메뉴 건너뛰기




Volumn 42, Issue 11, 2010, Pages 1808-1815

Development of cell-based immunoassays to measure type I collagen in cultured fibroblasts

Author keywords

Collagen; Extracellular matrix; Fibroblasts; Fibrosis; TGF

Indexed keywords

COLLAGEN TYPE 1; MONOCLONAL ANTIBODY; TRANSFORMING GROWTH FACTOR BETA;

EID: 77957277152     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2010.07.011     Document Type: Article
Times cited : (4)

References (38)
  • 1
    • 0024587195 scopus 로고
    • Liver fibrosis and extracellular matrix
    • Biagini G., Ballardini G. Liver fibrosis and extracellular matrix. J Hepatol 1989, 8:115-124.
    • (1989) J Hepatol , vol.8 , pp. 115-124
    • Biagini, G.1    Ballardini, G.2
  • 2
    • 0019511475 scopus 로고
    • Collagen biosynthesis by human skin fibroblasts. III. The effects of ascorbic acid on procollagen production and prolyl hydroxylase activity
    • Booth B.A., Uitto J. Collagen biosynthesis by human skin fibroblasts. III. The effects of ascorbic acid on procollagen production and prolyl hydroxylase activity. Biochim Biophys Acta 1981, 675:117-122.
    • (1981) Biochim Biophys Acta , vol.675 , pp. 117-122
    • Booth, B.A.1    Uitto, J.2
  • 3
    • 0030833343 scopus 로고    scopus 로고
    • Early detection of type III procollagen peptide in acute lung injury. Pathogenetic and prognostic significance
    • Chesnutt A.N., Matthay M.A., Tibayan F.A., Clark J.G. Early detection of type III procollagen peptide in acute lung injury. Pathogenetic and prognostic significance. Am J Respir Crit Care Med 1997, 156:840-845.
    • (1997) Am J Respir Crit Care Med , vol.156 , pp. 840-845
    • Chesnutt, A.N.1    Matthay, M.A.2    Tibayan, F.A.3    Clark, J.G.4
  • 4
    • 44949107350 scopus 로고    scopus 로고
    • Fibroblast growth factor represses Smad-mediated myofibroblast activation in aortic valvular interstitial cells
    • Cushing M.C., Mariner P.D., Liao J.T., Sims E.A., Anseth K.S. Fibroblast growth factor represses Smad-mediated myofibroblast activation in aortic valvular interstitial cells. FASEB J 2008, 22:1769-1777.
    • (2008) FASEB J , vol.22 , pp. 1769-1777
    • Cushing, M.C.1    Mariner, P.D.2    Liao, J.T.3    Sims, E.A.4    Anseth, K.S.5
  • 5
    • 0019730113 scopus 로고
    • Posttranslational events in collagen biosynthesis
    • Davidson J.M., Berg R.A. Posttranslational events in collagen biosynthesis. Methods Cell Biol 1981, 23:119-136.
    • (1981) Methods Cell Biol , vol.23 , pp. 119-136
    • Davidson, J.M.1    Berg, R.A.2
  • 6
    • 0030010244 scopus 로고    scopus 로고
    • The Ehlers-Danlos syndrome: a heritable collagen disorder as cause of bleeding
    • de Paepe A. The Ehlers-Danlos syndrome: a heritable collagen disorder as cause of bleeding. Thromb Haemost 1996, 75:379-386.
    • (1996) Thromb Haemost , vol.75 , pp. 379-386
    • de Paepe, A.1
  • 8
    • 33645977483 scopus 로고    scopus 로고
    • In-cell Western assay: a new approach to visualize tissue factor in human monocytes
    • Egorina E.M., Sovershaev M.A., Osterud B. In-cell Western assay: a new approach to visualize tissue factor in human monocytes. J Thromb Haemost 2006, 4:614-620.
    • (2006) J Thromb Haemost , vol.4 , pp. 614-620
    • Egorina, E.M.1    Sovershaev, M.A.2    Osterud, B.3
  • 10
    • 0024543691 scopus 로고
    • Collagen processing, crosslinking, and fibril bundle assembly in matrix produced by fibroblasts in long-term cultures supplemented with ascorbic acid
    • Grinnell F., Fukamizu H., Pawelek P., Nakagawa S. Collagen processing, crosslinking, and fibril bundle assembly in matrix produced by fibroblasts in long-term cultures supplemented with ascorbic acid. Exp Cell Res 1989, 181:483-491.
