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Volumn 581, Issue 14, 2007, Pages 2709-2714

Collagen matrix deposition is dramatically enhanced in vitro when crowded with charged macromolecules: The biological relevance of the excluded volume effect

Author keywords

Collagen deposition; Excluded volume effect; Extracellular matrix; Macromolecular crowding; Procollagen C proteinase

Indexed keywords

COLLAGEN; PROCOLLAGEN C PROTEINASE;

EID: 34249654626     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.05.020     Document Type: Article
Times cited : (135)

References (30)
  • 1
    • 0027318513 scopus 로고
    • Macromolecular crowding: biochemical, biophysical, and physiological consequences
    • Zimmerman S.B., and Minton A.P. Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 22 (1993) 27-65
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 2
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: an important but neglected aspect of the intracellular environment
    • Ellis R.J. Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr. Opin. Struct. Biol. 11 (2001) 114-119
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 114-119
    • Ellis, R.J.1
  • 3
    • 0000037251 scopus 로고    scopus 로고
    • Rapid diffusion of green fluorescent protein in the mitochondrial matrix
    • Partikian A., Ölveczky B., Swaminathan R., Li Y., and Verkman A.S. Rapid diffusion of green fluorescent protein in the mitochondrial matrix. J. Cell Biol. 140 (1998) 821-829
    • (1998) J. Cell Biol. , vol.140 , pp. 821-829
    • Partikian, A.1    Ölveczky, B.2    Swaminathan, R.3    Li, Y.4    Verkman, A.S.5
  • 4
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: obvious but underappreciated
    • Ellis R.J. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26 (2001) 597-604
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 5
    • 33847035543 scopus 로고    scopus 로고
    • In vitro enhancement of collagen matrix formation and crosslinking for applications in tissue engineering - a preliminary study
    • Lareu R.R., Arsianti I., Subramhanya K.H., Peng Y.X., and Raghunath M. In vitro enhancement of collagen matrix formation and crosslinking for applications in tissue engineering - a preliminary study. Tissue Eng. 13 (2007) 385-391
    • (2007) Tissue Eng. , vol.13 , pp. 385-391
    • Lareu, R.R.1    Arsianti, I.2    Subramhanya, K.H.3    Peng, Y.X.4    Raghunath, M.5
  • 6
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis, a cell-mediated matrix assembly process
    • Mao J., and Schwarzbauer J.E. Fibronectin fibrillogenesis, a cell-mediated matrix assembly process. Matrix Biol. 24 (2005) 389-399
    • (2005) Matrix Biol. , vol.24 , pp. 389-399
    • Mao, J.1    Schwarzbauer, J.E.2
  • 7
    • 2942714962 scopus 로고    scopus 로고
    • Tissue-engineered skin substitutes: from in vitro constructs to in vivo applications
    • Auger F.A., Berthod F., Moulin V., Pouliot R., and Germain L. Tissue-engineered skin substitutes: from in vitro constructs to in vivo applications. Biotechnol. Appl. Biochem. 39 (2004) 263-275
    • (2004) Biotechnol. Appl. Biochem. , vol.39 , pp. 263-275
    • Auger, F.A.1    Berthod, F.2    Moulin, V.3    Pouliot, R.4    Germain, L.5
  • 8
    • 0032937875 scopus 로고    scopus 로고
    • Carboxy-terminal conversion of profibrillin to fibrillin at a basic site by PACE/furin-like activity required for incorporation in the matrix
    • Raghunath M., et al. Carboxy-terminal conversion of profibrillin to fibrillin at a basic site by PACE/furin-like activity required for incorporation in the matrix. J. Cell. Sci. 112 (1999) 1093-1100
    • (1999) J. Cell. Sci. , vol.112 , pp. 1093-1100
    • Raghunath, M.1
  • 9
    • 33646364803 scopus 로고    scopus 로고
    • Fluid flow increases type II collagen deposition and tensile mechanical properties in bioreactor-grown tissue-engineering cartilage
