메뉴 건너뛰기




Volumn 258, Issue 1, 1998, Pages 1-18

Biochemistry of tropoelastin

Author keywords

Elastin; Extracellular matrix; Lysyl oxidase; Microfibril associated glycoprotein; Tropoelastin

Indexed keywords

ELASTIN; PROTEIN LYSINE 6 OXIDASE; TROPOELASTIN;

EID: 0032533711     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2580001.x     Document Type: Review
Times cited : (425)

References (233)
  • 1
    • 0242723637 scopus 로고
    • Regulation of extracellular matrix accumulation: A short review of elastin biosynthesis
    • Varner, J. E., ed. Liss, New York
    • Prosser, I. W. & Mecham, R. P. (1988) Regulation of extracellular matrix accumulation: a short review of elastin biosynthesis, in Self-assembling architecture (Varner, J. E., ed.) pp. 1-23, Liss, New York.
    • (1988) Self-assembling Architecture , pp. 1-23
    • Prosser, I.W.1    Mecham, R.P.2
  • 3
    • 0014465980 scopus 로고
    • The elastic fiber: I. The separation and partial characterization of its macromolecular components
    • Ross, R. & Bornstein, P. (1969) The elastic fiber: I. The separation and partial characterization of its macromolecular components, J. Cell Biol. 40, 366-381.
    • (1969) J. Cell Biol. , vol.40 , pp. 366-381
    • Ross, R.1    Bornstein, P.2
  • 5
    • 0024521529 scopus 로고
    • The protein components of the 12-nanometer microfibrils of elastic and nonelastic tissues
    • Gibson, M. A., Kumaratilake, J. S. & Cleary, E. G. (1989) The protein components of the 12-nanometer microfibrils of elastic and nonelastic tissues, J. Biol. Chem. 264, 4590-4598.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4590-4598
    • Gibson, M.A.1    Kumaratilake, J.S.2    Cleary, E.G.3
  • 6
    • 0023002893 scopus 로고
    • Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils
    • Sakai, L. Y., Keene, D. R. & Engvall, E. (1986) Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils, J. Cell Biol. 103, 2499-2509.
    • (1986) J. Cell Biol. , vol.103 , pp. 2499-2509
    • Sakai, L.Y.1    Keene, D.R.2    Engvall, E.3
  • 7
    • 0028267099 scopus 로고
    • Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices
    • Zhang, H., Apfelroth, S. D., Hu, W., Davis, E. C., Sanguinieti, C., Bonadio, J., Mecham, R. P. & Ramirez, F. (1994) Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices, J. Cell Biol. 124, 855-863.
    • (1994) J. Cell Biol. , vol.124 , pp. 855-863
    • Zhang, H.1    Apfelroth, S.D.2    Hu, W.3    Davis, E.C.4    Sanguinieti, C.5    Bonadio, J.6    Mecham, R.P.7    Ramirez, F.8
  • 8
    • 0025887137 scopus 로고
    • Complementary DNA cloning establishes microfibril-associated glycoprotein (MAGP) to be a discrete component of the elastin-associated microfibrils
    • Gibson, M. A., Sandberg, L. B., Grosso, L. E. & Cleary, E. G. (1991) Complementary DNA cloning establishes microfibril-associated glycoprotein (MAGP) to be a discrete component of the elastin-associated microfibrils, J. Biol. Chem. 266, 7596-7601.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7596-7601
    • Gibson, M.A.1    Sandberg, L.B.2    Grosso, L.E.3    Cleary, E.G.4
  • 9
    • 0030021441 scopus 로고    scopus 로고
    • Further characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25)
    • Gibson, M. A., Hatzinikolas, G., Kumaratilake, J. S., Sandberg, L. B., Nicholl, J. K., Sutherland, G. R. & Cleary, E. G. (1996) Further characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25), J. Biol. Chem. 271, 1096-1103.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1096-1103
    • Gibson, M.A.1    Hatzinikolas, G.2    Kumaratilake, J.S.3    Sandberg, L.B.4    Nicholl, J.K.5    Sutherland, G.R.6    Cleary, E.G.7
  • 10
    • 0023039150 scopus 로고
    • Ultrastructural immunolocalization of lysyl oxidase in vascular connective tissue
    • Kagan, H. M., Vaccaro, C. A., Bronson, R. E., Tang, S. S. & Brody, J. S. (1986) Ultrastructural immunolocalization of lysyl oxidase in vascular connective tissue, J. Cell. Biol. 103, 1121-1128.
    • (1986) J. Cell. Biol. , vol.103 , pp. 1121-1128
    • Kagan, H.M.1    Vaccaro, C.A.2    Bronson, R.E.3    Tang, S.S.4    Brody, J.S.5
  • 11
    • 0002616433 scopus 로고
    • The elastic fiber
    • (Hay, E. D., ed.) 2nd edn, Plenum Press, New York
    • Mecham, R. P. & Heuser, J. (1991) The elastic fiber, in Cell biology of the extracellular matrix (Hay, E. D., ed.) 2nd edn, pp. 79-109, Plenum Press, New York.
    • (1991) Cell Biology of the Extracellular Matrix , pp. 79-109
    • Mecham, R.P.1    Heuser, J.2
  • 13
    • 0027461783 scopus 로고
    • Emilin, a component of elastic fibers preferentially located at the elastin-microfibrils interface
    • Bressan, G. M., Daga-Gordini, D., Colombatti, A., Castellani, I., Mariga, V. & Volpin, D. (1993) Emilin, a component of elastic fibers preferentially located at the elastin-microfibrils interface, J. Cell Biol. 121, 201-212.
    • (1993) J. Cell Biol. , vol.121 , pp. 201-212
    • Bressan, G.M.1    Daga-Gordini, D.2    Colombatti, A.3    Castellani, I.4    Mariga, V.5    Volpin, D.6
  • 14
    • 0028961103 scopus 로고
    • The association of human fibulin-1 with elastic fibers: An immunohistological, ultrastructural, and RNA study
    • Roark, E. F., Keene, D. R., Haundenschild, C. C., Godyna, S., Little, C. D. & Argraves, W. S. (1995) The association of human fibulin-1 with elastic fibers: an immunohistological, ultrastructural, and RNA study, J. Histochem. Cytochem. 43, 401-411.
    • (1995) J. Histochem. Cytochem. , vol.43 , pp. 401-411
    • Roark, E.F.1    Keene, D.R.2    Haundenschild, C.C.3    Godyna, S.4    Little, C.D.5    Argraves, W.S.6
  • 15
    • 0024378486 scopus 로고
    • Isolation and characterization of a new 36-kDa microfibril-associated glycoprotein from porcine aorta
    • Kobayashi, R., Tashima, Y, Masuda, H., Shozawa, T., Numata, Y, Miyauchi, K. & Hayakawa, T. (1989) Isolation and characterization of a new 36-kDa microfibril-associated glycoprotein from porcine aorta, J. Biol. Chem. 264, 17437-17444.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17437-17444
    • Kobayashi, R.1    Tashima, Y.2    Masuda, H.3    Shozawa, T.4    Numata, Y.5    Miyauchi, K.6    Hayakawa, T.7
  • 16
    • 0026667717 scopus 로고
    • Characterization of an associated microfibril protein through recombinant DNA techniques
    • Horrigan, S. K., Rich, C. B., Streeton, B. W., Li, Z.-Y. & Foster, J. A. (1992) Characterization of an associated microfibril protein through recombinant DNA techniques, J. Biol. Chem. 267, 10087-10095.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10087-10095
    • Horrigan, S.K.1    Rich, C.B.2    Streeton, B.W.3    Li, Z.-Y.4    Foster, J.A.5
  • 18
    • 0018347149 scopus 로고
    • Biochemistry of the elastic fibers in normal connective tissues and its alterations in diseases
    • Uitto, J. (1979) Biochemistry of the elastic fibers in normal connective tissues and its alterations in diseases, J. Invest. Dermat. 72, 1-10.
    • (1979) J. Invest. Dermat. , vol.72 , pp. 1-10
    • Uitto, J.1
  • 19
    • 0018657591 scopus 로고
    • Studies on the evolution of elastin-I. Phylogenetic distribution
    • Sage, H. & Gray, W. R. (1979) Studies on the evolution of elastin-I. Phylogenetic distribution, Comp. Biochem. Physiol. 64B, 313-327.
    • (1979) Comp. Biochem. Physiol. , vol.64 B , pp. 313-327
    • Sage, H.1    Gray, W.R.2
  • 20
    • 0013598466 scopus 로고
    • The structure and physical properties of invertebrate and primitive vertebrate arteries
    • Davison, I. G., Wright, G. M. & DeMont, M. E. (1995) The structure and physical properties of invertebrate and primitive vertebrate arteries, J. Exp. Biol. 198, 2185-2196.
    • (1995) J. Exp. Biol. , vol.198 , pp. 2185-2196
    • Davison, I.G.1    Wright, G.M.2    DeMont, M.E.3
  • 22
    • 0030828688 scopus 로고    scopus 로고
    • A family of non-collagen-based cartilages in the skeleton of the sea lamprey, Petromyzon marinus
    • Robson, P., Wright, G. M., Youson, J. H. & Keeley, F. W. (1997) A family of non-collagen-based cartilages in the skeleton of the sea lamprey, Petromyzon marinus, Comp. Biochem. Physiol. 118S, 71-78.
    • (1997) Comp. Biochem. Physiol. , vol.118 S , pp. 71-78
    • Robson, P.1    Wright, G.M.2    Youson, J.H.3    Keeley, F.W.4
  • 23
    • 0030865952 scopus 로고    scopus 로고
    • Extensible collagen in mussel byssus: A natural block copolymer
    • Coyne, K. J., Qin, X.-X. & Waite, H. J. (1997) Extensible collagen in mussel byssus: a natural block copolymer, Science 277, 1830-1832.
    • (1997) Science , vol.277 , pp. 1830-1832
    • Coyne, K.J.1    Qin, X.-X.2    Waite, H.J.3
  • 24
    • 0018960146 scopus 로고
    • Studies on the evolution of elastin-II. Histology
    • Sage, H. & Gray, W. R. (1980) Studies on the evolution of elastin-II. Histology, Comp. Biochem. Physiol. 66B, 13-22.
    • (1980) Comp. Biochem. Physiol. , vol.66 B , pp. 13-22
    • Sage, H.1    Gray, W.R.2
  • 25
    • 0017429264 scopus 로고
    • Evolution of elastin structure
    • Sage, H. & Gray, W. R. (1977) Evolution of elastin structure. Adv. Exp. Med. Biol. 79, 291-309.
