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Volumn 87, Issue 12, 2007, Pages 1195-1205

Role of aggregated medin in the pathogenesis of thoracic aortic aneurysm and dissection

Author keywords

Amyloid; Aneurysm; Dissection; Lactadherin; Medin; Thoracic aorta

Indexed keywords

AMYLOID; COLLAGEN; ELASTIN; GELATINASE A; LACTADHERIN; MEDIN PEPTIDE; OLIGOMER; PEPTIDE DERIVATIVE; PROTEINASE; UNCLASSIFIED DRUG;

EID: 36248940276     PISSN: 00236837     EISSN: 15300307     Source Type: Journal    
DOI: 10.1038/labinvest.3700679     Document Type: Article
Times cited : (38)

References (46)
  • 1
    • 0020513501 scopus 로고
    • The morphology of ascending aortic aneurysms
    • Klima T, Spjut HJ, Coelho A, et al. The morphology of ascending aortic aneurysms. Hum Pathol 1983;14:810-817.
    • (1983) Hum Pathol , vol.14 , pp. 810-817
    • Klima, T.1    Spjut, H.J.2    Coelho, A.3
  • 3
    • 8444243749 scopus 로고    scopus 로고
    • Increased tissue microarray matrix metalloproteinase expression favors proteolysis in thoracic aortic aneurysms and dissections
    • Koullias GJ, Ravichandran P, Korkolis DP, et al. Increased tissue microarray matrix metalloproteinase expression favors proteolysis in thoracic aortic aneurysms and dissections. Ann Thorac Surg 2004;78:2106-2110.
    • (2004) Ann Thorac Surg , vol.78 , pp. 2106-2110
    • Koullias, G.J.1    Ravichandran, P.2    Korkolis, D.P.3
  • 4
    • 23044479358 scopus 로고    scopus 로고
    • Altered patterns of gene expression specific to thoracic aortic aneurysms: Microarray analysis of surgically resected specimens
    • Taketani T, Imai Y, Morota T, et al. Altered patterns of gene expression specific to thoracic aortic aneurysms: microarray analysis of surgically resected specimens. Int Heart J 2005;46:265-277.
    • (2005) Int Heart J , vol.46 , pp. 265-277
    • Taketani, T.1    Imai, Y.2    Morota, T.3
  • 5
    • 0034808341 scopus 로고    scopus 로고
    • Smooth muscle cells of the media in the dilatative pathology of ascending thoracic aorta: Morphology, immunoreactivity for osteopontin, matrix metalloproteinases, and their inhibitors
    • Lesauskaite V, Tanganelli P, Sassi C, et al. Smooth muscle cells of the media in the dilatative pathology of ascending thoracic aorta: morphology, immunoreactivity for osteopontin, matrix metalloproteinases, and their inhibitors. Hum Pathol 2001;32:1003-1011.
    • (2001) Hum Pathol , vol.32 , pp. 1003-1011
    • Lesauskaite, V.1    Tanganelli, P.2    Sassi, C.3
  • 6
    • 33748806587 scopus 로고    scopus 로고
    • Temporal disparity in the induction of matrix metalloproteinases and tissue inhibitors of metalloproteinases after thoracic aortic aneurysm formation
    • Barbour JR, Stroud RE, Lowry AS, et al. Temporal disparity in the induction of matrix metalloproteinases and tissue inhibitors of metalloproteinases after thoracic aortic aneurysm formation. J Thorac Cardiovasc Surg 2006;132:788-795.
    • (2006) J Thorac Cardiovasc Surg , vol.132 , pp. 788-795
    • Barbour, J.R.1    Stroud, R.E.2    Lowry, A.S.3
  • 8
    • 0018177381 scopus 로고
    • Pathological study on amyloidosis - relationship of amyloid deposits in the aorta to aging
    • Iwata T, Kamei T, Uchino F, et al. Pathological study on amyloidosis - relationship of amyloid deposits in the aorta to aging. Acta Pathol Jpn 1978;28:193-203.
