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Volumn 403, Issue 1-2, 2009, Pages 76-80

Different patterns of human serum procollagen C-proteinase enhancer1 (PCPE1)

Author keywords

Biochemical marker; Collagen type I; Glycopattern; Procollagen C proteinase enhancer1

Indexed keywords

BONE MORPHOGENETIC PROTEIN; OLIGOSACCHARIDE; PROCOLLAGEN C PROTEINASE; SIALIC ACID;

EID: 67349283546     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cca.2009.01.024     Document Type: Article
Times cited : (11)

References (29)
  • 1
    • 0022392606 scopus 로고
    • Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization
    • Hojima Y., van der Rest M., and Prockop D.J. Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization. J Biol Chem 260 (1985) 15996-16003
    • (1985) J Biol Chem , vol.260 , pp. 15996-16003
    • Hojima, Y.1    van der Rest, M.2    Prockop, D.J.3
  • 2
    • 0023656926 scopus 로고
    • Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process
    • Kadler K.E., Hojima Y., and Prockop D.J. Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process. J Biol Chem 262 (1987) 15696-15701
    • (1987) J Biol Chem , vol.262 , pp. 15696-15701
    • Kadler, K.E.1    Hojima, Y.2    Prockop, D.J.3
  • 3
  • 4
    • 33646567450 scopus 로고    scopus 로고
    • Developmental roles of the BMP1/TLD metalloproteinases
    • Ge G., and Greenspan D.S. Developmental roles of the BMP1/TLD metalloproteinases. Birth Defects Res C Embryo Today 78 (2006) 47-68
    • (2006) Birth Defects Res C Embryo Today , vol.78 , pp. 47-68
    • Ge, G.1    Greenspan, D.S.2
  • 5
    • 21244454923 scopus 로고    scopus 로고
    • Substrate-specific modulation of a multisubstrate proteinase. C-terminal processing of fibrillar procollagens is the only BMP-1-dependent activity to be enhanced by PCPE-1
    • Moali C., Font B., Ruggiero F., et al. Substrate-specific modulation of a multisubstrate proteinase. C-terminal processing of fibrillar procollagens is the only BMP-1-dependent activity to be enhanced by PCPE-1. J Biol Chem 280 (2005) 24188-24194
    • (2005) J Biol Chem , vol.280 , pp. 24188-24194
    • Moali, C.1    Font, B.2    Ruggiero, F.3
  • 6
    • 0027944145 scopus 로고
    • Type I procollagen COOH-terminal proteinase enhancer protein: identification, primary structure, and chromosomal localization of the cognate human gene (PCOLCE)
    • Takahara K., Kessler E., Biniaminov L., et al. Type I procollagen COOH-terminal proteinase enhancer protein: identification, primary structure, and chromosomal localization of the cognate human gene (PCOLCE). J Biol Chem 269 (1994) 26280-26285
    • (1994) J Biol Chem , vol.269 , pp. 26280-26285
    • Takahara, K.1    Kessler, E.2    Biniaminov, L.3
  • 7
    • 0038168257 scopus 로고    scopus 로고
    • NMR structure of the netrin-like domain (NTR) of human type I procollagen C-proteinase enhancer defines structural consensus of NTR domains and assesses potential proteinase inhibitory activity and ligand binding
    • Liepinsh E., Banyai L., Pintacuda G., Trexler M., Patthy L., and Otting G. NMR structure of the netrin-like domain (NTR) of human type I procollagen C-proteinase enhancer defines structural consensus of NTR domains and assesses potential proteinase inhibitory activity and ligand binding. J Biol Chem 278 (2003) 25982-25989
    • (2003) J Biol Chem , vol.278 , pp. 25982-25989
    • Liepinsh, E.1    Banyai, L.2    Pintacuda, G.3    Trexler, M.4    Patthy, L.5    Otting, G.6
  • 8
    • 0033955104 scopus 로고    scopus 로고
    • Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor
    • Mott J.D., Thomas C.L., Rosenbach M.T., Takahara K., Greenspan D.S., and Banda M.J. Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor. J Biol Chem 275 (2000) 1384-1390
    • (2000) J Biol Chem , vol.275 , pp. 1384-1390
    • Mott, J.D.1    Thomas, C.L.2    Rosenbach, M.T.3    Takahara, K.4    Greenspan, D.S.5    Banda, M.J.6
  • 9
    • 0035174117 scopus 로고    scopus 로고
    • Yeast PalA/AIP1/Alix homolog Rim20p associates with a PEST-like region and is required for its proteolytic cleavage
    • Xu W., and Mitchell A.P. Yeast PalA/AIP1/Alix homolog Rim20p associates with a PEST-like region and is required for its proteolytic cleavage. J Bacteriol 183 (2001) 6917-6923
