메뉴 건너뛰기




Volumn 67, Issue 3, 1996, Pages 1132-1144

Detection and quantitation of perlecan mRNA levels in Alzheimer's disease and normal aged hippocampus by competitive reverse transcription- polymerase chain reaction

Author keywords

Alzheimer's disease; Expression; Heparan sulfate; Perlecan; Proteoglycans; Reverse transcription polymerase chain reaction

Indexed keywords

AMYLOID BETA PROTEIN; MESSENGER RNA; PERLECAN; PROTEOHEPARAN SULFATE;

EID: 0029820953     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.67031132.x     Document Type: Article
Times cited : (21)

References (86)
  • 1
    • 0023838532 scopus 로고
    • 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease
    • 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease. Cell 52, 487-501.
    • (1988) Cell , vol.52 , pp. 487-501
    • Abraham, C.1    Selkoe, D.J.2    Potter, H.3
  • 2
    • 0027482564 scopus 로고
    • Induction of perlecan gene expression precedes amyloid formation during experimental murine AA amyloidogenesis
    • Ailles L., Kisilevsky R., and Young I. D. (1993) Induction of perlecan gene expression precedes amyloid formation during experimental murine AA amyloidogenesis. Lab. Invest. 69, 443-447.
    • (1993) Lab. Invest. , vol.69 , pp. 443-447
    • Ailles, L.1    Kisilevsky, R.2    Young, I.D.3
  • 5
    • 0027407521 scopus 로고
    • Binding of secreted human neuroblastoma proteoglycans to the Alzheimer's amyloid A4 peptide
    • Buee L., Ding W., Delacourte A., and Fillit H. (1993b) Binding of secreted human neuroblastoma proteoglycans to the Alzheimer's amyloid A4 peptide. Brain Res. 601, 154-163.
    • (1993) Brain Res. , vol.601 , pp. 154-163
    • Buee, L.1    Ding, W.2    Delacourte, A.3    Fillit, H.4
  • 6
    • 0024584913 scopus 로고
    • Molecular modeling of protein-glycosaminoglycan interactions
    • Cardin A. D. and Weintraub H. J. R. (1989) Molecular modeling of protein-glycosaminoglycan interactions. Arteriosclerosis 9, 21-32.
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.R.2
  • 8
    • 0026301776 scopus 로고
    • Assignment of the perlecan (heparan sulfate proteoglycan) gene to mouse chromosome 4
    • Chakravarti S., Phillips S. L., and Hassell J. R. (1991) Assignment of the perlecan (heparan sulfate proteoglycan) gene to mouse chromosome 4. Mamm. Genome 1, 270-272.
    • (1991) Mamm. Genome , vol.1 , pp. 270-272
    • Chakravarti, S.1    Phillips, S.L.2    Hassell, J.R.3
  • 9
    • 0027268021 scopus 로고
    • Perlecan gene expression precedes laminin gene expression during differentiation of F9 embryonal carcinoma cells
    • Chakravarti S., Hassell J. R., and Phillips S. (1993) Perlecan gene expression precedes laminin gene expression during differentiation of F9 embryonal carcinoma cells. Dev. Dyn. 197, 107-114.
    • (1993) Dev. Dyn. , vol.197 , pp. 107-114
    • Chakravarti, S.1    Hassell, J.R.2    Phillips, S.3
  • 10
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P. and Sacchi N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 11
    • 0027373292 scopus 로고
    • Structural characterization of the complete human perlecan gene and its promoter
    • Cohen I. R., Grassel S., Murdoch A. D., and Iozzo R. V. (1993) Structural characterization of the complete human perlecan gene and its promoter. Proc. Natl. Acad. Sci. USA 90, 10404-10408.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10404-10408
    • Cohen, I.R.1    Grassel, S.2    Murdoch, A.D.3    Iozzo, R.V.4
  • 12
    • 0023472509 scopus 로고
    • Neuron numbers and dendritic extent in normal aging and Alzheimer's disease
    • Coleman P. D. and Flood D. G. (1987) Neuron numbers and dendritic extent in normal aging and Alzheimer's disease. Neurobiol. Aging 8, 521-545.
    • (1987) Neurobiol. Aging , vol.8 , pp. 521-545
    • Coleman, P.D.1    Flood, D.G.2
  • 13
    • 0023899417 scopus 로고
    • Isolation and characterization of amyloid P component from Alzheimer's disease and other types of cerebral amyloidoses
    • Coria F., Castano E., Prelli F, Lillo-Larrondo M., Van Duinen S., Shelanski M. L., and Frangione B. (1988) Isolation and characterization of amyloid P component from Alzheimer's disease and other types of cerebral amyloidoses. Lab. Invest. 58, 454-458.