    • (1978) Acta Pathol Jpn , vol.28 , pp. 193-203
    • Iwata, T.1    Kamei, T.2    Uchino, F.3
  • 9
    • 0026551594 scopus 로고
    • Senile aortic amyloid. Evidence for two distinct forms of localized deposits
    • Mucchiano G, Cornwell III GG, Westermark P. Senile aortic amyloid. Evidence for two distinct forms of localized deposits. Am J Pathol 1992;140:871-877.
    • (1992) Am J Pathol , vol.140 , pp. 871-877
    • Mucchiano, G.1    Cornwell III, G.G.2    Westermark, P.3
  • 10
    • 0020519870 scopus 로고
    • Frequency and distribution of senile cardiovascular amyloid. A clinicopathologic correlation
    • Cornwell III GG, Murdoch WL, Kyle RA, et al. Frequency and distribution of senile cardiovascular amyloid. A clinicopathologic correlation. Am J Med 1983;75:618-623.
    • (1983) Am J Med , vol.75 , pp. 618-623
    • Cornwell III, G.G.1    Murdoch, W.L.2    Kyle, R.A.3
  • 11
    • 0033587677 scopus 로고    scopus 로고
    • Medin: An integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid
    • Häggqvist B, Näslund J, Sletten K, et al. Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid. Proc Natl Acad Sci USA 1999;96:8669-8674.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8669-8674
    • Häggqvist, B.1    Näslund, J.2    Sletten, K.3
  • 12
    • 0020376131 scopus 로고
    • Circulating human mammary epithelial antigens in breast cancer
    • Ceriani RL, Sasaki M, Sussman H, et al. Circulating human mammary epithelial antigens in breast cancer. Proc Natl Acad Sci USA 1982;79:5420-5424.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 5420-5424
    • Ceriani, R.L.1    Sasaki, M.2    Sussman, H.3
  • 13
    • 0037046580 scopus 로고    scopus 로고
    • Identification of a factor that links apoptotic cells to phagocytes
    • Hanayama R, Tanaka M, Miwa K, et al. Identification of a factor that links apoptotic cells to phagocytes. Nature 2002;417:182-187.
    • (2002) Nature , vol.417 , pp. 182-187
    • Hanayama, R.1    Tanaka, M.2    Miwa, K.3
  • 14
    • 0036679375 scopus 로고    scopus 로고
    • Characterization of novel breast carcinoma-associated BA46-derived peptides in HLA-A2.1/D(b)-beta2m transgenic mice
    • Carmon L, Bobilev-Priel I, Brenner B, et al. Characterization of novel breast carcinoma-associated BA46-derived peptides in HLA-A2.1/D(b)-beta2m transgenic mice. J Clin Invest 2002;110:453-462.
    • (2002) J Clin Invest , vol.110 , pp. 453-462
    • Carmon, L.1    Bobilev-Priel, I.2    Brenner, B.3
  • 15
    • 0033024052 scopus 로고    scopus 로고
    • Protective function of human milk: The milk fat globule
    • Hamosh M, Peterson JA, Henderson TR, et al. Protective function of human milk: the milk fat globule. Semin Perinatol 1999;23:242-249.
    • (1999) Semin Perinatol , vol.23 , pp. 242-249
    • Hamosh, M.1    Peterson, J.A.2    Henderson, T.R.3
  • 16
    • 0038107373 scopus 로고    scopus 로고
    • Lactadherin inhibits enzyme complexes of blood coagulation by competing for phospholipid-binding sites
    • Shi J, Gilbert GE. Lactadherin inhibits enzyme complexes of blood coagulation by competing for phospholipid-binding sites. Blood 2003;101:2628-2636.