    • (1977) Adv. Exp. Med. Biol. , vol.79 , pp. 291-309
    • Sage, H.1    Gray, W.R.2
  • 26
    • 0019967302 scopus 로고
    • Structure-function relationships in the evolution of elastin
    • Sage, H. (1982) Structure-function relationships in the evolution of elastin, J. Invest. Dermat. 79 (Suppl. 1), 146S-153S.
    • (1982) J. Invest. Dermat. , vol.79 , Issue.1 SUPPL.
    • Sage, H.1
  • 27
    • 0025880719 scopus 로고
    • Mammalian tropoelastin: Multiple domains of the protein define an evolutionarily divergent amino acid sequence
    • Boyd, C. C., Christiano, A. M., Pierce, R. A., Stolle, C. A. & Deak, S. B. (1991) Mammalian tropoelastin: multiple domains of the protein define an evolutionarily divergent amino acid sequence, Matrix 11, 235-241.
    • (1991) Matrix , vol.11 , pp. 235-241
    • Boyd, C.C.1    Christiano, A.M.2    Pierce, R.A.3    Stolle, C.A.4    Deak, S.B.5
  • 28
    • 0019491077 scopus 로고
    • Elastin structure, biosynthesis, and relation to disease states
    • Sandberg, L. B., Soskel, N. T. & Leslie, J. C. (1981) Elastin structure, biosynthesis, and relation to disease states, N. Engl. J. Med. 304, 566-579.
    • (1981) N. Engl. J. Med. , vol.304 , pp. 566-579
    • Sandberg, L.B.1    Soskel, N.T.2    Leslie, J.C.3
  • 29
    • 0026659229 scopus 로고
    • Buschke-Ollendorff syndrome associated with elevated elastin production by affected skin fibroblasts in culture
    • Giro, M. G., Duvic, M., Smith, L. T., Kennedy, R., Rapini, R., Arnett, F. C. & Davidson, J. M. (1992) Buschke-Ollendorff syndrome associated with elevated elastin production by affected skin fibroblasts in culture, J. Invest. Dermatol 99, 129-137.
    • (1992) J. Invest. Dermatol , vol.99 , pp. 129-137
    • Giro, M.G.1    Duvic, M.2    Smith, L.T.3    Kennedy, R.4    Rapini, R.5    Arnett, F.C.6    Davidson, J.M.7
  • 30
    • 0028985994 scopus 로고
    • Transforming growth factor-β reverses a posttranscriptional defect in elastin synthesis in a cutis laxa skin fibroblast strain
    • Zhang, M-C, Giro, M. G., Quaglino, D. Jr & Davidson, J. M. (1995) Transforming growth factor-β reverses a posttranscriptional defect in elastin synthesis in a cutis laxa skin fibroblast strain, J. Clin. Invest. 95, 986-994.
    • (1995) J. Clin. Invest. , vol.95 , pp. 986-994
    • Zhang, M.-C.1    Giro, M.G.2    Quaglino Jr., D.3    Davidson, J.M.4
  • 33
    • 0028852659 scopus 로고
    • Mutations in the human gene for fibrillin-1 (FBN1) in the Marfan syndrome and related disorders
    • Dietz, H. C. & Pyeritz, R. E. (1995) Mutations in the human gene for fibrillin-1 (FBN1) in the Marfan syndrome and related disorders, Hum. Mol. Genet. 4, 1799-1809.
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 1799-1809
    • Dietz, H.C.1    Pyeritz, R.E.2
  • 34
    • 0027446365 scopus 로고
    • Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase
    • Vulpe, C., Levinson, B., Whitney, S., Packman, S. & Gitschier, J. (1993) Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase, Nature Genet. 3, 7-13.
    • (1993) Nature Genet. , vol.3 , pp. 7-13
    • Vulpe, C.1    Levinson, B.2    Whitney, S.3    Packman, S.4    Gitschier, J.5
  • 35
    • 0028047232 scopus 로고
    • Exclusion of an elastin gene (ELN) mutation as the cause of pseudoxanthoma elasticum (PXE) in one family
    • Raybould, M. C., Birley, A. J., Moss, C., Hultén, M. & McKeown, C. M. E. (1994) Exclusion of an elastin gene (ELN) mutation as the cause of pseudoxanthoma elasticum (PXE) in one family, Clin. Genet. 45,48-51.
    • (1994) Clin. Genet. , vol.45 , pp. 48-51
    • Raybould, M.C.1    Birley, A.J.2    Moss, C.3    Hultén, M.4    McKeown, C.M.E.5
  • 38
    • 0028294413 scopus 로고
    • Supravalvular aortic stenosis associated with a deletion disrupting the elastin gene
    • Ewart, A. K., Jin, W., Atkinson, D., Morris, C. A. & Keating, M. T. (1994) Supravalvular aortic stenosis associated with a deletion disrupting the elastin gene, J. Clin. Invest. 93, 1071 -1077.
    • (1994) J. Clin. Invest. , vol.93 , pp. 1071-1077
    • Ewart, A.K.1    Jin, W.2    Atkinson, D.3    Morris, C.A.4    Keating, M.T.5
  • 40
    • 0028075998 scopus 로고
    • Molecular pathology of the elastic fibers
    • Christiano, A. M. & Uitto, J. (1994) Molecular pathology of the elastic fibers, J Invest. Dermal 103 (Suppl. 5), 53S-57S.
    • (1994) J Invest. Dermal , vol.103 , Issue.5 SUPPL.
    • Christiano, A.M.1    Uitto, J.2
  • 43
    • 0027403375 scopus 로고
    • The elastin gene is disrupted by a translocation associated with supravalvular aortic stenosis
    • Curran, M. E., Atkinson, D. L., Ewart, A. K., Morris, C. A., Leppert, M. F. & Keating, M. T. (1993) The elastin gene is disrupted by a translocation associated with supravalvular aortic stenosis, Cell 73, 159-168.
    • (1993) Cell , vol.73 , pp. 159-168
    • Curran, M.E.1    Atkinson, D.L.2    Ewart, A.K.3    Morris, C.A.4    Leppert, M.F.5    Keating, M.T.6
  • 44
    • 0030752982 scopus 로고    scopus 로고
    • Elastin: Genomic structure and point mutations in patients with supravalvular aortic stenosis
    • Tassabehji, M., Metcalfe, K., Donnai, D., Hurst, J., Reardon, W., Burch, M. & Read, A. P. (1997) Elastin: genomic structure and point mutations in patients with supravalvular aortic stenosis, Hum. Mal. Genet. 6, 1029-1036.
    • (1997) Hum. Mal. Genet. , vol.6 , pp. 1029-1036
    • Tassabehji, M.1    Metcalfe, K.2    Donnai, D.3    Hurst, J.4    Reardon, W.5    Burch, M.6    Read, A.P.7
  • 48
    • 0027971976 scopus 로고
    • Elastinolytic metalloproteinases produced by human mononuclear phagocytes. Potential roles in destructive lung disease
    • Shapiro, S. D. (1994) Elastinolytic metalloproteinases produced by human mononuclear phagocytes. Potential roles in destructive lung disease. Am. J. Respir. Crit. Care Med. 150, S160-S164.
    • (1994) Am. J. Respir. Crit. Care Med. , vol.150
    • Shapiro, S.D.1
  • 50
    • 0023062132 scopus 로고
    • Structure of the 3′ region of the human elastin gene: Great abundance of Alu repetitive sequences and few coding sequences
    • Indik, Z., Yoon, K., Morrow, S. D., Cicila, G., Rosenbloom, J., Rosenbloom, J. & Ornstein-Goldstein, N. (1987) Structure of the 3′ region of the human elastin gene: great abundance of Alu repetitive sequences and few coding sequences. Connect. Tissue Res. 16, 197-211.
    • (1987) Connect. Tissue Res. , vol.16 , pp. 197-211
    • Indik, Z.1    Yoon, K.2    Morrow, S.D.3    Cicila, G.4    Rosenbloom, J.5    Rosenbloom, J.6    Ornstein-Goldstein, N.7
  • 51
    • 0023663346 scopus 로고
    • Repeating structure of chick tropoelastin revealed by complementary DNA cloning
    • Bressan, G. M., Argos, P. & Stanley, K. K. (1987) Repeating structure of chick tropoelastin revealed by complementary DNA cloning, Biochemistry 26, 1497-1503.
    • (1987) Biochemistry , vol.26 , pp. 1497-1503
    • Bressan, G.M.1    Argos, P.2    Stanley, K.K.3
  • 52
    • 0023664380 scopus 로고
    • Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones
    • Raju, K. & Anwar, R. A. (1987) Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones, J. Biol. Chem. 262, 5755-5762.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5755-5762
    • Raju, K.1    Anwar, R.A.2
  • 54
    • 0025130777 scopus 로고
    • Heterogeneity of rat tropoelastin mRNA revealed by cDNA cloning
    • Pierce, R. A., Deak, S. B., Stolle, C. A. & Boyd, C. D. (1990) Heterogeneity of rat tropoelastin mRNA revealed by cDNA cloning. Biochemistry 29, 9677-9683.
    • (1990) Biochemistry , vol.29 , pp. 9677-9683
    • Pierce, R.A.1    Deak, S.B.2    Stolle, C.A.3    Boyd, C.D.4
  • 58
    • 0027324732 scopus 로고
    • Oxidation, cross-linking, and insolubilization of recombinant tropoelastin by purified lysyl oxidase
    • Bedell-Hogan, D., Trackman, P., Abrams, W., Rosenbloom, J. & Kagan, H. (1993) Oxidation, cross-linking, and insolubilization of recombinant tropoelastin by purified lysyl oxidase, J. Biol Chem. 268, 10345-10350.
    • (1993) J. Biol Chem. , vol.268 , pp. 10345-10350
    • Bedell-Hogan, D.1    Trackman, P.2    Abrams, W.3    Rosenbloom, J.4    Kagan, H.5
  • 59
    • 0026690128 scopus 로고
    • Predictions of the secondary structure and antigenicity of human and bovine tropoelastins
    • Debelle, L., Wei, S. M., Jacob, M. P., Hornebeck, W. & Alix, A. J. P. (1992) Predictions of the secondary structure and antigenicity of human and bovine tropoelastins, Eur. J. Biophys. 21, 321-329.