    • (1988) Lab. Invest. , vol.58 , pp. 454-458
    • Coria, F.1    Castano, E.2    Prelli, F.3    Lillo-Larrondo, M.4    Van Duinen, S.5    Shelanski, M.L.6    Frangione, B.7
  • 14
    • 0027209456 scopus 로고
    • Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's disease
    • DeWitt D. A., Silver J., Canning D. R., and Perry G. (1993) Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's disease. Exp. Neurol. 121, 149-152.
    • (1993) Exp. Neurol. , vol.121 , pp. 149-152
    • DeWitt, D.A.1    Silver, J.2    Canning, D.R.3    Perry, G.4
  • 15
    • 0025790413 scopus 로고
    • Heparan sulfate proteoglycan of human colon: Partial molecular cloning, cellular expression, and mapping of the gene (HSPG2) to the short arm of human chromosome 1
    • Dodge G. R., Kovalsky I., Chu M. L., Hassell J. R., McBride O. W., Yi H. F., and Iozzo R. (1991) Heparan sulfate proteoglycan of human colon: partial molecular cloning, cellular expression, and mapping of the gene (HSPG2) to the short arm of human chromosome 1. Genomics 10, 673-680.
    • (1991) Genomics , vol.10 , pp. 673-680
    • Dodge, G.R.1    Kovalsky, I.2    Chu, M.L.3    Hassell, J.R.4    McBride, O.W.5    Yi, H.F.6    Iozzo, R.7
  • 16
    • 0028818528 scopus 로고
    • Expression of the basement membrane heparan sulfate proteoglycan (perlecan) in human synovium and in cultured human synovial cells
    • Dodge G. R., Boesler E. W., and Jimenez S. A. (1995) Expression of the basement membrane heparan sulfate proteoglycan (perlecan) in human synovium and in cultured human synovial cells. Lab. Invest. 73, 649-657.
    • (1995) Lab. Invest. , vol.73 , pp. 649-657
    • Dodge, G.R.1    Boesler, E.W.2    Jimenez, S.A.3
  • 17
    • 0025976188 scopus 로고
    • Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan
    • Doege K. J., Sasaki M., Kimurai T., and Yamada Y. (1991) Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. J. Biol. Chem. 266, 894-902.
    • (1991) J. Biol. Chem. , vol.266 , pp. 894-902
    • Doege, K.J.1    Sasaki, M.2    Kimurai, T.3    Yamada, Y.4
  • 18
    • 0028566656 scopus 로고
    • A novel glycosaminoglycan attachment domain identified in two alternative splice variants of human versican
    • Dours-Zimmerman M. T. and Zimmerman D. R. (1994) A novel glycosaminoglycan attachment domain identified in two alternative splice variants of human versican. J. Biol. Chem. 269, 32992-32998.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32992-32998
    • Dours-Zimmerman, M.T.1    Zimmerman, D.R.2
  • 20
    • 0026673537 scopus 로고
    • Effect of sulfate ions on Alzheimer β/A4 assemblies: Implications for amyloid fibril-proteoglycan interactions
    • Fraser P. E., Nguyen J. T., Chin D. T., and Kirschner D. A. (1992) Effect of sulfate ions on Alzheimer β/A4 assemblies: implications for amyloid fibril-proteoglycan interactions. J. Neurochem. 59, 1531-1540.
    • (1992) J. Neurochem. , vol.59 , pp. 1531-1540
    • Fraser, P.E.1    Nguyen, J.T.2    Chin, D.T.3    Kirschner, D.A.4
  • 21
    • 0025355882 scopus 로고
    • Analysis of cytokine mRNA and DNA: Detection and quantitation by competitive polymerase chain reaction
    • Gilliland G., Perrin S., Blanchard K., and Bunn H. F. (1990) Analysis of cytokine mRNA and DNA: detection and quantitation by competitive polymerase chain reaction. Proc. Natl. Acad. Sci. USA 87, 2725-2729.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2725-2729
    • Gilliland, G.1    Perrin, S.2    Blanchard, K.3    Bunn, H.F.4
  • 22
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G. G. and Wong C. W. (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 23
    • 0027263169 scopus 로고
    • Versican gene expression in human articular cartilage and comparison of mRNA splicing variation with aggrecan
    • Grover J. and Roughley P. J. (1993) Versican gene expression in human articular cartilage and comparison of mRNA splicing variation with aggrecan. Biochem. J. 291, 361-367.
