메뉴 건너뛰기




Volumn 11, Issue 12, 2012, Pages 5890-5902

Proteomic profiling of breast tissue collagens and site-specific characterization of hydroxyproline residues of collagen alpha-1-(I)

Author keywords

breast cancer; collagen; hydroxyproline; iTRAQ; post translational modification

Indexed keywords

COLLAGEN; COLLAGEN ALPHA 3; COLLAGEN ALPHA 4; COLLAGEN ALPHA1 CHAIN; COLLAGEN ALPHA2 CHAIN; HYDROXYPROLINE; PROLINE; UNCLASSIFIED DRUG;

EID: 84870937402     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr300656r     Document Type: Article
Times cited : (24)

References (49)
  • 1
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases, and potentials for therapy
    • Prockop, D. J.; Kivirikko, K. I. Collagens: molecular biology, diseases, and potentials for therapy Annu. Rev. Biochem. 1995, 64, 403-34
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 2
    • 79851488199 scopus 로고    scopus 로고
    • Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up
    • Gautieri, A.; Vesentini, S.; Redaelli, A.; Buehler, M. J. Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up Nano Lett. 2011, 11 (2) 757-66
    • (2011) Nano Lett. , vol.11 , Issue.2 , pp. 757-766
    • Gautieri, A.1    Vesentini, S.2    Redaelli, A.3    Buehler, M.J.4
  • 3
    • 33745284997 scopus 로고    scopus 로고
    • Natural polymers for gene delivery and tissue engineering
    • Dang, J. M.; Leong, K. W. Natural polymers for gene delivery and tissue engineering Adv. Drug Delivery Rev. 2006, 58 (4) 487-99
    • (2006) Adv. Drug Delivery Rev. , vol.58 , Issue.4 , pp. 487-499
    • Dang, J.M.1    Leong, K.W.2
  • 4
    • 47749121495 scopus 로고    scopus 로고
    • Collagen scaffolds for tissue engineering
    • Glowacki, J.; Mizuno, S. Collagen scaffolds for tissue engineering Biopolymers 2008, 89 (5) 338-44
    • (2008) Biopolymers , vol.89 , Issue.5 , pp. 338-344
    • Glowacki, J.1    Mizuno, S.2
  • 5
    • 0346158554 scopus 로고    scopus 로고
    • Bone protects proteins over thousands of years: Extraction, analysis, and interpretation of extracellular matrix proteins in archeological skeletal remains
    • Schmidt-Schultz, T. H.; Schultz, M. Bone protects proteins over thousands of years: extraction, analysis, and interpretation of extracellular matrix proteins in archeological skeletal remains Am. J. Phys. Anthropol. 2004, 123 (1) 30-9
    • (2004) Am. J. Phys. Anthropol. , vol.123 , Issue.1 , pp. 30-39
    • Schmidt-Schultz, T.H.1    Schultz, M.2
  • 6
    • 83655164801 scopus 로고    scopus 로고
    • Identification of animal glue species in artworks using proteomics: Application to a 18th century gilt sample
    • Dallongeville, S.; Koperska, M.; Garnier, N.; Reille-Taillefert, G.; Rolando, C.; Tokarski, C. Identification of animal glue species in artworks using proteomics: application to a 18th century gilt sample Anal. Chem. 2011, 83 (24) 9431-7
    • (2011) Anal. Chem. , vol.83 , Issue.24 , pp. 9431-9437
    • Dallongeville, S.1    Koperska, M.2    Garnier, N.3    Reille-Taillefert, G.4    Rolando, C.5    Tokarski, C.6
  • 7
    • 71949102106 scopus 로고    scopus 로고
    • Species identification by analysis of bone collagen using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry
    • Buckley, M.; Collins, M.; Thomas-Oates, J.; Wilson, J. C. Species identification by analysis of bone collagen using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry Rapid Commun. Mass Spectrom. 2009, 23 (23) 3843-54
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , Issue.23 , pp. 3843-3854
    • Buckley, M.1    Collins, M.2    Thomas-Oates, J.3    Wilson, J.C.4
  • 9
    • 34247323509 scopus 로고    scopus 로고
    • Analyses of soft tissue from Tyrannosaurus rex suggest the presence of protein
