메뉴 건너뛰기




Volumn 9, Issue , 2013, Pages

Global remodelling of cellular microenvironment due to loss of collagen VII

Author keywords

disease proteomics; extracellular matrix (ECM); mass spectrometry; MMP14; primary human fibroblasts

Indexed keywords

COLLAGEN TYPE 7; MATRIX PROTEIN; METALLOPROTEINASE; PROTEINASE; PROTEOME; TRANSFORMING GROWTH FACTOR BETA; PROTEIN;

EID: 84876580040     PISSN: None     EISSN: 17444292     Source Type: Journal    
DOI: 10.1038/msb.2013.17     Document Type: Article
Times cited : (94)

References (59)
  • 2
    • 84872593231 scopus 로고    scopus 로고
    • Systems-level analysis of proteolytic events in increased vascular permeability and complement activation in skin inflammation
    • auf demKeller U, Prudova A, Eckhard U, Fingleton B, Overall CM (2013) Systems-level analysis of proteolytic events in increased vascular permeability and complement activation in skin inflammation. Sci Signal 6: rs2
    • (2013) Sci Signal , vol.6
    • Aufdemkeller, U.1    Prudova, A.2    Eckhard, U.3    Fingleton, B.4    Overall, C.M.5
  • 4
    • 84867840695 scopus 로고    scopus 로고
    • Extracellular matrix, integrins, and growth factors as tailors of the stem cell niche
    • Brizzi MF, Tarone G, Defilippi P (2012) Extracellular matrix, integrins, and growth factors as tailors of the stem cell niche. Curr Opin Cell Biol 24: 645-651
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 645-651
    • Brizzi, M.F.1    Tarone, G.2    Defilippi, P.3
  • 6
    • 72749114050 scopus 로고    scopus 로고
    • Updated biological roles for matrix metalloproteinases and new 'intracellular' substrates revealed by degradomics
    • Butler GS, Overall CM (2009) Updated biological roles for matrix metalloproteinases and new 'intracellular' substrates revealed by degradomics. Biochemistry 48: 10830-10845
    • (2009) Biochemistry , vol.48 , pp. 10830-10845
    • Butler, G.S.1    Overall, C.M.2
  • 7
    • 84857518627 scopus 로고    scopus 로고
    • Biological sequence motif discovery using motif-x
    • Chapter 13: Unit 13
    • Chou MF, Schwartz D (2011) Biological sequence motif discovery using motif-x. Curr Protoc Bioinformatics Chapter 13: Unit 13. 15-24
    • (2011) Curr Protoc Bioinformatics , pp. 15-24
    • Chou, M.F.1    Schwartz, D.2
  • 8
    • 0026688049 scopus 로고
    • Exclusion of stromelysin-1, stromelysin-2, interstitial collagenase and fibronectin genes as the mutant loci in a family with recessive epidermolysis bullosa dystrophica and a form of cerebellar ataxia
    • Colombi M, Gardella R, Zoppi N, Moro L, Marini D, Spurr NK, Barlati S (1992) Exclusion of stromelysin-1, stromelysin-2, interstitial collagenase and fibronectin genes as the mutant loci in a family with recessive epidermolysis bullosa dystrophica and a form of cerebellar ataxia. Hum Genet 89: 503-507
    • (1992) Hum Genet , vol.89 , pp. 503-507
    • Colombi, M.1    Gardella, R.2    Zoppi, N.3    Moro, L.4    Marini, D.5    Spurr, N.K.6    Barlati, S.7
  • 9
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J, Mann M (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26: 1367-1372
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 11
    • 77957350375 scopus 로고    scopus 로고
    • Proteomic analysis identification of a pattern of shared alterations in the secretome of dermal fibroblasts from systemic sclerosis and nephrogenic systemic fibrosis
    • Del Galdo F, Shaw MA, Jimenez SA (2010) Proteomic analysis identification of a pattern of shared alterations in the secretome of dermal fibroblasts from systemic sclerosis and nephrogenic systemic fibrosis. Am J Pathol 177: 1638-1646