    • Gemmiti C.V., and Guldberg R.E. Fluid flow increases type II collagen deposition and tensile mechanical properties in bioreactor-grown tissue-engineering cartilage. Tissue Eng. 12 (2006) 469-479
    • (2006) Tissue Eng. , vol.12 , pp. 469-479
    • Gemmiti, C.V.1    Guldberg, R.E.2
  • 10
    • 0028067615 scopus 로고
    • Prenatal diagnosis of collagen disorders by direct biochemical analysis of chorionic villus biopsies
    • Raghunath M., Steinmann B., DeLozier-Blanchet C., Extermann P., and Superti-Furga A. Prenatal diagnosis of collagen disorders by direct biochemical analysis of chorionic villus biopsies. Pediatr. Res. 36 (1994) 441-448
    • (1994) Pediatr. Res. , vol.36 , pp. 441-448
    • Raghunath, M.1    Steinmann, B.2    DeLozier-Blanchet, C.3    Extermann, P.4    Superti-Furga, A.5
  • 11
    • 34249747115 scopus 로고    scopus 로고
    • Macromolecular crowding in biological systems: dynamic light scattering (DLS) to quantify the excluded volume effect (EVE)
    • Harve K.S., Lareu R.R., Rajagopolan R., and Raghunath M. Macromolecular crowding in biological systems: dynamic light scattering (DLS) to quantify the excluded volume effect (EVE). Biophys. Rev. Lett. 1 (2006) 317-325
    • (2006) Biophys. Rev. Lett. , vol.1 , pp. 317-325
    • Harve, K.S.1    Lareu, R.R.2    Rajagopolan, R.3    Raghunath, M.4
  • 12
    • 0242558882 scopus 로고    scopus 로고
    • In vivo determination of steric and electrostatic exclusion of albumin in rat skin and skeletal muscle
    • Gyenge C.C., Tenstad O., and Wiig H. In vivo determination of steric and electrostatic exclusion of albumin in rat skin and skeletal muscle. J. Physiol. 552 (2003) 907-916
    • (2003) J. Physiol. , vol.552 , pp. 907-916
    • Gyenge, C.C.1    Tenstad, O.2    Wiig, H.3
  • 13
    • 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
  • 14
    • 0024818507 scopus 로고
    • Type I procollagen C-proteinase from mouse fibroblasts. Purification and demonstration of a 55-kDa enhancer glycoprotein
    • Kessler E., and Adar R. Type I procollagen C-proteinase from mouse fibroblasts. Purification and demonstration of a 55-kDa enhancer glycoprotein. Eur. J. Biochem. 186 (1989) 115-121
    • (1989) Eur. J. Biochem. , vol.186 , pp. 115-121
    • Kessler, E.1    Adar, R.2
  • 15
    • 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., 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
  • 16
    • 0033955104 scopus 로고    scopus 로고
    • Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor
    • Mott J.D., et al. 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
  • 17
    • 4544331662 scopus 로고    scopus 로고
    • Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges
    • Hall D., and Minton A.P. Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges. Biochim. Biophys. Acta 127 (2003) 1649-1656
    • (2003) Biochim. Biophys. Acta , vol.127 , pp. 1649-1656
    • Hall, D.1    Minton, A.P.2
  • 18
    • 0037470574 scopus 로고    scopus 로고
    • Effect of dextran on protein stability and conformation attributed to macromolecular crowding
    • Sasahara K., McPhie P., and Minton A.P. Effect of dextran on protein stability and conformation attributed to macromolecular crowding. J. Mol. Biol. 326 (2003) 1227-1237
    • (2003) J. Mol. Biol. , vol.326 , pp. 1227-1237
    • Sasahara, K.1    McPhie, P.2    Minton, A.P.3
  • 19
    • 0028420244 scopus 로고
    • Mammalian cell damage in a novel membrane bioreactor
    • Millward H.R., et al. Mammalian cell damage in a novel membrane bioreactor. Biotechnol. Bioeng. 43 (1994) 899-906
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 899-906
    • Millward, H.R.1
  • 20
    • 0036323143 scopus 로고    scopus 로고
    • Formation of three-dimensional cell/polymer constructs for bone tissue engineering in a spinner flask and a rotating wall vessel bioreactor