    • (2001) J Bacteriol , vol.183 , pp. 6917-6923
    • Xu, W.1    Mitchell, A.P.2
  • 10
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M., and Rogers S.W. PEST sequences and regulation by proteolysis. Trends Biochem Sci 21 (1996) 267-271
    • (1996) Trends Biochem Sci , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 11
    • 0347298758 scopus 로고    scopus 로고
    • PCOLCE2 encodes a functional procollagen C-proteinase enhancer (PCPE2) that is a collagen-binding protein differing in distribution of expression and post-translational modification from the previously described PCPE1
    • Steiglitz B.M., Keene D.R., and Greenspan D.S. PCOLCE2 encodes a functional procollagen C-proteinase enhancer (PCPE2) that is a collagen-binding protein differing in distribution of expression and post-translational modification from the previously described PCPE1. J Biol Chem 277 (2002) 49820-49830
    • (2002) J Biol Chem , vol.277 , pp. 49820-49830
    • Steiglitz, B.M.1    Keene, D.R.2    Greenspan, D.S.3
  • 12
    • 35348923714 scopus 로고    scopus 로고
    • The bone morphogenetic protein 1/Tolloid-like metalloproteinases
    • Hopkins D.R., Keles S., and Greenspan D.S. The bone morphogenetic protein 1/Tolloid-like metalloproteinases. Matrix Biol 26 (2007) 508-523
    • (2007) Matrix Biol , vol.26 , pp. 508-523
    • Hopkins, D.R.1    Keles, S.2    Greenspan, D.S.3
  • 13
    • 12444339443 scopus 로고    scopus 로고
    • The human serum proteome: display of nearly 3700 chromatographically separated protein spots on two-dimensional electrophoresis gels and identification of 325 distinct proteins
    • Pieper R., Gatlin C.L., Makusky A.J., et al. The human serum proteome: display of nearly 3700 chromatographically separated protein spots on two-dimensional electrophoresis gels and identification of 325 distinct proteins. Proteomics 3 (2003) 1345-1364
    • (2003) Proteomics , vol.3 , pp. 1345-1364
    • Pieper, R.1    Gatlin, C.L.2    Makusky, A.J.3
  • 14
    • 36348933941 scopus 로고    scopus 로고
    • Detection of bone and cartilage-related proteins in plasma of patients with a bone fracture using liquid chromatography-mass spectrometry
    • Grgurevic L., Macek B., Durdevic D., and Vukicevic S. Detection of bone and cartilage-related proteins in plasma of patients with a bone fracture using liquid chromatography-mass spectrometry. Int Orthop 31 (2007) 743-751
    • (2007) Int Orthop , vol.31 , pp. 743-751
    • Grgurevic, L.1    Macek, B.2    Durdevic, D.3    Vukicevic, S.4
  • 15
    • 33947192955 scopus 로고    scopus 로고
    • Comparison of the methods for profiling glycoprotein glycans-HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study
    • Wada Y., Azadi P., Costello C.E., et al. Comparison of the methods for profiling glycoprotein glycans-HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study. Glycobiology 17 (2007) 411-422
    • (2007) Glycobiology , vol.17 , pp. 411-422
    • Wada, Y.1    Azadi, P.2    Costello, C.E.3
  • 16
    • 0030561580 scopus 로고    scopus 로고
    • Isoelectric focusing (IEF) and immunofixation for determination of disialotransferrin
    • Dumon M.F., Nau A., Hervouet M., Paccalin J., and Clerc M. Isoelectric focusing (IEF) and immunofixation for determination of disialotransferrin. Clin Biochem 29 (1996) 549-553
    • (1996) Clin Biochem , vol.29 , pp. 549-553
    • Dumon, M.F.1    Nau, A.2    Hervouet, M.3    Paccalin, J.4    Clerc, M.5
  • 17
    • 0034131162 scopus 로고    scopus 로고
    • Protein glycosylation and diseases: blood and urinary oligosaccharides as markers for diagnosis and therapeutic monitoring
    • Durand G., and Seta N. Protein glycosylation and diseases: blood and urinary oligosaccharides as markers for diagnosis and therapeutic monitoring. Clin Chem 46 (2000) 795-805
    • (2000) Clin Chem , vol.46 , pp. 795-805
    • Durand, G.1    Seta, N.2
  • 18
    • 0022743324 scopus 로고
    • Evidence for a protein that enhances the activity of type I procollagen C-proteinase
    • Adar R., Kessler E., and Goldberg B. Evidence for a protein that enhances the activity of type I procollagen C-proteinase. Coll Relat Res 6 (1986) 267-277
