540, 1991.
    • (1991) In Vivo , vol.5 , pp. 533-540
    • Schmid, T.M.1    Bonen, D.K.2    Luchene, L.3    Linsenmayer, T.F.4
  • 65
    • 0020442640 scopus 로고
    • Metabolism of low molecular weight collagen by chondrocytes obtained from histologically distinct zones of the chick embryo tibiotarsus
    • Schmid, T.M. and Conrad, H.E.: Metabolism of low molecular weight collagen by chondrocytes obtained from histologically distinct zones of the chick embryo tibiotarsus. J. Biol. Chem. 257: 12451-12457, 1982a.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12451-12457
    • Schmid, T.M.1    Conrad, H.E.2
  • 66
    • 0020445377 scopus 로고
    • A unique low molecular weight collagen secreted by cultured chick embryo chondrocytes
    • Schmid, T.M. and Conrad, H.E.: A unique low molecular weight collagen secreted by cultured chick embryo chondrocytes. J. Biol. Chem. 257: 12444-12450, 1982b.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12444-12450
    • Schmid, T.M.1    Conrad, H.E.2
  • 67
    • 0025219168 scopus 로고
    • Immunoelectron microscopy of type X collagen: Supramolecular forms within embryonic chick cartilage
    • Schmid, T.M. and Linsenmayer, T.F.: Immunoelectron microscopy of type X collagen: supramolecular forms within embryonic chick cartilage. Dev. Biol. 138: 53-62, 1990.
    • (1990) Dev. Biol. , vol.138 , pp. 53-62
    • Schmid, T.M.1    Linsenmayer, T.F.2
  • 68
    • 0022982078 scopus 로고
    • Type X collagen contains two cleavage sites for a vertebrate collagenase
    • Schmid, T.M., Mayne, R., Jeffrey, J.J. and Linsenmayer, T.F.: Type X collagen contains two cleavage sites for a vertebrate collagenase. J. Biol. Chem. 261: 4184-4191, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4184-4191
    • Schmid, T.M.1    Mayne, R.2    Jeffrey, J.J.3    Linsenmayer, T.F.4
  • 69
    • 13144305641 scopus 로고
    • An achondroplastic mutation and the nature of its inheritance
    • Stevens, F.E.: An achondroplastic mutation and the nature of its inheritance. J. Hered. 34: 2229-2235, 1943.
    • (1943) J. Hered. , vol.34 , pp. 2229-2235
    • Stevens, F.E.1
  • 70
    • 0030462590 scopus 로고    scopus 로고
    • Dideoxyfingerprinting (DDF) analysis of the type X collagen gene (COL10A1) in a kindred with Schmid metaphyseal chondrodysplasia
    • Strataskis, C.A., Orban, Z., Burns, A.L., Vottero, A., Mitsiades, C.S., Marx, S.J., Abbassi, V. and Chrousos, G.P.: Dideoxyfingerprinting (DDF) analysis of the type X collagen gene (COL10A1) in a kindred with Schmid metaphyseal chondrodysplasia. Biochem. Mol. Med. 59: 112-117, 1996.
    • (1996) Biochem. Mol. Med. , vol.59 , pp. 112-117
    • Strataskis, C.A.1    Orban, Z.2    Burns, A.L.3    Vottero, A.4    Mitsiades, C.S.5    Marx, S.J.6    Abbassi, V.7    Chrousos, G.P.8
  • 72
    • 0001104936 scopus 로고
    • Here today, bone tomorrow
    • Wallis, G.: Here today, bone tomorrow, Curr. Biol. 3: 687-689, 1993.
    • (1993) Curr. Biol. , vol.3 , pp. 687-689
    • Wallis, G.1
  • 73
    • 0027958472 scopus 로고
    • Amino acid substitutions of conserved residues in the carboxyl-terminal domain of the α1(X) chain of type X collagen occur in two unrelated families with metaphyseal chondrodysplasia type Schmid
    • Wallis, G.A., Rash, B., Sweetman, W.A., Thomas, J.T., Super, M., Evans, G., Grant, M.E. and Boot-Handford, R.P.: Amino acid substitutions of conserved residues in the carboxyl-terminal domain of the α1(X) chain of type X collagen occur in two unrelated families with metaphyseal chondrodysplasia type Schmid. Am. J. Hum. Genet. 54: 169-178, 1994.