    • (2010) Am J Pathol , vol.177 , pp. 1638-1646
    • Del Galdo, F.1    Shaw, M.A.2    Jimenez, S.A.3
  • 13
    • 49549113643 scopus 로고    scopus 로고
    • Global mapping of the topography and magnitude of proteolytic events in apoptosis
    • Dix MM, Simon GM, Cravatt BF (2008) Global mapping of the topography and magnitude of proteolytic events in apoptosis. Cell 134: 679-691
    • (2008) Cell , vol.134 , pp. 679-691
    • Dix, M.M.1    Simon, G.M.2    Cravatt, B.F.3
  • 14
    • 84857959247 scopus 로고    scopus 로고
    • The degradative inventory of the cell: Proteomic insights
    • Engelke R, Becker AC, Dengjel J (2012) The degradative inventory of the cell: proteomic insights. Antioxid Redox Signal 17: 803-812
    • (2012) Antioxid Redox Signal , vol.17 , pp. 803-812
    • Engelke, R.1    Becker, A.C.2    Dengjel, J.3
  • 19
    • 0032563223 scopus 로고    scopus 로고
    • Some, but not all, glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils, and skin blistering
    • DOI 10.1074/jbc.273.30.19228
    • Hammami-Hauasli N, Schumann H, Raghunath M, Kilgus O, Luthi U, Luger T, Bruckner-Tuderman L (1998) Some, but not all, glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils, and skin blistering. J Biol Chem 273: 19228-19234 (Pubitemid 28366322)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.30 , pp. 19228-19234
    • Hammami-Hauasli, N.1    Schumann, H.2    Raghunath, M.3    Kilgus, O.4    Luthi, U.5    Luger, T.6    Bruckner-Tuderman, L.7
  • 20
    • 0035156633 scopus 로고    scopus 로고
    • TNF-α stimulates activation of pro-MMP2 in human skin through NF-κB mediated induction of MT1-MMP
    • Han YP, Tuan TL, Wu H, Hughes M, Garner WL (2001) TNF-alpha stimulates activation of pro-MMP2 in human skin through NF-(kappa)B mediated induction of MT1-MMP. J Cell Sci 114: 131-139 (Pubitemid 32118063)
    • (2001) Journal of Cell Science , vol.114 , Issue.1 , pp. 131-139
    • Han, Y.-P.1    Tuan, T.-L.2    Wu, H.3    Hughes, M.4    Garner, W.L.5
  • 21
    • 33751161054 scopus 로고    scopus 로고
    • Molecular and diagnostic aspects of genetic skin fragility
    • Has C, Bruckner-Tuderman L (2006) Molecular and diagnostic aspects of genetic skin fragility. J Dermatol Sci 44: 129-144
    • (2006) J Dermatol Sci , vol.44 , pp. 129-144
    • Has, C.1    Bruckner-Tuderman, L.2
  • 24
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da W, Sherman BT, Lempicki RA (2009) Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 4: 44-57
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • Huang Da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 25
    • 71949089798 scopus 로고    scopus 로고
    • Forty-two novel COL7A1 mutations and the role of a frequent single nucleotide polymorphism in the MMP1 promoter in modulation of disease severity in a large European dystrophic epidermolysis bullosa cohort
    • Kern JS, Gruninger G, Imsak R, Muller ML, Schumann H, Kiritsi D, Emmert S, Borozdin W, Kohlhase J, Bruckner-Tuderman L, Has C (2009) Forty-two novel COL7A1 mutations and the role of a frequent single nucleotide polymorphism in the MMP1 promoter in modulation of disease severity in a large European dystrophic epidermolysis bullosa cohort. Br J Dermatol 161: 1089-1097
    • (2009) Br J Dermatol , vol.161 , pp. 1089-1097
    • Kern, J.S.1    Gruninger, G.2    Imsak, R.3    Muller, M.L.4    Schumann, H.5    Kiritsi, D.6    Emmert, S.7    Borozdin, W.8    Kohlhase, J.9    Bruckner-Tuderman, L.10    Has, C.11
  • 26
    • 33646128739 scopus 로고    scopus 로고
