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Volumn 275, Issue 5 44-5, 1998, Pages

Isolation of rat fibrillin-1 cDNA and its relevance in metanephric development

Author keywords

Complementary deoxyribonucleic acid cloning; Extracellular matrix; Fibrillin

Indexed keywords

COMPLEMENTARY DNA; EPIDERMAL GROWTH FACTOR; FIBRILLIN; FIBRILLIN 1; INTEGRIN; TRANSFORMING GROWTH FACTOR; UNCLASSIFIED DRUG;

EID: 0031788735     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.1998.275.5.f710     Document Type: Article
Times cited : (18)

References (43)
  • 2
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin, J. M., A. E. Przybyla, R. J. MacDonald, and W. J. Rutter. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 18: 5294-5299, 1979.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 3
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium isothiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. Single-step method of RNA isolation by acid guanidinium isothiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156-159, 1987.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 4
    • 0020973415 scopus 로고
    • Elastin associated microfibrils and microfibrillar proteins
    • Cleary, E. G., and M. A. Gibson. Elastin associated microfibrils and microfibrillar proteins. Int. Rev. Connect. Tiss. Res. 10: 97-209, 1983.
    • (1983) Int. Rev. Connect. Tiss. Res. , vol.10 , pp. 97-209
    • Cleary, E.G.1    Gibson, M.A.2
  • 5
    • 0027257818 scopus 로고
    • Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5′ end
    • Corson, G. M., S. C. Chalberg, H. C. Dietz, N. L. Charbonneau, and L. Y. Sakai. Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5′ end. Genomics 17: 476-484, 1993.
    • (1993) Genomics , vol.17 , pp. 476-484
    • Corson, G.M.1    Chalberg, S.C.2    Dietz, H.C.3    Charbonneau, N.L.4    Sakai, L.Y.5
  • 7
    • 0029912222 scopus 로고    scopus 로고
    • Extracellular matrix and cell adhesion molecules in nephrogenesis
    • Ekblom, P. Extracellular matrix and cell adhesion molecules in nephrogenesis. Exp. Nephrol. 4: 92-96, 1996.
    • (1996) Exp. Nephrol. , vol.4 , pp. 92-96
    • Ekblom, P.1
  • 8
    • 0025277746 scopus 로고
    • Molecular interactions between the protein products of neurogenic loci Notch and Delta, two EGF-homologous genes in Drosophila
    • Fehon, R. G., P. J. Kooh, I. Rebay, C. L. Regan, T. Xu, M. A. T. Muskavitch, and S. Artavanis-Tsakonas. Molecular interactions between the protein products of neurogenic loci Notch and Delta, two EGF-homologous genes in Drosophila. Cell 61: 523-534, 1990.
    • (1990) Cell , vol.61 , pp. 523-534
    • Fehon, R.G.1    Kooh, P.J.2    Rebay, I.3    Regan, C.L.4    Xu, T.5    Muskavitch, M.A.T.6    Artavanis-Tsakonas, S.7
  • 9
    • 0028857166 scopus 로고
    • Bovine latent transforming growth factor β1-binding protein 2: Molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils
    • Gibson, M. A., G. Hatzinikolas, E. C. Davis, E. Baker, G. R. Sutherland, and R. P. Mecham. Bovine latent transforming growth factor β1-binding protein 2: molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils. Mol. Cell. Biol. 15: 6932-6942, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6932-6942
    • Gibson, M.A.1    Hatzinikolas, G.2    Davis, E.C.3    Baker, E.4    Sutherland, G.R.5    Mecham, R.P.6
  • 10
    • 0024521529 scopus 로고
    • The protein components of the 12-nm microfibrils of elastic and nonelastic tissues
    • Gibson, M. A., J. A. Kumaratilake, and E. G. Cleary. The protein components of the 12-nm microfibrils of elastic and nonelastic tissues. J. Biol. Chem. 264: 4590-4598, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4590-4598