    • (2003) Blood , vol.101 , pp. 2628-2636
    • Shi, J.1    Gilbert, G.E.2
  • 17
    • 21044455286 scopus 로고    scopus 로고
    • Lactadherin promotes VEGF-dependent neovascularization
    • Silvestre JS, Thery C, Hamard G, et al. Lactadherin promotes VEGF-dependent neovascularization. Nat Med 2005;11:499-506.
    • (2005) Nat Med , vol.11 , pp. 499-506
    • Silvestre, J.S.1    Thery, C.2    Hamard, G.3
  • 18
    • 33747619664 scopus 로고    scopus 로고
    • Lactadherin binds to elastin - a starting point for medin amyloid formation?
    • Larsson A, Peng S, Persson H, et al. Lactadherin binds to elastin - a starting point for medin amyloid formation? Amyloid 2006;13:78-85.
    • (2006) Amyloid , vol.13 , pp. 78-85
    • Larsson, A.1    Peng, S.2    Persson, H.3
  • 19
    • 0042709605 scopus 로고    scopus 로고
    • Molecular mechanisms of amyloidosis
    • Merlini G, Bellotti V. Molecular mechanisms of amyloidosis. N Engl J Med 2003;349:583-596.
    • (2003) N Engl J Med , vol.349 , pp. 583-596
    • Merlini, G.1    Bellotti, V.2
  • 20
    • 28244446220 scopus 로고    scopus 로고
    • Aspects on human amyloid forms and their fibril polypeptides
    • Westermark P. Aspects on human amyloid forms and their fibril polypeptides. FEBSJ 2005;272:5942-5949.
    • (2005) FEBSJ , vol.272 , pp. 5942-5949
    • Westermark, P.1
  • 21
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M, Giannoni E, Chiti F, et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002;416:507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3
  • 22
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003;300:486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3
  • 23
    • 23044501301 scopus 로고    scopus 로고
    • Aggregation and porin-like channel activity of a beta sheet peptide
    • Thundimadathil J, Roeske RW, Jiang HY, et al. Aggregation and porin-like channel activity of a beta sheet peptide. Biochemistry 2005;44:10259-10270.
    • (2005) Biochemistry , vol.44 , pp. 10259-10270
    • Thundimadathil, J.1    Roeske, R.W.2    Jiang, H.Y.3
  • 24
    • 0028957882 scopus 로고
    • Amyloid peptides are toxic via a common oxidative mechanism
    • Schubert D, Behl C, Lesley R, et al. Amyloid peptides are toxic via a common oxidative mechanism. Proc Natl Acad Sci USA 1995;92:1989-1993.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1989-1993
    • Schubert, D.1    Behl, C.2    Lesley, R.3
  • 25
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C, Davis JB, Lesley R, et al. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 1994;77:817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3
  • 26
    • 0035478665 scopus 로고    scopus 로고
    • Familial amyloid polyneuropathy: Receptor for advanced glycation end products-dependent triggering of neuronal inflammatory and apoptotic pathways
    • Sousa MM, Du Yan S, Fernandes R, et al. Familial amyloid polyneuropathy: receptor for advanced glycation end products-dependent triggering of neuronal inflammatory and apoptotic pathways. J Neurosci 2001;21:7576-7586.
    • (2001) J Neurosci , vol.21 , pp. 7576-7586
    • Sousa, M.M.1    Du Yan, S.2    Fernandes, R.3
  • 27
    • 0141566766 scopus 로고    scopus 로고
    • Cerebral amyloid angiopathies: A pathologic, biochemical, and genetic view
    • Revesz T, Ghiso J, Lashley T, et al. Cerebral amyloid angiopathies: a pathologic, biochemical, and genetic view. J Neuropathol Exp Neurol 2003;62:885-898.
    • (2003) J Neuropathol Exp Neurol , vol.62 , pp. 885-898
    • Revesz, T.1    Ghiso, J.2    Lashley, T.3
  • 28
    • 0025296269 scopus 로고
    • Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type
    • Levy E, Carman MD, Fernandez-Madrid IJ, et al. Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type. Science 1990;248:1124-1126.