    • (1989) Exp Cell Res , vol.181 , pp. 483-491
    • Grinnell, F.1    Fukamizu, H.2    Pawelek, P.3    Nakagawa, S.4
  • 11
    • 34948867738 scopus 로고    scopus 로고
    • The collagen family members as cell adhesion proteins
    • Heino J. The collagen family members as cell adhesion proteins. Bioessays 2007, 29:1001-1010.
    • (2007) Bioessays , vol.29 , pp. 1001-1010
    • Heino, J.1
  • 12
    • 1842579704 scopus 로고    scopus 로고
    • Matrix loading: assembly of extracellular matrix collagen fibrils during embryogenesis
    • Kadler K. Matrix loading: assembly of extracellular matrix collagen fibrils during embryogenesis. Birth Defects Res C Embryo Today 2004, 72:1-11.
    • (2004) Birth Defects Res C Embryo Today , vol.72 , pp. 1-11
    • Kadler, K.1
  • 14
    • 0031940007 scopus 로고    scopus 로고
    • Collagen biosynthesis: a mini-review cluster
    • Kivirikko K.I. Collagen biosynthesis: a mini-review cluster. Matrix Biol 1998, 16:355-356.
    • (1998) Matrix Biol , vol.16 , pp. 355-356
    • Kivirikko, K.I.1
  • 15
    • 0031572863 scopus 로고    scopus 로고
    • Measurement of histidinohydroxylysinonorleucine and hydroxyproline in skin collagen by reversed-phase high-performance liquid chromatography after 9-fluorenylmethyl chloroformate labeling
    • Kondo A., Ishikawa O., Okada K., Miyachi Y., Abe S., Kuboki Y. Measurement of histidinohydroxylysinonorleucine and hydroxyproline in skin collagen by reversed-phase high-performance liquid chromatography after 9-fluorenylmethyl chloroformate labeling. Anal Biochem 1997, 252:255-259.
    • (1997) Anal Biochem , vol.252 , pp. 255-259
    • Kondo, A.1    Ishikawa, O.2    Okada, K.3    Miyachi, Y.4    Abe, S.5    Kuboki, Y.6
  • 16
    • 3242661630 scopus 로고    scopus 로고
    • Secretion of collagen type IV by human renal fibroblasts is increased by high glucose via a TGF-beta-independent pathway
    • Lam S., van der Geest R.N., Verhagen N.A., Daha M.R., van Kooten C. Secretion of collagen type IV by human renal fibroblasts is increased by high glucose via a TGF-beta-independent pathway. Nephrol Dial Transplant 2004, 19:1694-1701.
    • (2004) Nephrol Dial Transplant , vol.19 , pp. 1694-1701
    • Lam, S.1    van der Geest, R.N.2    Verhagen, N.A.3    Daha, M.R.4    van Kooten, C.5
  • 18
    • 0026078964 scopus 로고
    • The effect of transforming growth factor beta on rates of procollagen synthesis and degradation in vitro
    • McAnulty R.J., Campa J.S., Cambrey A.D., Laurent G.J. The effect of transforming growth factor beta on rates of procollagen synthesis and degradation in vitro. Biochim Biophys Acta 1991, 1091:231-235.
    • (1991) Biochim Biophys Acta , vol.1091 , pp. 231-235
    • McAnulty, R.J.1    Campa, J.S.2    Cambrey, A.D.3    Laurent, G.J.4
  • 19
    • 0029938817 scopus 로고    scopus 로고
    • Immunoassay for intact amino-terminal propeptide of human type I procollagen
    • Melkko J., Kauppila S., Niemi S., Risteli L., Haukipuro K., Jukkola A., et al. Immunoassay for intact amino-terminal propeptide of human type I procollagen. Clin Chem 1996, 42:947-954.
    • (1996) Clin Chem , vol.42 , pp. 947-954
    • Melkko, J.1    Kauppila, S.2    Niemi, S.3    Risteli, L.4    Haukipuro, K.5    Jukkola, A.6
  • 20
    • 0037358282 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis
    • Myllyharju J. Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis. Matrix Biol 2003, 22:15-24.
    • (2003) Matrix Biol , vol.22 , pp. 15-24
    • Myllyharju, J.1
  • 21
    • 0033044717 scopus 로고    scopus 로고