    • Schweitzer, M. H.; Suo, Z.; Avci, R.; Asara, J. M.; Allen, M. A.; Arce, F. T.; Horner, J. R. Analyses of soft tissue from Tyrannosaurus rex suggest the presence of protein Science 2007, 316 (5822) 277-80
    • (2007) Science , vol.316 , Issue.5822 , pp. 277-280
    • Schweitzer, M.H.1    Suo, Z.2    Avci, R.3    Asara, J.M.4    Allen, M.A.5    Arce, F.T.6    Horner, J.R.7
  • 11
    • 70349925705 scopus 로고    scopus 로고
    • Reanalysis of Tyrannosaurus rex mass spectra
    • Bern, M.; Phinney, B. S.; Goldberg, D. Reanalysis of Tyrannosaurus rex mass spectra J. Proteome Res. 2009, 8 (9) 4328-32
    • (2009) J. Proteome Res. , vol.8 , Issue.9 , pp. 4328-4332
    • Bern, M.1    Phinney, B.S.2    Goldberg, D.3
  • 15
    • 50849135194 scopus 로고    scopus 로고
    • The urinary proteome in diabetes and diabetes-associated complications: New ways to assess disease progression and evaluate therapy
    • Rossing, K.; Mischak, H.; Rossing, P.; Schanstra, J. P.; Wiseman, A.; Maahs, D. M. The urinary proteome in diabetes and diabetes-associated complications: New ways to assess disease progression and evaluate therapy Proteomics Clin. Appl. 2008, 2 (7-8) 997-1007
    • (2008) Proteomics Clin. Appl. , vol.2 , Issue.7-8 , pp. 997-1007
    • Rossing, K.1    Mischak, H.2    Rossing, P.3    Schanstra, J.P.4    Wiseman, A.5    Maahs, D.M.6
  • 17
    • 67449143228 scopus 로고    scopus 로고
    • Identification of a unique urinary biomarker profile in patients with autosomal dominant polycystic kidney disease
    • Kistler, A. D.; Mischak, H.; Poster, D.; Dakna, M.; Wuthrich, R. P.; Serra, A. L. Identification of a unique urinary biomarker profile in patients with autosomal dominant polycystic kidney disease Kidney Int. 2009, 76 (1) 89-96
    • (2009) Kidney Int. , vol.76 , Issue.1 , pp. 89-96
    • Kistler, A.D.1    Mischak, H.2    Poster, D.3    Dakna, M.4    Wuthrich, R.P.5    Serra, A.L.6
  • 21
    • 80051721110 scopus 로고    scopus 로고
    • Urinary peptides as a diagnostic tool for renal failure detected by matrix-assisted laser desorption/ionisation mass spectrometry: An evaluation of their clinical significance
    • Lapolla, A.; Molin, L.; Seraglia, R.; Sechi, A.; Cosma, C.; Bonfante, L.; Chilelli, N. C.; Ragazzi, E.; Traldi, P. Urinary peptides as a diagnostic tool for renal failure detected by matrix-assisted laser desorption/ionisation mass spectrometry: an evaluation of their clinical significance Eur. J. Mass Spectrom. 2011, 17 (3) 245-53
    • (2011) Eur. J. Mass Spectrom. , vol.17 , Issue.3 , pp. 245-253
    • Lapolla, A.1    Molin, L.2    Seraglia, R.3    Sechi, A.4    Cosma, C.5    Bonfante, L.6    Chilelli, N.C.7    Ragazzi, E.8    Traldi, P.9
  • 22
    • 80054044048 scopus 로고    scopus 로고
    • Integrated proteomic profiling of cell line conditioned media and pancreatic juice for the identification of pancreatic cancer biomarkers
    • 008599
    • Makawita, S.; Smith, C.; Batruch, I.; Zheng, Y.; Ruckert, F.; Grutzmann, R.; Pilarsky, C.; Gallinger, S.; Diamandis, E. P. Integrated proteomic profiling of cell line conditioned media and pancreatic juice for the identification of pancreatic cancer biomarkers Mol. Cell. Proteomics 2011, 10 (10) M111 008599
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.10 , pp. 111
    • Makawita, S.1    Smith, C.2    Batruch, I.3    Zheng, Y.4    Ruckert, F.5    Grutzmann, R.6    Pilarsky, C.7    Gallinger, S.8    Diamandis, E.P.9
  • 23
    • 10344258050 scopus 로고    scopus 로고
    • The contribution of vascular basement membranes and extracellular matrix to the mechanics of tumor angiogenesis
    • Sund, M.; Xie, L.; Kalluri, R. The contribution of vascular basement membranes and extracellular matrix to the mechanics of tumor angiogenesis Apmis 2004, 112 (7-8) 450-62
    • (2004) Apmis , vol.112 , Issue.7-8 , pp. 450-462
    • Sund, M.1    Xie, L.2    Kalluri, R.3
  • 26