    • Expanding the COL7A1 mutation database: Novel and recurrent mutations and unusual genotype-phenotype constellations in 41 patients with dystrophic epidermolysis bullosa
    • Kern JS, Kohlhase J, Bruckner-Tuderman L, Has C (2006) Expanding the COL7A1 mutation database: novel and recurrent mutations and unusual genotype-phenotype constellations in 41 patients with dystrophic epidermolysis bullosa. J Invest Dermatol 126: 1006-1012
    • (2006) J Invest Dermatol , vol.126 , pp. 1006-1012
    • Kern, J.S.1    Kohlhase, J.2    Bruckner-Tuderman, L.3    Has, C.4
  • 27
    • 0028244447 scopus 로고
    • Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues
    • Leco KJ, Khokha R, Pavloff N, Hawkes SP, Edwards DR (1994) Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues. J Biol Chem 269: 9352-9360 (Pubitemid 24209266)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.12 , pp. 9352-9360
    • Leco, K.J.1    Khokha, R.2    Pavloff, N.3    Hawkes, S.P.4    Edwards, D.R.5
  • 28
    • 78650864017 scopus 로고    scopus 로고
    • Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases
    • Loenarz C, Schofield CJ (2011) Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases. Trends Biochem Sci 36: 7-18
    • (2011) Trends Biochem Sci , vol.36 , pp. 7-18
    • Loenarz, C.1    Schofield, C.J.2
  • 29
    • 79960153872 scopus 로고    scopus 로고
    • Series 'matrix metalloproteinases in lung health and disease': Biological role of matrix metalloproteinases: A critical balance
    • Loffek S, Schilling O, Franzke CW (2011) Series 'matrix metalloproteinases in lung health and disease': Biological role of matrix metalloproteinases: a critical balance. Eur Respir J 38: 191-208
    • (2011) Eur Respir J , vol.38 , pp. 191-208
    • Loffek, S.1    Schilling, O.2    Franzke, C.W.3
  • 33
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • DOI 10.1016/j.tig.2003.11.004
    • Myllyharju J, Kivirikko KI (2004) Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet 20: 33-43 (Pubitemid 38032818)
    • (2004) Trends in Genetics , vol.20 , Issue.1 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 34
    • 84859823928 scopus 로고    scopus 로고
    • The matrisome: In silico definition and in vivo characterization by proteomics of normal and tumor extracellular matrices
    • M111.014647
    • Naba A, Clauser KR, Hoersch S, Liu H, Carr SA, Hynes RO (2012) The matrisome: in silico definition and in vivo characterization by proteomics of normal and tumor extracellular matrices. Mol Cell Proteomics 11 : M111.014647
    • (2012) Mol Cell Proteomics , vol.11
    • Naba, A.1    Clauser, K.R.2    Hoersch, S.3    Liu, H.4    Carr, S.A.5    Hynes, R.O.6
  • 36
    • 33750456519 scopus 로고    scopus 로고
    • Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
    • DOI 10.1016/j.cell.2006.09.026, PII S0092867406012748
    • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127: 635-648 (Pubitemid 44647421)
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 37
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1: 376-386
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 38
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: Innovations for the post-trial era
    • DOI 10.1038/nrc884
    • Overall CM, Lopez-Otin C (2002) Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat Rev Cancer 2: 657-672 (Pubitemid 37328917)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.9 , pp. 657-672
    • Overall, C.M.1    Lopez-Otin, C.2
  • 39
    • 0026794057 scopus 로고