    • (1986) Coll Relat Res , vol.6 , pp. 267-277
    • Adar, R.1    Kessler, E.2    Goldberg, B.3
  • 19
    • 48149090000 scopus 로고    scopus 로고
    • Sialic acids in human health and disease
    • Varki A. Sialic acids in human health and disease. Trends Mol Med 14 (2008) 351-360
    • (2008) Trends Mol Med , vol.14 , pp. 351-360
    • Varki, A.1
  • 20
    • 0023864448 scopus 로고
    • Collagen expression, ultrastructural assembly, and mineralization in cultures of chicken embryo osteoblasts
    • Gerstenfeld L.C., Chipman S.D., Kelly C.M., Hodgens K.J., Lee D.D., and Landis W.J. Collagen expression, ultrastructural assembly, and mineralization in cultures of chicken embryo osteoblasts. J Cell Biol 106 (1988) 979-989
    • (1988) J Cell Biol , vol.106 , pp. 979-989
    • Gerstenfeld, L.C.1    Chipman, S.D.2    Kelly, C.M.3    Hodgens, K.J.4    Lee, D.D.5    Landis, W.J.6
  • 21
    • 33646827389 scopus 로고    scopus 로고
    • Biochemical markers of bone turnover: part I: biochemistry and variability
    • Seibel M.J. Biochemical markers of bone turnover: part I: biochemistry and variability. Clin Biochem Rev 26 (2005) 97-122
    • (2005) Clin Biochem Rev , vol.26 , pp. 97-122
    • Seibel, M.J.1
  • 22
    • 0036675220 scopus 로고    scopus 로고
    • Metastasis to bone: causes, consequences and therapeutic opportunities
    • Mundy G.R. Metastasis to bone: causes, consequences and therapeutic opportunities. Nat Rev Cancer 2 (2002) 584-593
    • (2002) Nat Rev Cancer , vol.2 , pp. 584-593
    • Mundy, G.R.1
  • 23
    • 0034326253 scopus 로고    scopus 로고
    • Bisphosphonates directly regulate cell proliferation, differentiation, and gene expression in human osteoblasts
    • Reinholz G.G., Getz B., Pederson L., et al. Bisphosphonates directly regulate cell proliferation, differentiation, and gene expression in human osteoblasts. Cancer Res 60 (2000) 6001-6007
    • (2000) Cancer Res , vol.60 , pp. 6001-6007
    • Reinholz, G.G.1    Getz, B.2    Pederson, L.3
  • 25
    • 33847633816 scopus 로고    scopus 로고
    • Analysis of human bone alkaline phosphatase isoforms: comparison of isoelectric focusing and ion-exchange high-performance liquid chromatography
    • Sharp C.A., Linder C., and Magnusson P. Analysis of human bone alkaline phosphatase isoforms: comparison of isoelectric focusing and ion-exchange high-performance liquid chromatography. Clin Chim Acta 379 (2007) 105-112
    • (2007) Clin Chim Acta , vol.379 , pp. 105-112
    • Sharp, C.A.1    Linder, C.2    Magnusson, P.3
  • 26
    • 0036667839 scopus 로고    scopus 로고
    • Serum sialic acid as a marker of alcohol consumption: effect of liver disease and heavy drinking
    • Romppanen J., Punnonen K., Anttila P., Jakobsson T., Blake J., and Niemela O. Serum sialic acid as a marker of alcohol consumption: effect of liver disease and heavy drinking. Alcohol Clin Exp Res 26 (2002) 1234-1238
    • (2002) Alcohol Clin Exp Res , vol.26 , pp. 1234-1238
    • Romppanen, J.1    Punnonen, K.2    Anttila, P.3    Jakobsson, T.4    Blake, J.5    Niemela, O.6
  • 27
    • 25844442417 scopus 로고    scopus 로고
    • Altered glycan structures: the molecular basis of congenital disorders of glycosylation
    • Freeze H.H., and Aebi M. Altered glycan structures: the molecular basis of congenital disorders of glycosylation. Curr Opin Struct Biol 15 (2005) 490-498
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 490-498
    • Freeze, H.H.1    Aebi, M.2
  • 28
    • 33745203732 scopus 로고    scopus 로고
    • Pediatric reference intervals for bone markers
    • Yang L., and Grey V. Pediatric reference intervals for bone markers. Clin Biochem 39 (2006) 561-568
    • (2006) Clin Biochem , vol.39 , pp. 561-568
    • Yang, L.1    Grey, V.2
  • 29
    • 33751227483 scopus 로고    scopus 로고
    • Clinical application of biochemical markers of bone turnover
    • Seibel M.J. Clinical application of biochemical markers of bone turnover. Arq Bras Endocrinol Metabol 50 (2006) 603-620
    • (2006) Arq Bras Endocrinol Metabol , vol.50 , pp. 603-620
    • Seibel, M.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.