    • 0034307327 scopus 로고    scopus 로고
    • Endostatin inhibits endothelial and tumor cellular invasion by blocking the activation and catalytic activity of matrix metalloproteinase
    • Kim, Y. M.; Jang, J. W.; Lee, O. H.; Yeon, J.; Choi, E. Y.; Kim, K. W.; Lee, S. T.; Kwon, Y. G. Endostatin inhibits endothelial and tumor cellular invasion by blocking the activation and catalytic activity of matrix metalloproteinase Cancer Res. 2000, 60 (19) 5410-3
    • (2000) Cancer Res. , vol.60 , Issue.19 , pp. 5410-5413
    • Kim, Y.M.1    Jang, J.W.2    Lee, O.H.3    Yeon, J.4    Choi, E.Y.5    Kim, K.W.6    Lee, S.T.7    Kwon, Y.G.8
  • 27
    • 0037805549 scopus 로고    scopus 로고
    • Basement membranes: Structure, assembly and role in tumour angiogenesis
    • Kalluri, R. Basement membranes: structure, assembly and role in tumour angiogenesis Nat. Rev. Cancer 2003, 3 (6) 422-33
    • (2003) Nat. Rev. Cancer , vol.3 , Issue.6 , pp. 422-433
    • Kalluri, R.1
  • 28
    • 0037093808 scopus 로고    scopus 로고
    • The clinical use of bone resorption markers in patients with malignant bone disease
    • Coleman, R. E. The clinical use of bone resorption markers in patients with malignant bone disease Cancer 2002, 94 (10) 2521-33
    • (2002) Cancer , vol.94 , Issue.10 , pp. 2521-2533
    • Coleman, R.E.1
  • 29
    • 43149112727 scopus 로고    scopus 로고
    • Mammographic density. Potential mechanisms of breast cancer risk associated with mammographic density: Hypotheses based on epidemiological evidence
    • Martin, L. J.; Boyd, N. F. Mammographic density. Potential mechanisms of breast cancer risk associated with mammographic density: hypotheses based on epidemiological evidence Breast Cancer Res. 2008, 10 (1) 201
    • (2008) Breast Cancer Res. , vol.10 , Issue.1 , pp. 201
    • Martin, L.J.1    Boyd, N.F.2
  • 30
    • 44249123986 scopus 로고    scopus 로고
    • Isolation, identification and quantification of differentially expressed proteins from cancerous and normal breast tissues
    • Othman, M. I.; Majid, M. I.; Singh, M.; Man, C. N.; Lay-Harn, G. Isolation, identification and quantification of differentially expressed proteins from cancerous and normal breast tissues Ann. Clin. Biochem. 2008, 45 (Pt 3) 299-306
    • (2008) Ann. Clin. Biochem. , vol.45 , Issue.PART 3 , pp. 299-306
    • Othman, M.I.1    Majid, M.I.2    Singh, M.3    Man, C.N.4    Lay-Harn, G.5
  • 32
    • 1542510987 scopus 로고    scopus 로고
    • Effect of collagen substrates on proteomic modulation of breast cancer cells
    • Fontana, S.; Pucci-Minafra, I.; Becchi, M.; Freyria, A. M.; Minafra, S. Effect of collagen substrates on proteomic modulation of breast cancer cells Proteomics 2004, 4 (3) 849-60
    • (2004) Proteomics , vol.4 , Issue.3 , pp. 849-860
    • Fontana, S.1    Pucci-Minafra, I.2    Becchi, M.3    Freyria, A.M.4    Minafra, S.5
  • 34
    • 36348963174 scopus 로고    scopus 로고
    • Cyanogen bromide peptides of the fibrillar collagens I, III, and v and their mass spectrometric characterization: Detection of linear peptides, peptide glycosylation, and cross-linking peptides involved in formation of homo- and heterotypic fibrils
    • Henkel, W.; Dreisewerd, K. Cyanogen bromide peptides of the fibrillar collagens I, III, and V and their mass spectrometric characterization: detection of linear peptides, peptide glycosylation, and cross-linking peptides involved in formation of homo- and heterotypic fibrils J. Proteome Res. 2007, 6 (11) 4269-89
    • (2007) J. Proteome Res. , vol.6 , Issue.11 , pp. 4269-4289
    • Henkel, W.1    Dreisewerd, K.2
  • 35
    • 79959388445 scopus 로고    scopus 로고
    • Hydroxylation of recombinant human collagen type i alpha 1 in transgenic maize co-expressed with a recombinant human prolyl 4-hydroxylase