    • Gibson, M.A.1    Kumaratilake, J.A.2    Cleary, E.G.3
  • 11
    • 0025355882 scopus 로고
    • Analysis of cytokine mRNA and DNA: Detection and quantitation by competitive polymerase chain reaction
    • Gilliland, G., S. Perrin, K. Blanchard, and H. F. Bunn. Analysis of cytokine mRNA and DNA: detection and quantitation by competitive polymerase chain reaction. Proc. Natl. Acad. Sci. USA 87: 2725-2729, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2725-2729
    • Gilliland, G.1    Perrin, S.2    Blanchard, K.3    Bunn, H.F.4
  • 12
    • 0028931325 scopus 로고
    • The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1
    • Handford, P., A. K. Downing, Z. Rao, D. R. Hewett, B. C. Sykes, and C. M. Kielty. The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1. J. Biol. Chem. 270: 6751-6756, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6751-6756
    • Handford, P.1    Downing, A.K.2    Rao, Z.3    Hewett, D.R.4    Sykes, B.C.5    Kielty, C.M.6
  • 14
    • 0029036338 scopus 로고
    • Origin of the glomerular vasculature in the developing kidney
    • Hyink, D. P., and D. R. Abrahamson. Origin of the glomerular vasculature in the developing kidney. Semin. Nephrol. 15: 300-314, 1995.
    • (1995) Semin. Nephrol. , vol.15 , pp. 300-314
    • Hyink, D.P.1    Abrahamson, D.R.2
  • 16
    • 0030769298 scopus 로고    scopus 로고
    • Role of extracellular matrix, growth factors and proto-oncogenes in metanephric development
    • Kanwar, Y. S., F. A. Carone, A. Kumar, J. Wada, K. Ota, and E. I. Wallner. Role of extracellular matrix, growth factors and proto-oncogenes in metanephric development. Kidney Int. 52: 589-606, 1997.
    • (1997) Kidney Int. , vol.52 , pp. 589-606
    • Kanwar, Y.S.1    Carone, F.A.2    Kumar, A.3    Wada, J.4    Ota, K.5    Wallner, E.I.6
  • 17
    • 0028858380 scopus 로고
    • Cloning of mouse c-ros renal cDNA, its role in development and relationship to extracellular matrix glycoproteins
    • Kanwar, Y. S., Z. Z. Liu, A. Kumar, J. Wada, and F. A. Carone. Cloning of mouse c-ros renal cDNA, its role in development and relationship to extracellular matrix glycoproteins. Kidney Int. 48: 1646-1659, 1995.
    • (1995) Kidney Int. , vol.48 , pp. 1646-1659
    • Kanwar, Y.S.1    Liu, Z.Z.2    Kumar, A.3    Wada, J.4    Carone, F.A.5
  • 18
    • 0024459991 scopus 로고
    • The tissue distribution of microfibrils reacting with a monospecific antibody to MAGP, the major glycoprotein antigen of elastin-associated microfibrils
    • Kumaratilake, J. A., M. A. Gibson, J. C. Fanning, and E. G. Cleary. The tissue distribution of microfibrils reacting with a monospecific antibody to MAGP, the major glycoprotein antigen of elastin-associated microfibrils. Eur. J. Cell Biol. 50: 117-127, 1989.
    • (1989) Eur. J. Cell Biol. , vol.50 , pp. 117-127
    • Kumaratilake, J.A.1    Gibson, M.A.2    Fanning, J.C.3    Cleary, E.G.4
  • 19
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157: 105-132, 1982.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 22
    • 0021919480 scopus 로고
    • Rapid and sensitive protein similarity searches
    • Lipman, D. J., and W. R. Pearson. Rapid and sensitive protein similarity searches. Science 227: 1435-1441, 1985.
    • (1985) Science , vol.227 , pp. 1435-1441
    • Lipman, D.J.1    Pearson, W.R.2
  • 23
  • 25
    • 0001976617 scopus 로고    scopus 로고
    • Development and maturation of the kidney
    • edited by B. M. Brenner. Philadelphia, PA: Saunders
    • Nigam, S. K., A. Aperia, and B. M. Brenner. Development and maturation of the kidney. In: The Kidney, edited by B. M. Brenner. Philadelphia, PA: Saunders, 1996, p. 72-98.