    • (1993) Biochem. J. , vol.291 , pp. 361-367
    • Grover, J.1    Roughley, P.J.2
  • 26
    • 0022549757 scopus 로고
    • Nerve growth factor and Alzheimer's disease
    • Hefti F. and Weiner W. J. (1986) Nerve growth factor and Alzheimer's disease. Ann. Neurol. 20, 275-281.
    • (1986) Ann. Neurol. , vol.20 , pp. 275-281
    • Hefti, F.1    Weiner, W.J.2
  • 27
    • 0024394332 scopus 로고
    • Function of neurotrophic factors in the adult and aging brain and their possible use in the treatment of neurodegenerative diseases
    • Hefti F., Hartikka J., and Knusel B. (1989) Function of neurotrophic factors in the adult and aging brain and their possible use in the treatment of neurodegenerative diseases. Neurobiol. Aging 10, 515-533.
    • (1989) Neurobiol. Aging , vol.10 , pp. 515-533
    • Hefti, F.1    Hartikka, J.2    Knusel, B.3
  • 29
    • 0028959255 scopus 로고
    • Multiple forms of mouse PG-M, a large chondroitin sulfate proteoglycan generated by alternative splicing
    • Ito K., Shinomura T., Zako M., Ujita M., and Kimata K. (1995) Multiple forms of mouse PG-M, a large chondroitin sulfate proteoglycan generated by alternative splicing. J. Biol. Chem. 270, 958-965.
    • (1995) J. Biol. Chem. , vol.270 , pp. 958-965
    • Ito, K.1    Shinomura, T.2    Zako, M.3    Ujita, M.4    Kimata, K.5
  • 30
    • 0026500541 scopus 로고
    • Human basement membrane heparan sulfate proteoglycan core protein: A 467-kD protein containing multiple domains resembling elements of the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor
    • Kallunki P. and Tryggvason K. (1992) Human basement membrane heparan sulfate proteoglycan core protein: a 467-kD protein containing multiple domains resembling elements of the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor. J. Cell Biol. 116, 559-571.
    • (1992) J. Cell Biol. , vol.116 , pp. 559-571
    • Kallunki, P.1    Tryggvason, K.2
  • 31
    • 0026014313 scopus 로고
    • Cloning of human heparan sulfate proteoglycan core protein, assignment of the gene (HSPG2) to Ip36.1-p35 and identification of a BamHI restriction fragment length polymorphism
    • Kallunki P., Eddy R. L., Byers M. G., Kestila M., Shows T. B., and Tryggvason K. (1991) Cloning of human heparan sulfate proteoglycan core protein, assignment of the gene (HSPG2) to Ip36.1-p35 and identification of a BamHI restriction fragment length polymorphism. Genomics 11, 389-396.
    • (1991) Genomics , vol.11 , pp. 389-396
    • Kallunki, P.1    Eddy, R.L.2    Byers, M.G.3    Kestila, M.4    Shows, T.B.5    Tryggvason, K.6
  • 32
    • 0023693333 scopus 로고
    • Basement membrane proteoglycan in various tissues: Characterization using monoclonal to the Engelbreth-Holm-Swarm mouse tumor low density heparan sulfate proteoglycan
    • Kato M., Koike Y., Suzuki S., and Kimata K. (1988) Basement membrane proteoglycan in various tissues: characterization using monoclonal to the Engelbreth-Holm-Swarm mouse tumor low density heparan sulfate proteoglycan. J. Cell Biol. 106, 2203-2210.
    • (1988) J. Cell Biol. , vol.106 , pp. 2203-2210
    • Kato, M.1    Koike, Y.2    Suzuki, S.3    Kimata, K.4
  • 33
    • 0025968239 scopus 로고
    • The binding of bFGF to Alzheimer's disease neurofibrillary tangles and senile plaques
    • Kato T., Sasaki H., Katagiri T., Koiwai K., Youki H., Totsuka S., and Ishii T. (1991) The binding of bFGF to Alzheimer's disease neurofibrillary tangles and senile plaques. Neuroscience 122, 33-36.
    • (1991) Neuroscience , vol.122 , pp. 33-36
    • Kato, T.1    Sasaki, H.2    Katagiri, T.3    Koiwai, K.4    Youki, H.5    Totsuka, S.6    Ishii, T.7
  • 34
    • 0023942763 scopus 로고
    • Structural characterization of heparan sulfate proteoglycan subclasses isolated from bovine aortic endothelial cell cultures
    • Kinsella M. G. and Wight T. N. (1988) Structural characterization of heparan sulfate proteoglycan subclasses isolated from bovine aortic endothelial cell cultures. Biochemistry 27, 2136-2144.