    • (1992) Eur. J. Biophys. , vol.21 , pp. 321-329
    • Debelle, L.1    Wei, S.M.2    Jacob, M.P.3    Hornebeck, W.4    Alix, A.J.P.5
  • 63
    • 0027422979 scopus 로고
    • Extracellular matrix 4: The elastic fiber
    • Rosenbloom, J., Abrams, W. R. & Mecham, R. (1993) Extracellular matrix 4: the elastic fiber, FASEB J. 7, 1208-1218.
    • (1993) FASEB J. , vol.7 , pp. 1208-1218
    • Rosenbloom, J.1    Abrams, W.R.2    Mecham, R.3
  • 64
    • 0025424630 scopus 로고
    • Tropoelastin heterogeneity: Implications for protein function and disease
    • Parks, W. C. & Deak, S. B. (1990) Tropoelastin heterogeneity: implications for protein function and disease, Am. J. Respir. Cell Mol. Biol. 2, 399-406.
    • (1990) Am. J. Respir. Cell Mol. Biol. , vol.2 , pp. 399-406
    • Parks, W.C.1    Deak, S.B.2
  • 65
    • 0023887474 scopus 로고
    • Developmental regulation of tropoelastin isoforms
    • Parks, W. C., Secrist, H., Wu, L. C. & Mecham, R. P. (1988) Developmental regulation of tropoelastin isoforms, J. Biol. Chem. 263, 4416-4423.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4416-4423
    • Parks, W.C.1    Secrist, H.2    Wu, L.C.3    Mecham, R.P.4
  • 68
    • 0023251949 scopus 로고
    • Developmental initiation of elastin gene expression by human fetal skin fibroblasts
    • Sephel, G. C., Buckley, A. & Davidson, J. M. (1987) Developmental initiation of elastin gene expression by human fetal skin fibroblasts, J. Invest. Dermatol. 88, 732-735.
    • (1987) J. Invest. Dermatol. , vol.88 , pp. 732-735
    • Sephel, G.C.1    Buckley, A.2    Davidson, J.M.3
  • 69
    • 0020070306 scopus 로고
    • Regulation of elastin synthesis in developing sheep nuchal ligament by elastin mRNA levels
    • Davidson, J. M., Smith, K., Shibahara, S., Tolstoshev, P. & Crystal. R. G. (1982) Regulation of elastin synthesis in developing sheep nuchal ligament by elastin mRNA levels, J. Biol. Chem. 257, 747-754.
    • (1982) J. Biol. Chem. , vol.257 , pp. 747-754
    • Davidson, J.M.1    Smith, K.2    Shibahara, S.3    Tolstoshev, P.4    Crystal, R.G.5
  • 71
    • 0021040619 scopus 로고
    • Elastin synthesis during perinatal lung development in the rat
    • Myers, B., Dubick, M., Last, J. A. & Rucker, R. B. (1983) Elastin synthesis during perinatal lung development in the rat, Biochim. Biophys. Acta 761, 17-22.
    • (1983) Biochim. Biophys. Acta , vol.761 , pp. 17-22
    • Myers, B.1    Dubick, M.2    Last, J.A.3    Rucker, R.B.4
  • 72
    • 0019793316 scopus 로고
    • Differential expression of aortic and lung elastin genes during chick embryogenesis
    • Barrineau, L. L., Rich, C. B., Przybyla, A. & Foster, J. A. (1981) Differential expression of aortic and lung elastin genes during chick embryogenesis, Dev. Biol. 87, 46-51.
    • (1981) Dev. Biol. , vol.87 , pp. 46-51
    • Barrineau, L.L.1    Rich, C.B.2    Przybyla, A.3    Foster, J.A.4
  • 73
    • 0028270763 scopus 로고
    • Evidence for a cell-specific negative regulatory element in the first intron of the gene for bovine elastin
    • Munohar, A. & Anwar, R. A. (1994) Evidence for a cell-specific negative regulatory element in the first intron of the gene for bovine elastin, Biochem. J. 300, 147-152.
    • (1994) Biochem. J. , vol.300 , pp. 147-152
    • Munohar, A.1    Anwar, R.A.2
  • 75
    • 0025166317 scopus 로고
    • Regulation of elastin gene expression: Evidence for functional promoter activity in the 5′-flanking region of the human gene
    • Fazio, M. J., Kähäri, V.-M., Bashir, M. M., Saitta, B., Rosenbloom, J. & Uitt, J. (1990) Regulation of elastin gene expression: evidence for functional promoter activity in the 5′-flanking region of the human gene. J. Invest. Dermatol. 94, 191-196.
    • (1990) J. Invest. Dermatol. , vol.94 , pp. 191-196
    • Fazio, M.J.1    Kähäri, V.-M.2    Bashir, M.M.3    Saitta, B.4    Rosenbloom, J.5    Uitt, J.6
  • 76
    • 0028108458 scopus 로고
    • Evidence for the presence of a functional TATA box (ATAAAA) sequence in the gene for bovine elastin
    • Manohar, A. & Anwar, R. A. (1994) Evidence for the presence of a functional TATA box (ATAAAA) sequence in the gene for bovine elastin, Biochim. Biophys. Acta 1219, 233-236.
    • (1994) Biochim. Biophys. Acta , vol.1219 , pp. 233-236
    • Manohar, A.1    Anwar, R.A.2
  • 77
    • 0028321395 scopus 로고
    • Tissue-specific and developmentally regulated expression of human elastin promoter activity in transgenic mice
    • Hsu-Wong, S., Katchman, S. D., Ledo, I., Wu. M., Khillan, J., Bashir, M. M., Rosenbloom, J. & Uitto, J. (1994) Tissue-specific and developmentally regulated expression of human elastin promoter activity in transgenic mice, J. Biol. Chem. 269, 18072-18075.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18072-18075
    • Hsu-Wong, S.1    Katchman, S.D.2    Ledo, I.3    Wu, M.4    Khillan, J.5    Bashir, M.M.6    Rosenbloom, J.7    Uitto, J.8
  • 78
    • 0028858125 scopus 로고
    • Decreased elastin synthesis in normal development and in longterm aortic organ and cell cultures is related to rapid and selective destabilization of mRNA for elastin
    • Johnson, D. J., Robson, P., Hew, Y. & Keeley, F. W. (1995) Decreased elastin synthesis in normal development and in longterm aortic organ and cell cultures is related to rapid and selective destabilization of mRNA for elastin, Circ. Res. 74, 1107-1113.
    • (1995) Circ. Res. , vol.74 , pp. 1107-1113
    • Johnson, D.J.1    Robson, P.2    Hew, Y.3    Keeley, F.W.4
  • 79
    • 0026751072 scopus 로고
    • Transforming growth factor-β up-regulates elastin gene expression in human skin fibroblasts
    • Kähäri, V.-M., Olsen, D. R., Rhudy, R. W., Carrillo, P., Chen, Y. Q. & Uitto, J. (1992) Transforming growth factor-β up-regulates elastin gene expression in human skin fibroblasts, Lab. Invest. 66, 580-588.
    • (1992) Lab. Invest. , vol.66 , pp. 580-588
    • Kähäri, V.-M.1    Olsen, D.R.2    Rhudy, R.W.3    Carrillo, P.4    Chen, Y.Q.5    Uitto, J.6
  • 80
    • 0028167689 scopus 로고
    • Transforming growth factor-β up-regulates human elastin promoter activity in transgenic mice
    • Katchman, S. D., Hsu-Wong, S., Ledo, I., Wu, M. & Uitto, J. (1994) Transforming growth factor-β up-regulates human elastin promoter activity in transgenic mice, Biochem. Biophys. Res. Commun. 203, 485-490.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 485-490
    • Katchman, S.D.1    Hsu-Wong, S.2    Ledo, I.3    Wu, M.4    Uitto, J.5
  • 82
    • 0031182720 scopus 로고    scopus 로고
    • Exogenous and endogenous transforming growth factor-β influences elastin gene expression in cultured lung fibroblasts
    • McGowan, S. E., Jackson, S. K., Olson, P. J., Parekh, T. & Gold, L. I. (1997) Exogenous and endogenous transforming growth factor-β influences elastin gene expression in cultured lung fibroblasts. Am. J. Resp. Cell Mol. Biol. 17, 25-35.
    • (1997) Am. J. Resp. Cell Mol. Biol. , vol.17 , pp. 25-35
    • McGowan, S.E.1    Jackson, S.K.2    Olson, P.J.3    Parekh, T.4    Gold, L.I.5
  • 84
    • 0026667313 scopus 로고
    • 3 represses tropoelastin expression by a posttranslational mechanism
    • 3 represses tropoelastin expression by a posttranslational mechanism, J. Biol. Chem. 267, 11593-11599.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11593-11599
    • Pierce, R.A.1    Kolodziej, M.E.2    Parks, W.C.3
  • 85
    • 0027480761 scopus 로고
    • Human recombinant interleukin-1β up-regulates elastin gene expression in dermal fibroblasts
    • Mauviel, A., Chen, Y. Q., Kähäri, V.-M., Ledo, I., Wu, M., Rudnicka, L. & Uitto, J. (1993) Human recombinant interleukin-1β up-regulates elastin gene expression in dermal fibroblasts, J. Biol. Chem. 268, 6520-6524.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6520-6524
    • Mauviel, A.1    Chen, Y.Q.2    Kähäri, V.-M.3    Ledo, I.4    Wu, M.5    Rudnicka, L.6    Uitto, J.7
  • 86
    • 0025163596 scopus 로고
    • The regulation of lung elastin synthesis
    • Foster, J. A. & Curtiss, S. W. (1990) The regulation of lung elastin synthesis, Am. J. Physiol. 259, L13-L23.
    • (1990) Am. J. Physiol. , vol.259
    • Foster, J.A.1    Curtiss, S.W.2
  • 88
    • 0023696859 scopus 로고
    • Cloning of full-length elastin cDNAs from a human skin fibroblast recombinant cDNA library: Further elucidation of alternative splicing utilizing exon-specific oligonucleotides
    • Fazio, M. J., Olsen, D. R., Kauh, E. A., Baldwin, C. D., Indik, Z., Omstein-Goldstein, N., Yeh, H., Rosenbloom, J. & Uitto, J. (1988) Cloning of full-length elastin cDNAs from a human skin fibroblast recombinant cDNA library: further elucidation of alternative splicing utilizing exon-specific oligonucleotides, J. Invest. Dermatol. 91, 458-464.
    • (1988) J. Invest. Dermatol. , vol.91 , pp. 458-464
    • Fazio, M.J.1    Olsen, D.R.2    Kauh, E.A.3    Baldwin, C.D.4    Indik, Z.5    Omstein-Goldstein, N.6    Yeh, H.7    Rosenbloom, J.8    Uitto, J.9
  • 90
    • 0026518649 scopus 로고
    • Elements of the rat tropoelastin gene associated with alternative splicing
    • Pierce, R. A., Alatawi, A., Deak, S. B. & Boyd, C. D. (1992) Elements of the rat tropoelastin gene associated with alternative splicing, Genomics 12, 651-658.