    • Xu, X.; Gan, Q.; Clough, R. C.; Pappu, K. M.; Howard, J. A.; Baez, J. A.; Wang, K. Hydroxylation of recombinant human collagen type I alpha 1 in transgenic maize co-expressed with a recombinant human prolyl 4-hydroxylase BMC Biotechnol. 2011, 11, 69
    • (2011) BMC Biotechnol. , vol.11 , pp. 69
    • Xu, X.1    Gan, Q.2    Clough, R.C.3    Pappu, K.M.4    Howard, J.A.5    Baez, J.A.6    Wang, K.7
  • 36
    • 79953160103 scopus 로고    scopus 로고
    • A novel 3-hydroxyproline (3Hyp)-rich motif marks the triple-helical C terminus of tendon type i collagen
    • Eyre, D. R.; Weis, M.; Hudson, D. M.; Wu, J. J.; Kim, L. A novel 3-hydroxyproline (3Hyp)-rich motif marks the triple-helical C terminus of tendon type I collagen J. Biol. Chem. 2011, 286 (10) 7732-6
    • (2011) J. Biol. Chem. , vol.286 , Issue.10 , pp. 7732-7736
    • Eyre, D.R.1    Weis, M.2    Hudson, D.M.3    Wu, J.J.4    Kim, L.5
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 1976, 72, 248-54
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 40
    • 77649265012 scopus 로고    scopus 로고
    • Glycation pattern of peptides condensed with maltose, lactose and glucose determined by ultraviolet matrix-assisted laser desorption/ionization tandem mass spectrometry
    • Montgomery, H.; Tanaka, K.; Belgacem, O. Glycation pattern of peptides condensed with maltose, lactose and glucose determined by ultraviolet matrix-assisted laser desorption/ionization tandem mass spectrometry Rapid Commun. Mass Spectrom. 2010, 24 (6) 841-8
    • (2010) Rapid Commun. Mass Spectrom. , vol.24 , Issue.6 , pp. 841-848
    • Montgomery, H.1    Tanaka, K.2    Belgacem, O.3
  • 42
    • 0025472946 scopus 로고
    • Differentiation of hydroxyproline isomers and isobars in peptides by tandem mass spectrometry
    • Kassel, D. B.; Biemann, K. Differentiation of hydroxyproline isomers and isobars in peptides by tandem mass spectrometry Anal. Chem. 1990, 62 (15) 1691-5
    • (1990) Anal. Chem. , vol.62 , Issue.15 , pp. 1691-1695
    • Kassel, D.B.1    Biemann, K.2
  • 43
    • 0003342555 scopus 로고
    • The amino acid composition of gelatins, collagens and elastins from different sources
    • Neuman, R. E. The amino acid composition of gelatins, collagens and elastins from different sources Arch. Biochem. 1949, 24 (2) 289-98
    • (1949) Arch. Biochem. , vol.24 , Issue.2 , pp. 289-298
    • Neuman, R.E.1
  • 44
    • 0014216708 scopus 로고
    • The incomplete hydroxylation of individual prolyl residues in collagen
    • Bornstein, P. The incomplete hydroxylation of individual prolyl residues in collagen J. Biol. Chem. 1967, 242 (10) 2572-4
    • (1967) J. Biol. Chem. , vol.242 , Issue.10 , pp. 2572-2574
    • Bornstein, P.1
  • 47
    • 71049119341 scopus 로고    scopus 로고
    • An in-solution ultrasonication-assisted digestion method for improved extracellular matrix proteome coverage
    • Hansen, K. C.; Kiemele, L.; Maller, O.; O'Brien, J.; Shankar, A.; Fornetti, J.; Schedin, P. An in-solution ultrasonication-assisted digestion method for improved extracellular matrix proteome coverage Mol. Cell. Proteomics 2009, 8 (7) 1648-57
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.7 , pp. 1648-1657
    • Hansen, K.C.1    Kiemele, L.2    Maller, O.3    O'Brien, J.4    Shankar, A.5    Fornetti, J.6    Schedin, P.7
  • 49
    • 0014144116 scopus 로고
    • Comparative sequence studies of rat skin and tendon collagen. I. Evidence for incomplete hydroxylation of individual prolyl residues in the normal proteins
    • Bornstein, P. Comparative sequence studies of rat skin and tendon collagen. I. Evidence for incomplete hydroxylation of individual prolyl residues in the normal proteins Biochemistry 1967, 6 (10) 3082-93
    • (1967) Biochemistry , vol.6 , Issue.10 , pp. 3082-3093
    • Bornstein, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.