    • (1988) Biochemistry , vol.27 , pp. 2136-2144
    • Kinsella, M.G.1    Wight, T.N.2
  • 35
    • 0023767031 scopus 로고
    • The potential significance of sulphated glycosaminoglycans as a common constituent of all amyloids; or perhaps amyloid is not a misnomer
    • Kisilevsky R. and Snow A. D. (1988) The potential significance of sulphated glycosaminoglycans as a common constituent of all amyloids; or perhaps amyloid is not a misnomer. Med. Hypotheses 26, 231-236.
    • (1988) Med. Hypotheses , vol.26 , pp. 231-236
    • Kisilevsky, R.1    Snow, A.D.2
  • 36
    • 0029050693 scopus 로고
    • Formation of heparan sulfate or chondroitin/dermatan sulfate on recombinant domain I of mouse perlecan expressed in Chinese hamster ovary cells
    • Kokenyesi R. and Silbert J. E. (1995) Formation of heparan sulfate or chondroitin/dermatan sulfate on recombinant domain I of mouse perlecan expressed in Chinese hamster ovary cells. Biochem. Biophys. Res. Commun. 211, 262-267.
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 262-267
    • Kokenyesi, R.1    Silbert, J.E.2
  • 37
    • 0009364134 scopus 로고
    • Microtubuleassociated protein tau is a major antigenic component of paired helical filaments in Alzheimer's disease
    • Kosik K. S., Joachim C. L., and Selkoe D. J. (1986) Microtubuleassociated protein tau is a major antigenic component of paired helical filaments in Alzheimer's disease. Proc. Natl. Acad. Sci. USA 83, 4044-4048.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 38
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal tau
    • Lee V. M. Y., Balin B. J., Otvos L. Jr., and Trojanowski J. Q. (1991) A68: a major subunit of paired helical filaments and derivatized forms of normal tau. Science 251, 675-678.
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.Y.1    Balin, B.J.2    Otvos Jr., L.3    Trojanowski, J.Q.4
  • 39
    • 0028787874 scopus 로고
    • Role of microglia in senile plaque formation
    • Mackenzie I. R. A., Hao C., and Munoz D. G. (1995) Role of microglia in senile plaque formation. Neurobiology 16, 797-804.
    • (1995) Neurobiology , vol.16 , pp. 797-804
    • Mackenzie, I.R.A.1    Hao, C.2    Munoz, D.G.3
  • 41
    • 0024212706 scopus 로고
    • Circular-dichroism studies on two murine serum amyloid A proteins
    • McCubbin W. D., Kay C. M., Narindrasorasak S., and Kisilevsky R. (1988) Circular-dichroism studies on two murine serum amyloid A proteins. Biochem. J. 256, 775-783.
    • (1988) Biochem. J. , vol.256 , pp. 775-783
    • McCubbin, W.D.1    Kay, C.M.2    Narindrasorasak, S.3    Kisilevsky, R.4
  • 43
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • Mori H., Kondo J., and Ihara Y. (1987) Ubiquitin is a component of paired helical filaments in Alzheimer's disease. Science 235, 1641-1644.
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 44
    • 0020956552 scopus 로고
    • Cortical neuronal counts in normal elderly controls and demented patients
    • Mountjoy C. Q., Roth M., Evans N. J. R., and Evans H. M. (1983) Cortical neuronal counts in normal elderly controls and demented patients. Neurobiol. Aging 4, 1 -11.
    • (1983) Neurobiol. Aging , vol.4 , pp. 1-11
    • Mountjoy, C.Q.1    Roth, M.2    Evans, N.J.R.3    Evans, H.M.4
  • 45
    • 0026758187 scopus 로고
    • Primary structure of the human heparan sulfate proteoglycan from basement membrane (HSPG/perlecan). A chimeric molecule with multiple domains homologous to the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor
    • Murdoch A. D., Dodge G. R., Cohen I., Tuan R. S., and Iozzo R. V. (1992) Primary structure of the human heparan sulfate proteoglycan from basement membrane (HSPG/perlecan). A chimeric molecule with multiple domains homologous to the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor. J. Biol. Chem. 267, 8544-8557.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8544-8557
    • Murdoch, A.D.1    Dodge, G.R.2    Cohen, I.3    Tuan, R.S.4    Iozzo, R.V.5
  • 46
    • 0028158005 scopus 로고
    • Widespread expression of perlecan proteoglycan in basement membranes and extracellular matrices of human tissues as detected by a novel monoclonal antibody against domain III and by in situ hybridization
    • Murdoch A. D., Liu B., Schwarting R., Tuan R. S., and Iozzo R. V. (1994) Widespread expression of perlecan proteoglycan in basement membranes and extracellular matrices of human tissues as detected by a novel monoclonal antibody against domain III and by in situ hybridization. J. Histochem. Cytochem. 42, 239-249.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 239-249
    • Murdoch, A.D.1    Liu, B.2    Schwarting, R.3    Tuan, R.S.4    Iozzo, R.V.5
  • 47
    • 0029969488 scopus 로고    scopus 로고
    • PDGF-A mRNA expression in fetal, normal adult, and atherosclerotic human aortas. Analysis by competitive PCR
    • Murry C. E., Bartosek T., Giachelli C. M., Alpers C. E., and Schwartz S. M. (1996) PDGF-A mRNA expression in fetal, normal adult, and atherosclerotic human aortas. Analysis by competitive PCR. Circulation 93, 1095-1106.