    • (1992) Genomics , vol.12 , pp. 651-658
    • Pierce, R.A.1    Alatawi, A.2    Deak, S.B.3    Boyd, C.D.4
  • 91
    • 0023948122 scopus 로고
    • Isolation and characterization of human elastin cDNAs, and age-associated variation in elastin gene expression in cultured skin fibroblasts
    • Fazio, M. J., Olsen, D. R., Kuivaniemi, H., Chu, M.-L., Davidson, J. M. & Uitto, J. (1988) Isolation and characterization of human elastin cDNAs, and age-associated variation in elastin gene expression in cultured skin fibroblasts, Lab. Invest. 58, 270-277.
    • (1988) Lab. Invest. , vol.58 , pp. 270-277
    • Fazio, M.J.1    Olsen, D.R.2    Kuivaniemi, H.3    Chu, M.-L.4    Davidson, J.M.5    Uitto, J.6
  • 92
    • 0025933205 scopus 로고
    • Alternative splicing of rat tropoelastin mRNA is tissue-specific and developmentally regulated
    • Heim, R. A., Pierce, R. A., Deak, S. B., Riley, D. J., Boyd, C. D. & Stolle, C. A. (1991) Alternative splicing of rat tropoelastin mRNA is tissue-specific and developmentally regulated, Matrix 11, 359-366.
    • (1991) Matrix , vol.11 , pp. 359-366
    • Heim, R.A.1    Pierce, R.A.2    Deak, S.B.3    Riley, D.J.4    Boyd, C.D.5    Stolle, C.A.6
  • 94
    • 0024548534 scopus 로고
    • Characterization of rat heart tropoelastin
    • Rich, C. B. & Foster, J. A. (1989) Characterization of rat heart tropoelastin, Arch. Biochem. Biophys. 268, 551-558.
    • (1989) Arch. Biochem. Biophys. , vol.268 , pp. 551-558
    • Rich, C.B.1    Foster, J.A.2
  • 95
    • 0026574306 scopus 로고
    • Cellular expression of tropoelastin mRNA splice variants
    • Parks, W. C., Roby, J. D., Wu, L. C. & Grosso, L. E. (1992) Cellular expression of tropoelastin mRNA splice variants. Matrix 12, 156-162.
    • (1992) Matrix , vol.12 , pp. 156-162
    • Parks, W.C.1    Roby, J.D.2    Wu, L.C.3    Grosso, L.E.4
  • 96
    • 0021225342 scopus 로고
    • Elastin biosynthesis in chick-embryo arteries. Studies on the intracellular site of synthesis of tropoelastin
    • Saunders, N. A. & Grant, M. E. (1984) Elastin biosynthesis in chick-embryo arteries. Studies on the intracellular site of synthesis of tropoelastin, Biochem. J. 221, 393-400.
    • (1984) Biochem. J. , vol.221 , pp. 393-400
    • Saunders, N.A.1    Grant, M.E.2
  • 98
    • 0022405859 scopus 로고
    • The secretion of tropoelastin by chick-embryo artery cells
    • Saunders, N. A. & Grant, M. E. (1985) The secretion of tropoelastin by chick-embryo artery cells, Biochem. J. 230, 217-225.
    • (1985) Biochem. J. , vol.230 , pp. 217-225
    • Saunders, N.A.1    Grant, M.E.2
  • 99
    • 0030063331 scopus 로고    scopus 로고
    • Selective degradation of accumulated secretory proteins in the endoplasmic reticulum. A possible clearance pathway for abnormal tropoelastin
    • Davis, E. C. & Mecham, R. P. (1996) Selective degradation of accumulated secretory proteins in the endoplasmic reticulum. A possible clearance pathway for abnormal tropoelastin, J. Biol. Chem. 271, 3787-3794.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3787-3794
    • Davis, E.C.1    Mecham, R.P.2
  • 100
    • 0031015625 scopus 로고    scopus 로고
    • Effects of monensin on tropoelastin metabolism in vascular smooth muscle cells: Monensin causes intracellular degradation of accumulated tropoelastin
    • Ikeda, K., Wachi, H., Seyama, Y. & Tajima, S. (1997) Effects of monensin on tropoelastin metabolism in vascular smooth muscle cells: monensin causes intracellular degradation of accumulated tropoelastin, J. Biochem. 121, 5-7.
    • (1997) J. Biochem. , vol.121 , pp. 5-7
    • Ikeda, K.1    Wachi, H.2    Seyama, Y.3    Tajima, S.4
  • 101
    • 0020357126 scopus 로고
    • Kinetics of the incorporation of tropoelastin into elastic fibers in embryonic chick aorta
    • Kao, W. W., Bressan, G. M. & Prockop, D. J. (1982) Kinetics of the incorporation of tropoelastin into elastic fibers in embryonic chick aorta, Connect. Tissue Res. 10, 263-274.
    • (1982) Connect. Tissue Res. , vol.10 , pp. 263-274
    • Kao, W.W.1    Bressan, G.M.2    Prockop, D.J.3
  • 102
    • 0017228713 scopus 로고
    • Biosynthesis and secretion of tropoelastin by chick aorta cells
    • Rosenbloom, J. & Cywinski, A. (1976) Biosynthesis and secretion of tropoelastin by chick aorta cells, Biochem. Biophys. Res. Commun. 69, 613-620.
    • (1976) Biochem. Biophys. Res. Commun. , vol.69 , pp. 613-620
    • Rosenbloom, J.1    Cywinski, A.2
  • 103
    • 0017106401 scopus 로고
    • Synthesis of elastin and procollagen by cells from embryonic aorta
    • Uitto, J., Hoffmann, H. & Prockop, D. J. (1976) Synthesis of elastin and procollagen by cells from embryonic aorta, Arch. Bio-chem. Biophys. 173, 187-200.
    • (1976) Arch. Bio-chem. Biophys. , vol.173 , pp. 187-200
    • Uitto, J.1    Hoffmann, H.2    Prockop, D.J.3
  • 104
    • 0017175055 scopus 로고
    • Inhibition of proline hy droxylation does not inhibit secretion of tropoelastin by chick aorta cells
    • Rosenbloom, J. & Cywinski, A. (1976) Inhibition of proline hy droxylation does not inhibit secretion of tropoelastin by chick aorta cells, FEBS Lett. 65, 246-250.
    • (1976) FEBS Lett. , vol.65 , pp. 246-250
    • Rosenbloom, J.1    Cywinski, A.2
  • 105
    • 0017432748 scopus 로고
    • Studies on the action of lysyl oxidase on soluble elastin
    • Narayanan, A. S., Page, R. C. & Kuzan, F. (1977) Studies on the action of lysyl oxidase on soluble elastin, Adv. Exp. Med. biol. 79, 491-508.
    • (1977) Adv. Exp. Med. Biol. , vol.79 , pp. 491-508
    • Narayanan, A.S.1    Page, R.C.2    Kuzan, F.3
  • 106
    • 0021336907 scopus 로고
    • Effect of varying amounts of ascorbate on collagen, elastin and lysyl oxidase synthesis in aortic smooth muscle cell cultures
    • Faris, B., Ferrera, R., Toselli, P., Nambu, J., Gonnerman, W. A. & Franzblau, C. (1984) Effect of varying amounts of ascorbate on collagen, elastin and lysyl oxidase synthesis in aortic smooth muscle cell cultures, Biochim. Biophys. Acta 797. 71-75.
    • (1984) Biochim. Biophys. Acta , vol.797 , pp. 71-75
    • Faris, B.1    Ferrera, R.2    Toselli, P.3    Nambu, J.4    Gonnerman, W.A.5    Franzblau, C.6
  • 107
    • 0021838127 scopus 로고
    • Role of selected nutrients in synthesis, accumulation, and chemical modification of connective tissue proteins
    • Tinker, D. & Rucker, R. B. (1985) Role of selected nutrients in synthesis, accumulation, and chemical modification of connective tissue proteins, Physiol. Rev. 65, 607-657.
    • (1985) Physiol. Rev. , vol.65 , pp. 607-657
    • Tinker, D.1    Rucker, R.B.2
  • 109
    • 0031016656 scopus 로고    scopus 로고
    • Ascorbate differentially regulates elastin and collagen biosynthesis in vascular smooth muscle cells and skin fibroblasts by pretranslational mechanisms
    • Davidson, J. M., LuValle, P. A., Zoia, O., Quaglino, D. Jr & Giro. M. G. (1997) Ascorbate differentially regulates elastin and collagen biosynthesis in vascular smooth muscle cells and skin fibroblasts by pretranslational mechanisms, J. Biol. Chem. 272, 345-352.
    • (1997) J. Biol. Chem. , vol.272 , pp. 345-352
    • Davidson, J.M.1    LuValle, P.A.2    Zoia, O.3    Quaglino Jr., D.4    Giro, M.G.5
  • 111
    • 0017332120 scopus 로고
    • Synthesis of elastin in aortas from chick embryos. Conversion of newly secreted elastin to cross-linked elastin without apparent proteolysis of the molecule
    • Bressan, G. M. & Prockop, D. J. (1977) Synthesis of elastin in aortas from chick embryos. Conversion of newly secreted elastin to cross-linked elastin without apparent proteolysis of the molecule, Biochemistry 16, 1406-1412.
    • (1977) Biochemistry , vol.16 , pp. 1406-1412
    • Bressan, G.M.1    Prockop, D.J.2
  • 112
    • 0013835523 scopus 로고
    • Fine fibrils of extracellular space (microfibrils). Their structure and role in connective tissue organization
    • Haust, M. D. (1965) Fine fibrils of extracellular space (microfibrils). Their structure and role in connective tissue organization. Am. J. Pathol. 47, 1113-1137.
    • (1965) Am. J. Pathol. , vol.47 , pp. 1113-1137
    • Haust, M.D.1
  • 113
    • 0013807177 scopus 로고
    • Elastogenesis in human aorta: An electron microscopic study
    • Haust, M. D., More, R. H., Bencosme, S. A. & Balis, J. U. (1965) Elastogenesis in human aorta: an electron microscopic study, Exp. Mol. Pathol. 4, 508-524.