    • (1996) The Kidney , pp. 72-98
    • Nigam, S.K.1    Aperia, A.2    Brenner, B.M.3
  • 26
  • 27
    • 0029665565 scopus 로고    scopus 로고
    • Fibrillin mutations in Marfan syndrome and related phenotypes
    • Ramirez, F. Fibrillin mutations in Marfan syndrome and related phenotypes. Curr. Opi. Gene. Dev. 6: 309-315, 1996.
    • (1996) Curr. Opi. Gene. Dev. , vol.6 , pp. 309-315
    • Ramirez, F.1
  • 30
    • 0027258592 scopus 로고
    • Mapping of nidogen binding sites for collagen type IV, heparan sulfate proteoglycan and zinc
    • Reinhardt, D. P., K. Mann, R. Nischt, J. W. Fox, M. Chu, T. Krieg, and R. Timpl. Mapping of nidogen binding sites for collagen type IV, heparan sulfate proteoglycan and zinc. J. Biol. Chem. 268: 10881-10887, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10881-10887
    • Reinhardt, D.P.1    Mann, K.2    Nischt, R.3    Fox, J.W.4    Chu, M.5    Krieg, T.6    Timpl, R.7
  • 32
    • 0028335948 scopus 로고
    • Anchorage dependence, integrins and apoptosis
    • Ruoslahti, E., and J. C. Reed. Anchorage dependence, integrins and apoptosis. Cell 77: 477-478, 1994.
    • (1994) Cell , vol.77 , pp. 477-478
    • Ruoslahti, E.1    Reed, J.C.2
  • 33
    • 0023002893 scopus 로고
    • Fibrillin, a new 350-kD glycoprotein is a component of extracellular microfibrils
    • Sakai, L. Y., R. K. Douglas, and E. Engvall. Fibrillin, a new 350-kD glycoprotein is a component of extracellular microfibrils. J. Cell Biol. 103: 2499-2509, 1986.
    • (1986) J. Cell Biol. , vol.103 , pp. 2499-2509
    • Sakai, L.Y.1    Douglas, R.K.2    Engvall, E.3
  • 34
    • 0029915120 scopus 로고    scopus 로고
    • Cell-type specific recognition of RGD- and Non-RGD-containing cell binding domains in fibrillin-1
    • Sakamoto, H., T. Broekelmann, D. A. Cheresh, F. Ramirez, J. Rosenblom, and R. P. Mecham. Cell-type specific recognition of RGD- and Non-RGD-containing cell binding domains in fibrillin-1. J. Biol. Chem. 271: 4916-4922, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4916-4922
    • Sakamoto, H.1    Broekelmann, T.2    Cheresh, D.A.3    Ramirez, F.4    Rosenblom, J.5    Mecham, R.P.6
  • 38
    • 0023056546 scopus 로고
    • Nucleotide sequence of a full-length cDNA for mouse cytoskeletal β-actin mRNA
    • Tokunaga, K., H. Taniguchi, K. Yoda, M. Shimizu, and S. Sakiyama. Nucleotide sequence of a full-length cDNA for mouse cytoskeletal β-actin mRNA. Nucleic Acid Res. 14: 2829-2832, 1986.
    • (1986) Nucleic Acid Res. , vol.14 , pp. 2829-2832
    • Tokunaga, K.1    Taniguchi, H.2    Yoda, K.3    Shimizu, M.4    Sakiyama, S.5
  • 41
    • 0030989330 scopus 로고    scopus 로고
    • Developmental regulation, expression, and apoptotic potential of galectin-9, a β-galactoside binding lectin
    • Wada, J., K. Ota, A. Kumar, E. I. Wallner, and Y. S. Kanwar. Developmental regulation, expression, and apoptotic potential of galectin-9, a β-galactoside binding lectin. J. Clin. Invest. 99: 2452-2461, 1997.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2452-2461
    • Wada, J.1    Ota, K.2    Kumar, A.3    Wallner, E.I.4    Kanwar, Y.S.5
  • 43
    • 0029023792 scopus 로고
    • Developmental expression of fibrillin genes suggests heterogeneity of extracellular microfibrills
    • Zhang, H., W. Hu, and F. Ramirez. Developmental expression of fibrillin genes suggests heterogeneity of extracellular microfibrills. J. Cell Biol. 129: 1165-1176, 1995.
    • (1995) J. Cell Biol. , vol.129 , pp. 1165-1176
    • Zhang, H.1    Hu, W.2    Ramirez, F.3


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