    • In vitro synthesis of type I collagen: quantification of carboxyterminal propeptide of procollagen type I versus tritiated proline incorporation
    • Nacher M., Serrano S., Marinoso M.L., Garcia M.C., Bosch J., Diez A., et al. In vitro synthesis of type I collagen: quantification of carboxyterminal propeptide of procollagen type I versus tritiated proline incorporation. Calcif Tissue Int 1999, 64:224-228.
    • (1999) Calcif Tissue Int , vol.64 , pp. 224-228
    • Nacher, M.1    Serrano, S.2    Marinoso, M.L.3    Garcia, M.C.4    Bosch, J.5    Diez, A.6
  • 22
    • 0020954847 scopus 로고
    • Collagen: structure, function, and metabolism in normal and fibrotic tissues
    • Nimni M.E. Collagen: structure, function, and metabolism in normal and fibrotic tissues. Semin Arthritis Rheum 1983, 13:1-86.
    • (1983) Semin Arthritis Rheum , vol.13 , pp. 1-86
    • Nimni, M.E.1
  • 23
    • 0023938927 scopus 로고
    • Expression of basement membrane zone genes coding for type IV procollagen and laminin by human skin fibroblasts in vitro: elevated alpha 1 (IV) collagen mRNA levels in lipoid proteinosis
    • Olsen D.R., Chu M.L., Uitto J. Expression of basement membrane zone genes coding for type IV procollagen and laminin by human skin fibroblasts in vitro: elevated alpha 1 (IV) collagen mRNA levels in lipoid proteinosis. J Invest Dermatol 1988, 90:734-738.
    • (1988) J Invest Dermatol , vol.90 , pp. 734-738
    • Olsen, D.R.1    Chu, M.L.2    Uitto, J.3
  • 24
    • 0030220663 scopus 로고    scopus 로고
    • Procollagen type I N-terminal propeptide (PINP) as an indicator of type I collagen metabolism: ELISA development, reference interval, and hypovitaminosis D induced hyperparathyroidism
    • Orum O., Hansen M., Jensen C.H., Sorensen H.A., Jensen L.B., Horslev-Petersen K., et al. Procollagen type I N-terminal propeptide (PINP) as an indicator of type I collagen metabolism: ELISA development, reference interval, and hypovitaminosis D induced hyperparathyroidism. Bone 1996, 19:157-163.
    • (1996) Bone , vol.19 , pp. 157-163
    • Orum, O.1    Hansen, M.2    Jensen, C.H.3    Sorensen, H.A.4    Jensen, L.B.5    Horslev-Petersen, K.6
  • 25
    • 0035218932 scopus 로고    scopus 로고
    • Collagen structure and functional implications
    • Ottani V., Raspanti M., Ruggeri A. Collagen structure and functional implications. Micron 2001, 32:251-260.
    • (2001) Micron , vol.32 , pp. 251-260
    • Ottani, V.1    Raspanti, M.2    Ruggeri, A.3
  • 26
    • 0027745820 scopus 로고
    • Mutations in type 1 procollagen that cause osteogenesis imperfecta: effects of the mutations on the assembly of collagen into fibrils, the basis of phenotypic variations, and potential antisense therapies
    • Prockop D.J., Colige A., Helminen H., Khillan J.S., Pereira R., Vandenberg P. Mutations in type 1 procollagen that cause osteogenesis imperfecta: effects of the mutations on the assembly of collagen into fibrils, the basis of phenotypic variations, and potential antisense therapies. J Bone Miner Res 1993, 8(Suppl. 2):S489-492.
    • (1993) J Bone Miner Res , vol.8 , Issue.SUPPL. 2
    • Prockop, D.J.1    Colige, A.2    Helminen, H.3    Khillan, J.S.4    Pereira, R.5    Vandenberg, P.6
  • 27
    • 0027939832 scopus 로고
    • The role of extracellular matrix in postinflammatory wound healing and fibrosis
    • Raghow R. The role of extracellular matrix in postinflammatory wound healing and fibrosis. FASEB J 1994, 8:823-831.
    • (1994) FASEB J , vol.8 , pp. 823-831
    • Raghow, R.1
  • 28
    • 23444447845 scopus 로고    scopus 로고