    • (1965) Exp. Mol. Pathol. , vol.4 , pp. 508-524
    • Haust, M.D.1    More, R.H.2    Bencosme, S.A.3    Balis, J.U.4
  • 114
    • 0015239894 scopus 로고
    • Studies on the nature of the 'microfibrillar' component of elasticfibers
    • Robert, B., Szigeti, M., Derouette, J. C. & Robert, L. (1971) Studies on the nature of the 'microfibrillar' component of elasticfibers, Eur. J. Biochem. 21, 507-516.
    • (1971) Eur. J. Biochem. , vol.21 , pp. 507-516
    • Robert, B.1    Szigeti, M.2    Derouette, J.C.3    Robert, L.4
  • 115
    • 0026379091 scopus 로고
    • Elastin synthesis and fiber assembly
    • Mecham, R. P. (1991) Elastin synthesis and fiber assembly. Ann. N.Y. Acad. Sci. 624, 137-146.
    • (1991) Ann. N.Y. Acad. Sci. , vol.624 , pp. 137-146
    • Mecham, R.P.1
  • 116
    • 0027396755 scopus 로고
    • The ductus arteriosis migratory smooth muscle cell phenotype processes tropoelastin to a 52 kDa product associated with impaired assembly of elasticlaminae
    • Hinek, A. & Rabinovitch, M. (1993) The ductus arteriosis migratory smooth muscle cell phenotype processes tropoelastin to a 52 kDa product associated with impaired assembly of elasticlaminae, J. Biol Chem. 268, 1405-1413.
    • (1993) J. Biol Chem. , vol.268 , pp. 1405-1413
    • Hinek, A.1    Rabinovitch, M.2
  • 117
    • 0026641004 scopus 로고
    • The cysteine residues in the carboxy terminal domain of tropoelastin form an intrachain disulfide bond that stabilizes a loop structure and positively charged pocket
    • Brown, P., Mecham, L., Tisdale, C. & Mecham, R. P. (1992) The cysteine residues in the carboxy terminal domain of tropoelastin form an intrachain disulfide bond that stabilizes a loop structure and positively charged pocket, Biochem. Biophys. Res. Commun. 186, 549-555.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 549-555
    • Brown, P.1    Mecham, L.2    Tisdale, C.3    Mecham, R.P.4
  • 120
    • 0029811144 scopus 로고    scopus 로고
    • Functional domains on elastin and microfibril-associated glycoprotein involved in elastic fibre assembly
    • Brown-Augsburger, P., Broekelmann, T., Rosenbloom, J. & Mecham, R. P. (1996) Functional domains on elastin and microfibril-associated glycoprotein involved in elastic fibre assembly. Biochem. J. 318, 149-155.
    • (1996) Biochem. J. , vol.318 , pp. 149-155
    • Brown-Augsburger, P.1    Broekelmann, T.2    Rosenbloom, J.3    Mecham, R.P.4
  • 121
    • 0030930661 scopus 로고    scopus 로고
    • Microfibril-associated glycoprotein-1 (MAGP-1) binds to the pepsin-resistant domain of the α3(VI) chain of type VI collagen
    • Finnis, M. L. & Gibson, M. A. (1997) Microfibril-associated glycoprotein-1 (MAGP-1) binds to the pepsin-resistant domain of the α3(VI) chain of type VI collagen, J. Biol. Chem 272, 22817-22823.
    • (1997) J. Biol. Chem , vol.272 , pp. 22817-22823
    • Finnis, M.L.1    Gibson, M.A.2
  • 124
    • 0030447195 scopus 로고    scopus 로고
    • Microfibril-associated glycoprotein-1 (MAGP-1) is specifically located on the beads of the beaded-filament structure for fibrillin-containing microfibrils as visualised by the rotary shadowing technique
    • Henderson, M., Polewski, R., Fanning, T. C. & Gibson, M. A. (1996) Microfibril-associated glycoprotein-1 (MAGP-1) is specifically located on the beads of the beaded-filament structure for fibrillin-containing microfibrils as visualised by the rotary shadowing technique. J. Histochem. Cytochem. 44, 1389-1397.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 1389-1397
    • Henderson, M.1    Polewski, R.2    Fanning, T.C.3    Gibson, M.A.4
  • 125
    • 0023947632 scopus 로고
    • In vitro processing of tropoelastin: Investigation of a possible transport function associated with the carboxy-terminal domain
    • Grosso, L. E. & Mecham, R. P. (1988) In vitro processing of tropoelastin: investigation of a possible transport function associated with the carboxy-terminal domain, Biochem. Biophys. Res. Commun. 153, 545-551.
    • (1988) Biochem. Biophys. Res. Commun. , vol.153 , pp. 545-551
    • Grosso, L.E.1    Mecham, R.P.2
  • 126
    • 0023938183 scopus 로고
    • The elastin receptor: A galactoside-binding protein
    • Hinek, A., Wrenn, D. S., Mecham, R. P. & Barondes, S. H. (1988) The elastin receptor: a galactoside-binding protein, Science 239, 1539-1541.
    • (1988) Science , vol.239 , pp. 1539-1541
    • Hinek, A.1    Wrenn, D.S.2    Mecham, R.P.3    Barondes, S.H.4
  • 128
    • 0032513204 scopus 로고    scopus 로고
    • The 67-kDa enzymatically inactive alternatively spliced variant of β-galactosidase is identical to the elastin/laminin-binding protein
    • Privitera, S., Prody, C. A., Callahan, J. W. & Hinek, A. (1998) The 67-kDa enzymatically inactive alternatively spliced variant of β-galactosidase is identical to the elastin/laminin-binding protein, J. Biol. Chem. 273, 6319-6326.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6319-6326
    • Privitera, S.1    Prody, C.A.2    Callahan, J.W.3    Hinek, A.4
  • 129
    • 0027479052 scopus 로고
    • The 67-kD elastin/laminin-binding protein is related to an enzymatically inactive, alternatively spliced form of β-galactosidase
    • Hinek, A., Rabinovitch, M., Keeley, F., Okamura-Oho, Y. & Callahan, J. (1993) The 67-kD elastin/laminin-binding protein is related to an enzymatically inactive, alternatively spliced form of β-galactosidase, J. Clin. Invest. 91, 1198-1205.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1198-1205
    • Hinek, A.1    Rabinovitch, M.2    Keeley, F.3    Okamura-Oho, Y.4    Callahan, J.5
  • 130
    • 0026332784 scopus 로고
    • Impaired elastin fiber assembly related to reduced 67-kD elastinbinding protein in fetal lamb ductus arteriosus and in cultured aortic smooth muscle cells treated with chondroitin sulfate
    • Hinek, A., Mecham, R. P., Keeley, F. & Rabinovitch, M. (1991) Impaired elastin fiber assembly related to reduced 67-kD elastinbinding protein in fetal lamb ductus arteriosus and in cultured aortic smooth muscle cells treated with chondroitin sulfate, J. Clin. Invest. 88, 2083-2094.
    • (1991) J. Clin. Invest. , vol.88 , pp. 2083-2094
    • Hinek, A.1    Mecham, R.P.2    Keeley, F.3    Rabinovitch, M.4
  • 131
    • 0025805986 scopus 로고
    • Ligand affinity of the 67 kDa elastin/laminin binding protein is modulated by the protein's lectin domain: Visualization of elastin/laminin-receptor complexes with gold-tagged ligands
    • Mecham, R. P., Whitehouse, L., Hay, M., Hinek, A. & Sheetz, M. P. (1991) Ligand affinity of the 67 kDa elastin/laminin binding protein is modulated by the protein's lectin domain: visualization of elastin/laminin-receptor complexes with gold-tagged ligands, J. Cell Biol. 113, 187-194.
    • (1991) J. Cell Biol. , vol.113 , pp. 187-194
    • Mecham, R.P.1    Whitehouse, L.2    Hay, M.3    Hinek, A.4    Sheetz, M.P.5
  • 132
    • 0027717916 scopus 로고
    • Peptide sequences selected by BA4, a tropoelastin-specific monoclonal antibody, are ligands for the 67-kilodalton bovine elastin receptor
    • Grosso, L. E. & Scott, M. (1993) Peptide sequences selected by BA4, a tropoelastin-specific monoclonal antibody, are ligands for the 67-kilodalton bovine elastin receptor, Biochemistry 32, 13369-13374.
    • (1993) Biochemistry , vol.32 , pp. 13369-13374
    • Grosso, L.E.1    Scott, M.2
  • 133
    • 0028263645 scopus 로고
    • 67-kD elastin binding protein is a protective 'companion' of extracellular insoluble elastin and intracellular tropoelastin
    • Hinek, A. & Rabinovitch, M. (1994) 67-kD elastin binding protein is a protective 'companion' of extracellular insoluble elastin and intracellular tropoelastin, J. Cell Biol. 126, 563-574.
    • (1994) J. Cell Biol. , vol.126 , pp. 563-574
    • Hinek, A.1    Rabinovitch, M.2
  • 134
    • 0029089501 scopus 로고
    • Recycling of the 67-kDa elastin binding protein in arterial monocytes is imperative for secretion of tropoelastin
    • Hinek, A., Keeley, F. W. & Callahan, J. (1995) Recycling of the 67-kDa elastin binding protein in arterial monocytes is imperative for secretion of tropoelastin, Exp. Cell Res. 220, 312-324.
    • (1995) Exp. Cell Res. , vol.220 , pp. 312-324
    • Hinek, A.1    Keeley, F.W.2    Callahan, J.3
  • 137
    • 0032567714 scopus 로고    scopus 로고
    • Identification of tropoelastin as a ligand for the 65-kd FK506-binding protein, FKBP65, in the secretory pathway
    • Davis, E. C., Broekelmann, T. J., Ozawa, Y. & Mecham, R. P. (1998) Identification of tropoelastin as a ligand for the 65-kd FK506-binding protein, FKBP65, in the secretory pathway, J. Cell Biol. 140, 295-303.
    • (1998) J. Cell Biol. , vol.140 , pp. 295-303
    • Davis, E.C.1    Broekelmann, T.J.2    Ozawa, Y.3    Mecham, R.P.4
  • 138
    • 0023953406 scopus 로고
    • Entropic elastic processes in protein mechanisms I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics
    • Urry, D. W. (1988) Entropic elastic processes in protein mechanisms I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics, J. Protein Chem. 7, 1-34.
    • (1988) J. Protein Chem. , vol.7 , pp. 1-34
    • Urry, D.W.1
  • 139
    • 0029110869 scopus 로고
    • Elastic biomolecular machines
    • Urry, D. W. (1995) Elastic biomolecular machines. Sci. Am. 272, 44-49.