    • (1990) Science , vol.248 , pp. 1124-1126
    • Levy, E.1    Carman, M.D.2    Fernandez-Madrid, I.J.3
  • 29
    • 0035282982 scopus 로고    scopus 로고
    • Spontaneous hemorrhagic stroke in a mouse model of cerebral amyloid angiopathy
    • Winkler DT, Bondolfi L, Herzig MC, et al. Spontaneous hemorrhagic stroke in a mouse model of cerebral amyloid angiopathy. J Neurosci 2001;21:1619-1627.
    • (2001) J Neurosci , vol.21 , pp. 1619-1627
    • Winkler, D.T.1    Bondolfi, L.2    Herzig, M.C.3
  • 30
    • 0035099136 scopus 로고    scopus 로고
    • Structural and functional disruption of vascular smooth muscle cells in a transgenic mouse model of amyloid angiopathy
    • Christie R, Yamada M, Moskowitz M, et al. Structural and functional disruption of vascular smooth muscle cells in a transgenic mouse model of amyloid angiopathy. Am J Pathol 2001;158:1065-1071.
    • (2001) Am J Pathol , vol.158 , pp. 1065-1071
    • Christie, R.1    Yamada, M.2    Moskowitz, M.3
  • 33
    • 0028260652 scopus 로고
    • Mechanisms of transthyretin amyloidogenesis. Antigenic mapping of transthyretin purified from plasma and amyloid fibrils and within in situ tissue localizations
    • Gustavsson Å, Engström U, Westermark P. Mechanisms of transthyretin amyloidogenesis. Antigenic mapping of transthyretin purified from plasma and amyloid fibrils and within in situ tissue localizations. Am J Pathol 1994;144:1301-1311.
    • (1994) Am J Pathol , vol.144 , pp. 1301-1311
    • Gustavsson, A.1    Engström, U.2    Westermark, P.3
  • 34
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate- polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, von Jagow G. Tricine-sodium dodecyl sulfate- polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 1987;166:368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 35
    • 22144483471 scopus 로고    scopus 로고
    • Medin-amyloid: A recently characterized age-associated arterial amyloid form affects mainly arteries in the upper part of the body
    • Peng S, Glennert J, Westermark P. Medin-amyloid: A recently characterized age-associated arterial amyloid form affects mainly arteries in the upper part of the body. Amyloid 2005;12:96-102.
    • (2005) Amyloid , vol.12 , pp. 96-102
    • Peng, S.1    Glennert, J.2    Westermark, P.3
  • 36
    • 0033135143 scopus 로고    scopus 로고
    • Multiple forms of lactadherin (breast antigen BA46) and butyrophilin are secreted into human milk as major components of milk fat globule membrane
    • Cavaletto M, Giuffrida MG, Giunta C, et al. Multiple forms of lactadherin (breast antigen BA46) and butyrophilin are secreted into human milk as major components of milk fat globule membrane. J Dairy Res 1999;66:295-301.
    • (1999) J Dairy Res , vol.66 , pp. 295-301
    • Cavaletto, M.1    Giuffrida, M.G.2    Giunta, C.3
  • 37
    • 0033856957 scopus 로고    scopus 로고
    • Investigation of the Alamar Blue (resazurin) fluorescent dye for the assessment of mammalian cell cytotoxicity
    • O'Brien J, Wilson I, Orton T, et al. Investigation of the Alamar Blue (resazurin) fluorescent dye for the assessment of mammalian cell cytotoxicity. Eur J Biochem 2000;267:5421-5426.
    • (2000) Eur J Biochem , vol.267 , pp. 5421-5426
    • O'Brien, J.1    Wilson, I.2    Orton, T.3
  • 38
    • 0036145233 scopus 로고    scopus 로고
    • Medin and medin-amyloid in ageing inflamed and non-inflamed temporal arteries
    • Peng S, Westermark GT, Näslund J, et al. Medin and medin-amyloid in ageing inflamed and non-inflamed temporal arteries. J Pathol 2002;196:91-96.