    • A new inhibitor of metalloproteinases from chicken: ChIMP-3. A third member of the TIMP family
    • Pavloff N, Staskus PW, Kishnani NS, Hawkes SP (1992) A new inhibitor of metalloproteinases from chicken: ChIMP-3. A third member of the TIMP family. J Biol Chem 267: 17321-17326
    • (1992) J Biol Chem , vol.267 , pp. 17321-17326
    • Pavloff, N.1    Staskus, P.W.2    Kishnani, N.S.3    Hawkes, S.P.4
  • 40
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • Petersen TN, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8: 785-786
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 41
    • 33751103918 scopus 로고    scopus 로고
    • Comparative proteomic analysis of extracellular matrix proteins secreted by two types of skin fibroblasts
    • DOI 10.1002/pmic.200402040
    • Pflieger D, Chabane S, Gaillard O, Bernard BA, Ducoroy P, Rossier J, Vinh J (2006) Comparative proteomic analysis of extracellular matrix proteins secreted by two types of skin fibroblasts. Proteomics 6: 5868-5879 (Pubitemid 44764023)
    • (2006) Proteomics , vol.6 , Issue.21 , pp. 5868-5879
    • Pflieger, D.1    Chabane, S.2    Gaillard, O.3    Bernard, B.A.4    Ducoroy, P.5    Rossier, J.6    Vinh, J.7
  • 42
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • DOI 10.1038/nprot.2007.261, PII NPROT.2007.261
    • Rappsilber J, Mann M, Ishihama Y (2007) Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat Protoc 2: 1896-1906 (Pubitemid 47308128)
    • (2007) Nature Protocols , vol.2 , Issue.8 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 43
    • 61649126270 scopus 로고    scopus 로고
    • Predicting protein post-translational modifications using meta-analysis of proteome scale data sets
    • Schwartz D, Chou MF, Church GM (2009) Predicting protein post-translational modifications using meta-analysis of proteome scale data sets. Mol Cell Proteomics 8: 365-379
    • (2009) Mol Cell Proteomics , vol.8 , pp. 365-379
    • Schwartz, D.1    Chou, M.F.2    Church, G.M.3
  • 44
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • DOI 10.1038/nbt1146, PII N1146
    • Schwartz D, Gygi SP (2005) An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat Biotechnol 23: 1391-1398 (Pubitemid 41679391)
    • (2005) Nature Biotechnology , vol.23 , Issue.11 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 45
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A, Tomas H, Havlis J, Olsen JV, Mann M (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc 1: 2856-2860
    • (2006) Nat Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 46
    • 4544341015 scopus 로고    scopus 로고
    • Linear models and empirical bayes methods for assessing differential expression in microarray experiments
    • Article 3
    • Smyth GK (2004) Linear models and empirical bayes methods for assessing differential expression in microarray experiments. Stat Appl Genet Mol Biol 3: Article 3
    • (2004) Stat Appl Genet Mol Biol , vol.3
    • Smyth, G.K.1
  • 47
    • 78649279980 scopus 로고    scopus 로고
    • Comparative quantitation of proteome alterations induced by aging or immortalization in primary human fibroblasts and keratinocytes for clinical applications
    • Sprenger A, Kuttner V, Biniossek ML, Gretzmeier C, Boerries M, Mack C, Has C, Bruckner-Tuderman L, Dengjel J (2010) Comparative quantitation of proteome alterations induced by aging or immortalization in primary human fibroblasts and keratinocytes for clinical applications. Mol Biosyst 6: 1579-1582
    • (2010) Mol Biosyst , vol.6 , pp. 1579-1582