    • (1995) Sci. Am. , vol.272 , pp. 44-49
    • Urry, D.W.1
  • 140
    • 0018256199 scopus 로고
    • Molecular perspectives of vascular wall structure and disease: The elastic component
    • Urry, D. W. (1978) Molecular perspectives of vascular wall structure and disease: the elastic component, Perspect. Biol. Med. 21, 265-295.
    • (1978) Perspect. Biol. Med. , vol.21 , pp. 265-295
    • Urry, D.W.1
  • 142
    • 0014689359 scopus 로고
    • Coacervation of solubilized elastin effects a notable conformational change
    • Urry, D. W., Starchier, B. & Partridge, S. M. (1969) Coacervation of solubilized elastin effects a notable conformational change, Nature 222, 795-796.
    • (1969) Nature , vol.222 , pp. 795-796
    • Urry, D.W.1    Starchier, B.2    Partridge, S.M.3
  • 143
    • 0015852026 scopus 로고
    • Coacervation and ion-binding studies on aortic elastin
    • Starcher, B. C., Saccoman, G. & Urry, D. W. (1973) Coacervation and ion-binding studies on aortic elastin, Biochim. Biophys. Acta 310, 481-486.
    • (1973) Biochim. Biophys. Acta , vol.310 , pp. 481-486
    • Starcher, B.C.1    Saccoman, G.2    Urry, D.W.3
  • 144
    • 0015967414 scopus 로고
    • Coacervation of tropoelastin results in fiber formation
    • Cox, B. A., Starcher, B. C. & Urry, D. W. (1974) Coacervation of tropoelastin results in fiber formation, J. Biol. Chem. 249, 997-998.
    • (1974) J. Biol. Chem. , vol.249 , pp. 997-998
    • Cox, B.A.1    Starcher, B.C.2    Urry, D.W.3
  • 147
    • 0017064531 scopus 로고
    • Optical diffraction of tropoelastin and α-elastin coacervates
    • Volpin, D., Urry, D, W., Cox, B. A. & Gotte, L. (1976) Optical diffraction of tropoelastin and α-elastin coacervates. Biochim. Biophys. Acta 439, 253-258.
    • (1976) Biochim. Biophys. Acta , vol.439 , pp. 253-258
    • Volpin, D.1    Urry, D.W.2    Cox, B.A.3    Gotte, L.4
  • 148
    • 0016181437 scopus 로고
    • The synthetic polypentapeptide of elastin coacervates and forms filamentous aggregates
    • Urry, D. W., Long, M. M., Cox, B. A., Ohnishi, T., Mitchell, L. W. & Jacobs, M. (1974) The synthetic polypentapeptide of elastin coacervates and forms filamentous aggregates, Biochim. Biophys. Acta 371, 597-602.
    • (1974) Biochim. Biophys. Acta , vol.371 , pp. 597-602
    • Urry, D.W.1    Long, M.M.2    Cox, B.A.3    Ohnishi, T.4    Mitchell, L.W.5    Jacobs, M.6
  • 149
    • 0016966143 scopus 로고
    • Conformations of the repeat peptides of elastin in solution: An application of proton and carbon-13 magnetic resonance to the determination of polypeptide secondary structure
    • Urry, D. W. & Long, M. M. (1976) Conformations of the repeat peptides of elastin in solution: an application of proton and carbon-13 magnetic resonance to the determination of polypeptide secondary structure, CRC Crit. Rev. Biochem. 4, 1-45.
    • (1976) CRC Crit. Rev. Biochem. , vol.4 , pp. 1-45
    • Urry, D.W.1    Long, M.M.2
  • 150
    • 0017869984 scopus 로고
    • Coacervation of sequential polypeptide models of tropoelastin
    • Rapaka, R. S. & Urry, D. W. (1978) Coacervation of sequential polypeptide models of tropoelastin. Int. J. Pept. Protein Res. 11, 97-108.
    • (1978) Int. J. Pept. Protein Res. , vol.11 , pp. 97-108
    • Rapaka, R.S.1    Urry, D.W.2
  • 151
    • 0023605829 scopus 로고
    • Lysyl oxidase activity and elastin/glycosaminoglycan interactions in growing chick and rat aortas
    • Fornieri, C., Baccarani-Contri, M., Quaglino, D. Jr & Pasquali-Ronchetti, I. (1987) Lysyl oxidase activity and elastin/glycosaminoglycan interactions in growing chick and rat aortas, J. Cell Biol. 105, 1463-1469.
    • (1987) J. Cell Biol. , vol.105 , pp. 1463-1469
    • Fornieri, C.1    Baccarani-Contri, M.2    Quaglino Jr., D.3    Pasquali-Ronchetti, I.4
  • 152
    • 0030809954 scopus 로고    scopus 로고
    • Coacervation characteristics of recombinant human tropoelastin
    • Vrhovski, B., Jensen, S. & Weiss, A. S. (1997) Coacervation characteristics of recombinant human tropoelastin, Eur. J. Biochem. 250, 92-98.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 92-98
    • Vrhovski, B.1    Jensen, S.2    Weiss, A.S.3
  • 154
    • 0020021572 scopus 로고
    • Characterization of soluble peptides of elastin by physical techniques
    • Urry, D. W. (1982) Characterization of soluble peptides of elastin by physical techniques, Methods Enzymot. 82, 673-716.
    • (1982) Methods Enzymot. , vol.82 , pp. 673-716
    • Urry, D.W.1
  • 155
    • 0001728735 scopus 로고
    • Protein elasticity based on conformations of sequential polypeptides: The biological elastic fiber
    • Urry, D. W. (1984) Protein elasticity based on conformations of sequential polypeptides: the biological elastic fiber, J. Protein Chem. 3, 403-436.
    • (1984) J. Protein Chem. , vol.3 , pp. 403-436
    • Urry, D.W.1
  • 156
    • 0026643352 scopus 로고
    • Enzymatic and nonenzymatic cross-linking of collagen and elastin
    • Reiser, K., McCormick, R. J. & Rucker, R. B. (1992) Enzymatic and nonenzymatic cross-linking of collagen and elastin, FASEB J. 6, 2439-2449.
    • (1992) FASEB J. , vol.6 , pp. 2439-2449
    • Reiser, K.1    McCormick, R.J.2    Rucker, R.B.3
  • 157
    • 0020018910 scopus 로고
    • Lysyl oxidase: Preparation and role in elastin biosynthesis
    • Kagan, H. M. & Sullivan, K. A. (1982) Lysyl oxidase: preparation and role in elastin biosynthesis, Methods Enzymol. 82, 637-650.
    • (1982) Methods Enzymol. , vol.82 , pp. 637-650
    • Kagan, H.M.1    Sullivan, K.A.2
  • 159
    • 0020017230 scopus 로고
    • Isolation of soluble elastin from copper-deficient chick aorta
    • Rucker, R. B. (1982) Isolation of soluble elastin from copper-deficient chick aorta. Methods Enzymol. 82, 650-657.
    • (1982) Methods Enzymol. , vol.82 , pp. 650-657
    • Rucker, R.B.1
  • 160
    • 0020018047 scopus 로고
    • Production and isolation of soluble elastin from copper-deficient swine
    • Sandberg, L. B. & Wolt, T. B. (1982) Production and isolation of soluble elastin from copper-deficient swine. Methods Enzymol. 82, 657-665.
    • (1982) Methods Enzymol. , vol.82 , pp. 657-665
    • Sandberg, L.B.1    Wolt, T.B.2
  • 161
    • 0016721367 scopus 로고
    • Isolation of soluble elastin from lathyritic chicks. Comparison to tropoelastin from copper deficient pigs
    • Foster, J. A., Shapiro, R., Vaynow, P., Crombie, G. & Faris, B. (1975) Isolation of soluble elastin from lathyritic chicks. Comparison to tropoelastin from copper deficient pigs, Biochemistry 14, 5343-5347.
    • (1975) Biochemistry , vol.14 , pp. 5343-5347
    • Foster, J.A.1    Shapiro, R.2    Vaynow, P.3    Crombie, G.4    Faris, B.5
  • 162
    • 0020018048 scopus 로고
    • Isolation of soluble elastinlathyrism
    • Rich, C. B. & Foster, J. A. (1982) Isolation of soluble elastinlathyrism, Methods Enzymol. 82, 665-673.
    • (1982) Methods Enzymol. , vol.82 , pp. 665-673
    • Rich, C.B.1    Foster, J.A.2
  • 163
  • 166
    • 0029051024 scopus 로고
    • Identification of an elastin cross-linking domain that joins three peptide chains
    • Brown-Augsburger, P., Tisdale, C., Broekelmann, T., Sloan, C. & Mecham, R. P. (1995) Identification of an elastin cross-linking domain that joins three peptide chains, J. Biol. Chem. 270, 17778-17783.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17778-17783
    • Brown-Augsburger, P.1    Tisdale, C.2    Broekelmann, T.3    Sloan, C.4    Mecham, R.P.5
  • 173
    • 0020049070 scopus 로고
    • Studies in cutaneous aging: I. The elastic fiber network
    • Braverman, I. M. & Fonferko, E. (1982) Studies in cutaneous aging: I. The elastic fiber network, J. Invest. Dermatol. 78, 434-443.
    • (1982) J. Invest. Dermatol. , vol.78 , pp. 434-443
    • Braverman, I.M.1    Fonferko, E.2
  • 174
    • 0021646130 scopus 로고
    • Elastin metabolism and chemistry: Potential roles in lung development and structure
    • Rucker, R. B. & Dubick, M. A. (1984) Elastin metabolism and chemistry: potential roles in lung development and structure, Environ. Health Perspect. 55, 179-191.
    • (1984) Environ. Health Perspect. , vol.55 , pp. 179-191
    • Rucker, R.B.1    Dubick, M.A.2
  • 176
    • 0024268511 scopus 로고
    • Repair of protease-damaged elastin in neonatal rat aortic smooth muscle cell cultures
    • Stone, P. J., Morris, S. M., Martin, B. M., McMahon, M. P., Faris, B. & Franzblau, C. (1988) Repair of protease-damaged elastin in neonatal rat aortic smooth muscle cell cultures, J. Clin. Invest. 82, 1644-1654.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1644-1654
    • Stone, P.J.1    Morris, S.M.2    Martin, B.M.3    McMahon, M.P.4    Faris, B.5    Franzblau, C.6
  • 177
    • 0030029583 scopus 로고    scopus 로고
    • Tropoelastin gene expression in individual vascular smooth muscle cells. Relationship to DNA synthesis during vascular development and after arterial injury
    • Belknap, J. K., Grieshaber, N. A., Schwartz, P. E., Orton, E. C., Reidy, M. A. & Majack, R. A. (1996) Tropoelastin gene expression in individual vascular smooth muscle cells. Relationship to DNA synthesis during vascular development and after arterial injury, Circ. Res. 78, 388-394.