    • (2002) J Pathol , vol.196 , pp. 91-96
    • Peng, S.1    Westermark, G.T.2    Näslund, J.3
  • 39
    • 0037466395 scopus 로고    scopus 로고
    • Beta-amyloid induces the production of active, matrix-degrading proteases in cultured rat astrocytes
    • Deb S, Wenjun Zhang J, Gottschall PE. Beta-amyloid induces the production of active, matrix-degrading proteases in cultured rat astrocytes. Brain Res 2003;970:205-213.
    • (2003) Brain Res , vol.970 , pp. 205-213
    • Deb, S.1    Wenjun Zhang, J.2    Gottschall, P.E.3
  • 40
    • 0038241040 scopus 로고    scopus 로고
    • Pathogenic A beta induces the expression and activation of matrix metalloproteinase-2 in human cerebrovascular smooth muscle cells
    • Jung SS, Zhang W, Van Nostrand WE. Pathogenic A beta induces the expression and activation of matrix metalloproteinase-2 in human cerebrovascular smooth muscle cells. J Neurochem 2003;85:1208-1215.
    • (2003) J Neurochem , vol.85 , pp. 1208-1215
    • Jung, S.S.1    Zhang, W.2    Van Nostrand, W.E.3
  • 41
    • 0041835847 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 and spontaneous hemorrhage in an animal model of cerebral amyloid angiopathy
    • Lee JM, Yin KJ, Hsin I, et al. Matrix metalloproteinase-9 and spontaneous hemorrhage in an animal model of cerebral amyloid angiopathy. Ann Neurol 2003;54:379-382.
    • (2003) Ann Neurol , vol.54 , pp. 379-382
    • Lee, J.M.1    Yin, K.J.2    Hsin, I.3
  • 42
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 2003;26:267-298.
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 43
    • 0031575827 scopus 로고    scopus 로고
    • Oxidative stress is found in amyloid deposits in systemic amyloidosis
    • Ando Y, Nyhlin N, Suhr O, et al. Oxidative stress is found in amyloid deposits in systemic amyloidosis. Biochem Biophys Res Commun 1997;232:497-502.
    • (1997) Biochem Biophys Res Commun , vol.232 , pp. 497-502
    • Ando, Y.1    Nyhlin, N.2    Suhr, O.3
  • 44
    • 0028363366 scopus 로고
    • Advanced glycation end products contribute to amyloidosis in Alzheimer disease
    • Vitek MP, Bhattacharya K, Glendening JM, et al. Advanced glycation end products contribute to amyloidosis in Alzheimer disease. Proc Natl Acad Sci USA 1994;91:4766-4770.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4766-4770
    • Vitek, M.P.1    Bhattacharya, K.2    Glendening, J.M.3
  • 45
    • 0034017171 scopus 로고    scopus 로고
    • Advanced glycation end product in familial amyloidotic polyneuropathy (FAP)
    • Nyhlin N, Ando Y, Nagai R, et al. Advanced glycation end product in familial amyloidotic polyneuropathy (FAP). J Intern Med 2000;247:485-492.
    • (2000) J Intern Med , vol.247 , pp. 485-492
    • Nyhlin, N.1    Ando, Y.2    Nagai, R.3
  • 46
    • 34547897456 scopus 로고    scopus 로고
    • Unwinding fibril formation of medin, the peptide of the most common form of human amyloid
    • Larsson A, Söderberg L, Westermark GT, et al. Unwinding fibril formation of medin, the peptide of the most common form of human amyloid. Biochem Biophys Res Commun 2007;361:822-828.
    • (2007) Biochem Biophys Res Commun , vol.361 , pp. 822-828
    • Larsson, A.1    Söderberg, L.2    Westermark, G.T.3


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