    • The collagen superfamily: from the extracellular matrix to the cell membrane
    • Ricard-Blum S., Ruggiero F. The collagen superfamily: from the extracellular matrix to the cell membrane. Pathol Biol (Paris) 2005, 53:430-442.
    • (2005) Pathol Biol (Paris) , vol.53 , pp. 430-442
    • Ricard-Blum, S.1    Ruggiero, F.2
  • 31
    • 33745808765 scopus 로고    scopus 로고
    • Transforming growth factor beta: a central modulator of pulmonary and airway inflammation and fibrosis
    • Sheppard D. Transforming growth factor beta: a central modulator of pulmonary and airway inflammation and fibrosis. Proc Am Thorac Soc 2006, 3:413-417.
    • (2006) Proc Am Thorac Soc , vol.3 , pp. 413-417
    • Sheppard, D.1
  • 32
    • 14644409764 scopus 로고    scopus 로고
    • Expression of type IV collagen and laminin at the interface between epithelial cells and fibroblasts from human periodontal ligament
    • Shimonishi M., Sato J., Takahashi N., Komatsu M. Expression of type IV collagen and laminin at the interface between epithelial cells and fibroblasts from human periodontal ligament. Eur J Oral Sci 2005, 113:34-40.
    • (2005) Eur J Oral Sci , vol.113 , pp. 34-40
    • Shimonishi, M.1    Sato, J.2    Takahashi, N.3    Komatsu, M.4
  • 33
    • 0018559403 scopus 로고
    • Collagen in scar formation
    • Shoshan S. Collagen in scar formation. Agents Actions Suppl 1979, 67-72.
    • (1979) Agents Actions Suppl , pp. 67-72
    • Shoshan, S.1
  • 34
    • 0025107487 scopus 로고
    • Determination of 4-hydroxyproline in collagen by gas chromatography/mass spectrometry
    • Tredget E.E., Falk N., Scott P.G., Hogg A.M., Burke J.F. Determination of 4-hydroxyproline in collagen by gas chromatography/mass spectrometry. Anal Biochem 1990, 190:259-265.
    • (1990) Anal Biochem , vol.190 , pp. 259-265
    • Tredget, E.E.1    Falk, N.2    Scott, P.G.3    Hogg, A.M.4    Burke, J.F.5
  • 35
    • 0034757168 scopus 로고    scopus 로고
    • Collagen-receptor signaling in health and disease
    • Vogel W.F. Collagen-receptor signaling in health and disease. Eur J Dermatol 2001, 11:506-514.
    • (2001) Eur J Dermatol , vol.11 , pp. 506-514
    • Vogel, W.F.1
  • 36
    • 0027548091 scopus 로고
    • Expression of type III and IV procollagen, prolyl 4-hydroxylase mRNAs in fibrotic human liver
    • Yamada H., Aida T., Taguchi K., Asano G. Expression of type III and IV procollagen, prolyl 4-hydroxylase mRNAs in fibrotic human liver. Nippon Rinsho 1993, 51:423-427.
    • (1993) Nippon Rinsho , vol.51 , pp. 423-427
    • Yamada, H.1    Aida, T.2    Taguchi, K.3    Asano, G.4
  • 37
    • 0037309642 scopus 로고    scopus 로고
    • DNase I-hypersensitive sites enhance alpha1(I) collagen gene expression in hepatic stellate cells
    • Yata Y., Scanga A., Gillan A., Yang L., Reif S., Breindl M., et al. DNase I-hypersensitive sites enhance alpha1(I) collagen gene expression in hepatic stellate cells. Hepatology 2003, 37:267-276.
    • (2003) Hepatology , vol.37 , pp. 267-276
    • Yata, Y.1    Scanga, A.2    Gillan, A.3    Yang, L.4    Reif, S.5    Breindl, M.6
  • 38
    • 0029044820 scopus 로고
    • Increased types I and III collagen and transforming growth factor-beta 1 mRNA and protein in hypertrophic burn scar
    • Zhang K., Garner W., Cohen L., Rodriguez J., Phan S. Increased types I and III collagen and transforming growth factor-beta 1 mRNA and protein in hypertrophic burn scar. J Invest Dermatol 1995, 104:750-754.
    • (1995) J Invest Dermatol , vol.104 , pp. 750-754
    • Zhang, K.1    Garner, W.2    Cohen, L.3    Rodriguez, J.4    Phan, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.