    • (1996) Circ. Res. , vol.78 , pp. 388-394
    • Belknap, J.K.1    Grieshaber, N.A.2    Schwartz, P.E.3    Orton, E.C.4    Reidy, M.A.5    Majack, R.A.6
  • 179
    • 0021340337 scopus 로고
    • Isolation of tropoelastin a from lathyritic chick aortae
    • Rich, C. B. & Foster, J. A. (1984) Isolation of tropoelastin a from lathyritic chick aortae, Biochem. J. 217, 581-584.
    • (1984) Biochem. J. , vol.217 , pp. 581-584
    • Rich, C.B.1    Foster, J.A.2
  • 181
    • 0029026513 scopus 로고
    • Presence of elastinrelated 45 kDa fragment in culture medium: Specific cleavage product of tropoelastin in vascular smooth muscle cell culture
    • Hayashi, A., Wachi, H. & Tajima, S. (1995) Presence of elastinrelated 45 kDa fragment in culture medium: specific cleavage product of tropoelastin in vascular smooth muscle cell culture, Biochim. Biophys. Acta 1244, 325-330.
    • (1995) Biochim. Biophys. Acta , vol.1244 , pp. 325-330
    • Hayashi, A.1    Wachi, H.2    Tajima, S.3
  • 182
    • 0017086040 scopus 로고
    • Intrinsic enzyme activity associated with tropoelastin
    • Mecham, R. P., Foster, J. A. & Franzblau, C. (1976) Intrinsic enzyme activity associated with tropoelastin, Biochim. Biophys. Acta 446, 245-254.
    • (1976) Biochim. Biophys. Acta , vol.446 , pp. 245-254
    • Mecham, R.P.1    Foster, J.A.2    Franzblau, C.3
  • 183
    • 0017691476 scopus 로고
    • Trypsin-like neutral protease associated with soluble elastin
    • Mecham, R. P. & Foster, J. A. (1977) Trypsin-like neutral protease associated with soluble elastin, Biochemistry 16, 3825-3831.
    • (1977) Biochemistry , vol.16 , pp. 3825-3831
    • Mecham, R.P.1    Foster, J.A.2
  • 184
    • 0028945002 scopus 로고
    • Total synthesis and expression in Escherichia coli of a gene encoding human tropoelastin
    • Martin, S. L., Vrhovski, B. & Weiss, A. S. (1995) Total synthesis and expression in Escherichia coli of a gene encoding human tropoelastin, Gene 154, 159-166.
    • (1995) Gene , vol.154 , pp. 159-166
    • Martin, S.L.1    Vrhovski, B.2    Weiss, A.S.3
  • 185
    • 0022580180 scopus 로고
    • Role of plasma and serum proteases in the degradation of elastin
    • Romero, N., Tinker, D., Hyde, D. & Rucker, R. B. (1986) Role of plasma and serum proteases in the degradation of elastin, Arch. Biochem. Biophys. 244, 161-168.
    • (1986) Arch. Biochem. Biophys. , vol.244 , pp. 161-168
    • Romero, N.1    Tinker, D.2    Hyde, D.3    Rucker, R.B.4
  • 186
    • 0028301228 scopus 로고
    • Serum-induced vascular smooth muscle cell elastolytic activity through tyrosine kinase intracellular signalling
    • Kobayashi, J., Wigle, D., Childs, T., Zhu, L., Keeley, F. W. & Rabinovitch, M. (1994) Serum-induced vascular smooth muscle cell elastolytic activity through tyrosine kinase intracellular signalling, J. Cell. Physiol. 160, 121-131.
    • (1994) J. Cell. Physiol. , vol.160 , pp. 121-131
    • Kobayashi, J.1    Wigle, D.2    Childs, T.3    Zhu, L.4    Keeley, F.W.5    Rabinovitch, M.6
  • 187
    • 0029915363 scopus 로고    scopus 로고
    • Serine proteinase inhibitors influence the stability of tropoelastin mRNA in neonatal rat lung fibroblast cultures
    • McGowan, S. E., Lui, R., Harvey, C. S. & Jaeckel, E. C. (1996) Serine proteinase inhibitors influence the stability of tropoelastin mRNA in neonatal rat lung fibroblast cultures, Am. J. Physiol. 270, L376-L385.
    • (1996) Am. J. Physiol. , vol.270
    • McGowan, S.E.1    Lui, R.2    Harvey, C.S.3    Jaeckel, E.C.4
  • 188
    • 0025146214 scopus 로고
    • Pulmonary fibroblasts: An in vitro model of emphysema. Regulation of elastin gene expression
    • Foster, J. A., Rich, C. B. & Miller, M. F. (1990) Pulmonary fibroblasts: an in vitro model of emphysema. Regulation of elastin gene expression, J. Biol. Chem. 265, 15544-15549.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15544-15549
    • Foster, J.A.1    Rich, C.B.2    Miller, M.F.3
  • 189
    • 0027283014 scopus 로고
    • PGAIPG, a repeated hexapeptide of bovine and human tropoelastin, is chemotactic for neutrophils and Lewis lung carcinoma cells
    • Grosso, L. E. & Scott, M. (1993) PGAIPG, a repeated hexapeptide of bovine and human tropoelastin, is chemotactic for neutrophils and Lewis lung carcinoma cells, Arch. Biochem. Biophys. 305, 401-404.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 401-404
    • Grosso, L.E.1    Scott, M.2
  • 191
    • 0029056536 scopus 로고
    • Stimulation of cell proliferation and autoregulation of elastin expression by elastin peptide VPGVG in cultured chick vascular smooth muscle cells
    • Wachi, H., Seyama, Y., Yamashita, S., Suganami, H., Uemura, Y., Okamoto, K., Yamada, H. & Tajima, S. (1995) Stimulation of cell proliferation and autoregulation of elastin expression by elastin peptide VPGVG in cultured chick vascular smooth muscle cells, FEBS Lett. 368, 215-219.
    • (1995) FEBS Lett. , vol.368 , pp. 215-219
    • Wachi, H.1    Seyama, Y.2    Yamashita, S.3    Suganami, H.4    Uemura, Y.5    Okamoto, K.6    Yamada, H.7    Tajima, S.8
  • 192
    • 0017444981 scopus 로고
    • Recent observations on the structure and composition of elastin
    • Gotte, L. (1977) Recent observations on the structure and composition of elastin, Adv. Exp. Med. Biol. 79, 105-116.
    • (1977) Adv. Exp. Med. Biol. , vol.79 , pp. 105-116
    • Gotte, L.1
  • 195
    • 0024988663 scopus 로고
    • Three-dimensional organization of extracellular matrix in elastic cartilage as viewed by quick freeze, deep etch electron microscopy
    • Mecham, R. P. & Heuser, J. (1990) Three-dimensional organization of extracellular matrix in elastic cartilage as viewed by quick freeze, deep etch electron microscopy. Connect. Tissue Res. 24, 83-93.
    • (1990) Connect. Tissue Res. , vol.24 , pp. 83-93
    • Mecham, R.P.1    Heuser, J.2
  • 196
    • 0018424687 scopus 로고
    • The ultrastructure of elastin revealed by freeze-fracture electron microscopy
    • Pasquali-Ronchetti, I., Fornieri, C., Baccarani-Contri, M. & Volpin, D. (1979) The ultrastructure of elastin revealed by freeze-fracture electron microscopy, Micron 10, 89-99.
    • (1979) Micron , vol.10 , pp. 89-99
    • Pasquali-Ronchetti, I.1    Fornieri, C.2    Baccarani-Contri, M.3    Volpin, D.4
  • 199
    • 0001676342 scopus 로고
    • Optical spectroscopic determination of bovine tropoelastin molecular model
    • Debelle, L. & Alix, A. J. P. (1995) Optical spectroscopic determination of bovine tropoelastin molecular model, J. Mol. Struct. 348, 321-324.
    • (1995) J. Mol. Struct. , vol.348 , pp. 321-324
    • Debelle, L.1    Alix, A.J.P.2
  • 200
    • 0028874868 scopus 로고
    • Bovine elastin and κ-elastin secondary structure determination by optical spectroscopies
    • Debelle, L., Alix, A. J. P., Jacob, M. P., Huvenne, J., Berjot, M., Sombret, B. & Legrand, P. (1995) Bovine elastin and κ-elastin secondary structure determination by optical spectroscopies, J. Biol. Chem. 270, 26099-26103.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26099-26103
    • Debelle, L.1    Alix, A.J.P.2    Jacob, M.P.3    Huvenne, J.4    Berjot, M.5    Sombret, B.6    Legrand, P.7
  • 201
    • 0014949231 scopus 로고
    • New molecular model for the long-range elasticity of elastin
    • Weis-Fogh, T. & Andersen, S. O. (1970) New molecular model for the long-range elasticity of elastin, Nature 227, 718 -721.
    • (1970) Nature , vol.227 , pp. 718-721
    • Weis-Fogh, T.1    Andersen, S.O.2
  • 203
    • 0017849526 scopus 로고
    • Hydrophobic interaction and a model for the elasticity of elastin
    • Gosline, J. M. (1978) Hydrophobic interaction and a model for the elasticity of elastin, Biopolymers 17, 677-695.
    • (1978) Biopolymers , vol.17 , pp. 677-695
    • Gosline, J.M.1
  • 204
    • 0016168148 scopus 로고
    • The elastic properties of elastin
    • Hoeve, C. A. J. & Flory, P. J. (1974) The elastic properties of elastin, Biopolymers 13, 677-686.
    • (1974) Biopolymers , vol.13 , pp. 677-686
    • Hoeve, C.A.J.1    Flory, P.J.2
  • 205
    • 0011944583 scopus 로고
    • Metabolism of collagen and elastin
    • Florkin, M., ed. Elsevier, Amsterdam
    • Bailey, A. J. & Etherington, D. J. (1980) Metabolism of collagen and elastin, in Comprehensive Biochemistry, vol. 19B part 1 (Florkin, M., ed.), pp. 299-459, Elsevier, Amsterdam.
    • (1980) Comprehensive Biochemistry , vol.19 B , Issue.1 PART , pp. 299-459
    • Bailey, A.J.1    Etherington, D.J.2
  • 206
    • 0019289928 scopus 로고
    • The elastic properties of rubber-like proteins and highly extensible tissues
    • Gosline, J. M. (1980) The elastic properties of rubber-like proteins and highly extensible tissues, Symp. Soc. Exp. Biol. 34, 331-357.