    • Sikavitsas V.I., Bancroft G.N., and Antonios M.G. Formation of three-dimensional cell/polymer constructs for bone tissue engineering in a spinner flask and a rotating wall vessel bioreactor. J. Biomed. Mater. Res. 62 (2002) 136-148
    • (2002) J. Biomed. Mater. Res. , vol.62 , pp. 136-148
    • Sikavitsas, V.I.1    Bancroft, G.N.2    Antonios, M.G.3
  • 21
    • 0035372005 scopus 로고    scopus 로고
    • Effect of convection on osteoblastic cell growth and function in biodegradable polymer foam scaffolds
    • Goldstein A.S., Juarez T.M., Helmke C.D., Gustin M.C., and Mikos A.G. Effect of convection on osteoblastic cell growth and function in biodegradable polymer foam scaffolds. Biomaterials 22 (2001) 1279-1288
    • (2001) Biomaterials , vol.22 , pp. 1279-1288
    • Goldstein, A.S.1    Juarez, T.M.2    Helmke, C.D.3    Gustin, M.C.4    Mikos, A.G.5
  • 22
    • 3843112154 scopus 로고    scopus 로고
    • Bioreactor-based bone tissue engineering: the influence of dynamic flow on osteoblast phenotypic expression and matrix mineralization
    • Yu X., Botchwey E.A., Levine E.M., Pollack S.R., and Laurencin C.T. Bioreactor-based bone tissue engineering: the influence of dynamic flow on osteoblast phenotypic expression and matrix mineralization. Proc. Natl. Acad. Sci. USA 101 (2004) 11203-11208
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11203-11208
    • Yu, X.1    Botchwey, E.A.2    Levine, E.M.3    Pollack, S.R.4    Laurencin, C.T.5
  • 23
    • 16344389134 scopus 로고    scopus 로고
    • Molecular crowding enhances native state stability and refolding rates of globular proteins
    • Cheung M.S., Klimov D., and Thirumalai D. Molecular crowding enhances native state stability and refolding rates of globular proteins. Proc. Natl. Acad. Sci. USA 102 (2005) 4753-4758
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4753-4758
    • Cheung, M.S.1    Klimov, D.2    Thirumalai, D.3
  • 25
    • 0037418563 scopus 로고    scopus 로고
    • Metabolic buffering exerted by macromolecular crowding on DNA-DNA interactions: origin and physiological significance
    • Goobes R., Kahana N., Cohen O., and Minsky A. Metabolic buffering exerted by macromolecular crowding on DNA-DNA interactions: origin and physiological significance. Biochemistry 42 (2003) 2431-2440
    • (2003) Biochemistry , vol.42 , pp. 2431-2440
    • Goobes, R.1    Kahana, N.2    Cohen, O.3    Minsky, A.4
  • 26
    • 4544252011 scopus 로고    scopus 로고
    • The effect of macromolecular crowding on protein aggregation and amyloid fibril formation
    • Munishkina L.A., Cooper E.M., Uversky V.N., and Fink A.L. The effect of macromolecular crowding on protein aggregation and amyloid fibril formation. J. Mol. Recog. 17 (2004) 456-464
    • (2004) J. Mol. Recog. , vol.17 , pp. 456-464
    • Munishkina, L.A.1    Cooper, E.M.2    Uversky, V.N.3    Fink, A.L.4
  • 27
    • 34249677135 scopus 로고
    • The resistance to dispersion of collagen fibres formed in vitro in the presence of ascorbic acid
    • Candlish J.K., and Tristram G.R. The resistance to dispersion of collagen fibres formed in vitro in the presence of ascorbic acid. Biochim. Biophys. Acta 78 (1963) 289-294
    • (1963) Biochim. Biophys. Acta , vol.78 , pp. 289-294
    • Candlish, J.K.1    Tristram, G.R.2
  • 28
    • 0034210902 scopus 로고    scopus 로고
    • A novel injectable collagen matrix: in vitro characterization and in vivo evaluation
    • Laude D., Odlum K., Rudnicki S., and Bachrach N. A novel injectable collagen matrix: in vitro characterization and in vivo evaluation. J. Biomech. Eng. 122 (2000) 231-235
    • (2000) J. Biomech. Eng. , vol.122 , pp. 231-235
    • Laude, D.1    Odlum, K.2    Rudnicki, S.3    Bachrach, N.4
  • 30
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton A.P. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem. 276 (2001) 10577-10580
    • (2001) J. Biol. Chem. , vol.276 , pp. 10577-10580
    • Minton, A.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.