    • (1994) Am. J. Hum. Genet. , vol.54 , pp. 169-178
    • Wallis, G.A.1    Rash, B.2    Sweetman, W.A.3    Thomas, J.T.4    Super, M.5    Evans, G.6    Grant, M.E.7    Boot-Handford, R.P.8
  • 74
    • 0029952201 scopus 로고    scopus 로고
    • Mutation within the gene encoding the α1(X) chain of type X collagen (COL10A1) cause metaphyseal chondrodysplasia type Schmid but not several other forms of metaphyseal chondrodysplasia
    • Wallis, G.A., Rash, B., Sykes, B., Bonaventure, J., Maroteaux, P., Zabel, B., Wynnedavies, R., Grant, M.E. and Boot-Handford, R.P.: Mutation within the gene encoding the α1(X) chain of type X collagen (COL10A1) cause metaphyseal chondrodysplasia type Schmid but not several other forms of metaphyseal chondrodysplasia. J. Med. Genet. 33: 450-457, 1996.
    • (1996) J. Med. Genet. , vol.33 , pp. 450-457
    • Wallis, G.A.1    Rash, B.2    Sykes, B.3    Bonaventure, J.4    Maroteaux, P.5    Zabel, B.6    Wynnedavies, R.7    Grant, M.E.8    Boot-Handford, R.P.9
  • 77
    • 0025166680 scopus 로고
    • Differential susceptibility of type X collagen to cleavage by two mammalian interstitial collagenases and 72-kDa type IV collagenase
    • Welgus, H.G., Fliszar, C.J., Seltzer, J.L., Schmid, T.M. and Jeffrey, J.J.: 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.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13521-13527
    • Welgus, H.G.1    Fliszar, C.J.2    Seltzer, J.L.3    Schmid, T.M.4    Jeffrey, J.J.5
  • 78
    • 0025976194 scopus 로고
    • Collagen-binding proteins in collagenase-released matrix vesicles from cartilage. Interaction between matrix vesicle proteins and different types of collagen
    • Wu, L.N., Genge, B.R., Lloyd, G.G. and Wuthier, R.E.: Collagen-binding proteins in collagenase-released matrix vesicles from cartilage. Interaction between matrix vesicle proteins and different types of collagen. J. Biol. Chem. 266: 1195-1203, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1195-1203
    • Wu, L.N.1    Genge, B.R.2    Lloyd, G.G.3    Wuthier, R.E.4
  • 79
    • 0026507227 scopus 로고
    • Evidence for specific interaction between matrix vesicle proteins and the connective tissue matrix
    • Wu, L.N., Genge, B.R. and Wuthier, R.E.: Evidence for specific interaction between matrix vesicle proteins and the connective tissue matrix. Bone Miner. 17: 247-252, 1992.
    • (1992) Bone Miner. , vol.17 , pp. 247-252
    • Wu, L.N.1    Genge, B.R.2    Wuthier, R.E.3
  • 80
    • 0025911342 scopus 로고
    • The α1(VIII) collagen gene is homologous to the α1(X) gene and contains a large exon encoding the entire triple-helical and carboxyl-terminal non-triple-helical domains of the α1(VIII) polypeptide
    • Yamaguchi, N., Mayne, R. and Ninomiya, Y.: The α1(VIII) collagen gene is homologous to the α1(X) gene and contains a large exon encoding the entire triple-helical and carboxyl-terminal non-triple-helical domains of the α1(VIII) polypeptide. J. Biol. Chem. 266: 4508-4513, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4508-4513
    • Yamaguchi, N.1    Mayne, R.2    Ninomiya, Y.3


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