    • (1980) Symp. Soc. Exp. Biol. , vol.34 , pp. 331-357
    • Gosline, J.M.1
  • 207
    • 0019142643 scopus 로고
    • Optical properties of single elastin fibres indicate random protein conformation
    • Aaron, B. B. & Gosline, J. M. (1980) Optical properties of single elastin fibres indicate random protein conformation. Nature 287, 865-867.
    • (1980) Nature , vol.287 , pp. 865-867
    • Aaron, B.B.1    Gosline, J.M.2
  • 208
    • 0016795899 scopus 로고
    • Mechanical state of elastin
    • Dorrington, K. L., Grut, W. & McCrum, N. G. (1975) Mechanical state of elastin, Nature 255, 476-478.
    • (1975) Nature , vol.255 , pp. 476-478
    • Dorrington, K.L.1    Grut, W.2    McCrum, N.G.3
  • 209
    • 0018294163 scopus 로고
    • Dynamic mechanical properties of elastin
    • Gosline, J. M. & French, C. J. (1979) Dynamic mechanical properties of elastin, Biopolymers 18, 2091-2103.
    • (1979) Biopolymers , vol.18 , pp. 2091-2103
    • Gosline, J.M.1    French, C.J.2
  • 210
    • 0023353716 scopus 로고
    • Raman spectrum and structure of elastin in relation to Type-II β-turns
    • Prescott, B., Renugopalakrishnan, V. & Thomas, G. J. (1987) Raman spectrum and structure of elastin in relation to Type-II β-turns, Biopolymers 26, 934-936.
    • (1987) Biopolymers , vol.26 , pp. 934-936
    • Prescott, B.1    Renugopalakrishnan, V.2    Thomas, G.J.3
  • 212
    • 0017818044 scopus 로고
    • The temperature-dependent swelling of elastin
    • Gosline, J. M. (1978) The temperature-dependent swelling of elastin, Biopolymers 17, 697-707.
    • (1978) Biopolymers , vol.17 , pp. 697-707
    • Gosline, J.M.1
  • 213
    • 0025325403 scopus 로고
    • The effects of hydration on the dynamic mechanical properties of elastin
    • Lillie, M. A. & Gosline, J. M. (1990) The effects of hydration on the dynamic mechanical properties of elastin, Biopolymers 29, 1147-1160.
    • (1990) Biopolymers , vol.29 , pp. 1147-1160
    • Lillie, M.A.1    Gosline, J.M.2
  • 214
    • 36949043812 scopus 로고
    • Thermoelasticity of elastin
    • Volpin, D. & Ciferri, A. (1970) Thermoelasticity of elastin. Nature 225, 382
    • (1970) Nature , vol.225 , pp. 382
    • Volpin, D.1    Ciferri, A.2
  • 215
    • 0017105762 scopus 로고
    • The physical properties of elastic tissues
    • Gosline, J. M. (1976) The physical properties of elastic tissues, Int. Rev. Connect, Tissue Res. 7, 211-249.
    • (1976) Int. Rev. Connect, Tissue Res. , vol.7 , pp. 211-249
    • Gosline, J.M.1
  • 216
    • 0015932437 scopus 로고
    • Molecular model for elastin structure and function
    • Gray, W. R., Sandberg, L. B. & Foster, J. A. (1973) Molecular model for elastin structure and function, Nature 246, 461-466.
    • (1973) Nature , vol.246 , pp. 461-466
    • Gray, W.R.1    Sandberg, L.B.2    Foster, J.A.3
  • 217
    • 0016007798 scopus 로고
    • Arterial mesenchyme and arteriosclerosis. Studies on the conformation and interactions of elastin
    • Urry, D. W. (1974) Arterial mesenchyme and arteriosclerosis. Studies on the conformation and interactions of elastin, Adv. Exp. Med. Biol. 43, 211-243.
    • (1974) Adv. Exp. Med. Biol. , vol.43 , pp. 211-243
    • Urry, D.W.1
  • 218
    • 0016309331 scopus 로고
    • Circular dichroism and absorption of the polytetrapeptide of elastin: A polymer model for the β-turn
    • Urry, D. W., Long, M. M., Ohnishi, T. & Jacobs, M. (1974) Circular dichroism and absorption of the polytetrapeptide of elastin: a polymer model for the β-turn, Biochem. Biophys. Res. Commun. 61, 1427-1483.
    • (1974) Biochem. Biophys. Res. Commun. , vol.61 , pp. 1427-1483
    • Urry, D.W.1    Long, M.M.2    Ohnishi, T.3    Jacobs, M.4
  • 219
    • 0017444462 scopus 로고
    • On the conformation, coacervation and function of polymeric models of elastin
    • Urry, D. W. & Long, M. M. (1977) On the conformation, coacervation and function of polymeric models of elastin, Adv. Exp. Med. Biol. 79, 685-714.
    • (1977) Adv. Exp. Med. Biol. , vol.79 , pp. 685-714
    • Urry, D.W.1    Long, M.M.2
  • 220
    • 0025343528 scopus 로고
    • Synthetic fragments and analogues of elastin II. Conformational studies
    • Tamburro, A. M., Guantieri, V., Pandolfo, L. & Scopa, A. (1990) Synthetic fragments and analogues of elastin II. Conformational studies, Biopolymers 29, 855-870.
    • (1990) Biopolymers , vol.29 , pp. 855-870
    • Tamburro, A.M.1    Guantieri, V.2    Pandolfo, L.3    Scopa, A.4
  • 223
    • 0017421493 scopus 로고
    • The coacervate-sol transition observed with α-elastin and its N-formyl O-methyl derivative
    • Partridge, S. M. & Whiting, A. H. (1977) The coacervate-sol transition observed with α-elastin and its N-formyl O-methyl derivative, Adv. Exp. Med. Biol 79, 715-721.
    • (1977) Adv. Exp. Med. Biol , vol.79 , pp. 715-721
    • Partridge, S.M.1    Whiting, A.H.2
  • 224
    • 0022263575 scopus 로고
    • Polypentapeptide of elastin: Temperature dependence and correlation with elastomeric force
    • Urry, D. W., Show, R. G. & Prasad, K. U. (1985) Polypentapeptide of elastin: temperature dependence and correlation with elastomeric force. Biochem. Biophys. Res. Commun. 130, 50-57.
    • (1985) Biochem. Biophys. Res. Commun. , vol.130 , pp. 50-57
    • Urry, D.W.1    Show, R.G.2    Prasad, K.U.3
  • 225
    • 0015522986 scopus 로고
    • Preparation and properties of salt-soluble elastin
    • Smith, D. W., Brown, D. M. & Carnes, W, H. (1972) Preparation and properties of salt-soluble elastin, J. Biol. Chem. 247, 2427-2432.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2427-2432
    • Smith, D.W.1    Brown, D.M.2    Carnes, W.H.3
  • 226
    • 0016299847 scopus 로고
    • Molecular weight heterogeneity of tropoelastin resulting from proteolysis during preparation
    • Narayanan, A. S. & Page, R. C. (1974) Molecular weight heterogeneity of tropoelastin resulting from proteolysis during preparation, FEBS Lett. 44, 59-62.
    • (1974) FEBS Lett. , vol.44 , pp. 59-62
    • Narayanan, A.S.1    Page, R.C.2
  • 227
    • 0016654523 scopus 로고
    • Tropoelastin purification: Improvements using enzyme inhibitors
    • Sandherg, L. B., Bruenger, E. & Cleary, E. G. (1974) Tropoelastin purification: improvements using enzyme inhibitors, Anal. Biochem. 64, 249-254.
    • (1974) Anal. Biochem. , vol.64 , pp. 249-254
    • Sandherg, L.B.1    Bruenger, E.2    Cleary, E.G.3
  • 228
    • 0025965333 scopus 로고
    • Fibroblast adhesion to recombinant tropoelastin expressed as a protein-A fusion protein
    • Grosso, L. E., Parks, W. C., Wu, L. & Mecham, R. P. (1991) Fibroblast adhesion to recombinant tropoelastin expressed as a protein-A fusion protein, Biochem. J. 273, 517-522.
    • (1991) Biochem. J. , vol.273 , pp. 517-522
    • Grosso, L.E.1    Parks, W.C.2    Wu, L.3    Mecham, R.P.4
  • 229
    • 0025274806 scopus 로고
    • Studies on the formation, separation, and characterization of cyanogen bromide fragments of human AI apolipoprotein
    • Morrison, J. R., Fidge, N. H. & Grego, B. (1990) Studies on the formation, separation, and characterization of cyanogen bromide fragments of human AI apolipoprotein, Anal. Biochem. 186, 145-152.
    • (1990) Anal. Biochem. , vol.186 , pp. 145-152
    • Morrison, J.R.1    Fidge, N.H.2    Grego, B.3
  • 230
    • 0025322996 scopus 로고
    • Production of recombinant human tropoelastin: Characterization and demonstration of immunologic and chemotactic activity
    • Indik, Z., Abrams, W. R., Kucich, U., Gibson, C. W., Mecham, R. P. & Rosenbloom, J. (1990) Production of recombinant human tropoelastin: characterization and demonstration of immunologic and chemotactic activity, Arch. Biochem. Biophys. 280, 80-86.
    • (1990) Arch. Biochem. Biophys. , vol.280 , pp. 80-86
    • Indik, Z.1    Abrams, W.R.2    Kucich, U.3    Gibson, C.W.4    Mecham, R.P.5    Rosenbloom, J.6
  • 231
    • 0030590845 scopus 로고    scopus 로고
    • Expression of active, human lysyl oxidase in Escherichia coli
    • Ouzzine, M., Boyd, A. & Hulmes, D. J. S. (1996) Expression of active, human lysyl oxidase in Escherichia coli. FEBS Lett. 399. 215-219.
    • (1996) FEBS Lett. , vol.399 , pp. 215-219
    • Ouzzine, M.1    Boyd, A.2    Hulmes, D.J.S.3
  • 232
  • 233
    • 0027672469 scopus 로고
    • Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome
    • Pereira, L., D'Alessio, M., Ramirez, F., Lynch, J. R., Sykes, B., Pangilinan, T. & Bonadio, J. (1993) Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome, Hum. Mol. Genet. 2, 961-968.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 961-968
    • Pereira, L.1    D'Alessio, M.2    Ramirez, F.3    Lynch, J.R.4    Sykes, B.5    Pangilinan, T.6    Bonadio, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.