    • Sprenger, A.1    Kuttner, V.2    Biniossek, M.L.3    Gretzmeier, C.4    Boerries, M.5    MacK, C.6    Has, C.7    Bruckner-Tuderman, L.8    Dengjel, J.9
  • 49
    • 38949094346 scopus 로고    scopus 로고
    • A frequent functional SNP in the MMP1 promoter is associated with higher disease severity in recessive dystrophic epidermolysis bullosa
    • DOI 10.1002/humu.20647
    • Titeux M, Pendaries V, Tonasso L, Decha A, Bodemer C, Hovnanian A (2008) A frequent functional SNP in the MMP1 promoter is associated with higher disease severity in recessive dystrophic epidermolysis bullosa. Hum Mutat 29: 267-276 (Pubitemid 351240599)
    • (2008) Human Mutation , vol.29 , Issue.2 , pp. 267-276
    • Titeux, M.1    Pendaries, V.2    Tonasso, L.3    Decha, A.4    Bodemer, C.5    Hovnanian, A.6
  • 52
    • 39549115926 scopus 로고    scopus 로고
    • Preparation of extracellular matrices produced by cultured corneal endothelial and PF-HR9 endodermal cells
    • Chapter 10: Unit 10.4
    • Vlodavsky I (2001) Preparation of extracellular matrices produced by cultured corneal endothelial and PF-HR9 endodermal cells. Curr Protoc Cell Biol Chapter 10: Unit 10.4
    • (2001) Curr Protoc Cell Biol
    • Vlodavsky, I.1
  • 54
    • 84863872233 scopus 로고    scopus 로고
    • Cell-extracellular matrix interactions in normal and diseased skin
    • (pii)
    • Watt FM, Fujiwara H (2011) Cell-extracellular matrix interactions in normal and diseased skin. Cold Spring Harb Perspect Biol 3(pii): a005124
    • (2011) Cold Spring Harb Perspect Biol , vol.3
    • Watt, F.M.1    Fujiwara, H.2
  • 55
    • 0030016342 scopus 로고    scopus 로고
    • The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3
    • DOI 10.1074/jbc.271.29.17119
    • Will H, Atkinson SJ, Butler GS, Smith B, Murphy G (1996) The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3. J Biol Chem 271: 17119-17123 (Pubitemid 26244261)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.29 , pp. 17119-17123
    • Will, H.1    Atkinson, S.J.2    Butler, G.S.3    Smith, B.4    Murphy, G.5
  • 56
    • 0024529260 scopus 로고
    • Collagenase expression in skin fibroblasts from families with recessive dystrophic epidermolysis bullosa
    • Winberg JO, Gedde-Dahl Jr. T, Bauer EA (1989) Collagenase expression in skin fibroblasts from families with recessive dystrophic epidermolysis bullosa. J Invest Dermatol 92: 82-85 (Pubitemid 19027696)
    • (1989) Journal of Investigative Dermatology , vol.92 , Issue.1 , pp. 82-85
    • Winberg, J.-O.1    Gedde-Dahl Jr., T.2    Bauer, E.A.3
  • 57
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski JR, Zougman A, Nagaraj N, Mann M (2009) Universal sample preparation method for proteome analysis. Nat Methods 6: 359-362
    • (2009) Nat Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 58
    • 84863702343 scopus 로고    scopus 로고
    • Mechanisms of fibrosis: Therapeutic translation for fibrotic disease
    • Wynn TA, Ramalingam TR (2012) Mechanisms of fibrosis: therapeutic translation for fibrotic disease. Nat Med 18: 1028-1040
    • (2012) Nat Med , vol.18 , pp. 1028-1040
    • Wynn, T.A.1    Ramalingam, T.R.2
  • 59
    • 78649301860 scopus 로고    scopus 로고
    • Quantitative proteomics for the analysis of spatio-temporal protein dynamics during autophagy
    • Zimmermann AC, Zarei M, Eiselein S, Dengjel J (2010) Quantitative proteomics for the analysis of spatio-temporal protein dynamics during autophagy. Autophagy 6: 1009-1016
    • (2010) Autophagy , vol.6 , pp. 1009-1016
    • Zimmermann, A.C.1    Zarei, M.2    Eiselein, S.3    Dengjel, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.