    • (1996) Circulation , vol.93 , pp. 1095-1106
    • Murry, C.E.1    Bartosek, T.2    Giachelli, C.M.3    Alpers, C.E.4    Schwartz, S.M.5
  • 48
    • 0025971426 scopus 로고
    • Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease
    • Namba Y., Tomonaga M., Kawasaki H., Otomon E., and Ikeda K. (1991) Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease. Brain Res. 541, 163-166.
    • (1991) Brain Res. , vol.541 , pp. 163-166
    • Namba, Y.1    Tomonaga, M.2    Kawasaki, H.3    Otomon, E.4    Ikeda, K.5
  • 49
    • 0025864064 scopus 로고
    • High affinity interactions between the Alzheimer's beta-amyloid precursor proteins and the basement membrane form of heparan sulfate proteoglycan
    • Narindrasorasak S., Lowry D. E., Gonzalez-DeWhitt P. A., Poorman R. A., Greenberg B. D., and Kisilevsky R. (1991) High affinity interactions between the Alzheimer's beta-amyloid precursor proteins and the basement membrane form of heparan sulfate proteoglycan. J. Biol. Chem. 266, 12878-12883.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12878-12883
    • Narindrasorasak, S.1    Lowry, D.E.2    Gonzalez-DeWhitt, P.A.3    Poorman, R.A.4    Greenberg, B.D.5    Kisilevsky, R.6
  • 50
    • 0027358984 scopus 로고
    • A simple method of rapid freezing adequately preserves brain tissue for immunocytochemistry, light and electron microscopic examination
    • Nochlin D., Mackenzie A. P., Bryant E. M., Norwood T. H., and Sumi S. M. (1993) A simple method of rapid freezing adequately preserves brain tissue for immunocytochemistry, light and electron microscopic examination. Acta Neuropathol (Berlin) 86, 645-650.
    • (1993) Acta Neuropathol (Berlin) , vol.86 , pp. 645-650
    • Nochlin, D.1    Mackenzie, A.P.2    Bryant, E.M.3    Norwood, T.H.4    Sumi, S.M.5
  • 51
    • 0027245578 scopus 로고
    • Perlecan, the large low density proteoglycan of basement membranes: Structure and variant forms
    • Noonan D. M. and Hassell J. R. (1993) Perlecan, the large low density proteoglycan of basement membranes: structure and variant forms. Kidney Int. 43, 53-60.
    • (1993) Kidney Int. , vol.43 , pp. 53-60
    • Noonan, D.M.1    Hassell, J.R.2
  • 52
    • 0026317977 scopus 로고
    • The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor, and the neural cell adhesion molecule
    • Noonan D. M., Fulle A., Valente P., Cai S., Horigan E., Sasaki M., Yamada Y., and Hassell J. R. (1991) The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor, and the neural cell adhesion molecule. J. Biol. Chem. 266, 22939-22947.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22939-22947
    • Noonan, D.M.1    Fulle, A.2    Valente, P.3    Cai, S.4    Horigan, E.5    Sasaki, M.6    Yamada, Y.7    Hassell, J.R.8
  • 53
    • 0025341743 scopus 로고
    • Microangiopathy, the vascular basement membrane and Alzheimer's disease: A review
    • Perlmutter L. S. and Chui H. C. (1990) Microangiopathy, the vascular basement membrane and Alzheimer's disease: a review. Brain Res. Bull. 24, 677-686.
    • (1990) Brain Res. Bull. , vol.24 , pp. 677-686
    • Perlmutter, L.S.1    Chui, H.C.2
  • 54
    • 0025195769 scopus 로고
    • Microangiopathy and the colocalization of heparan sulfate proteoglycan with amyloid in senile plaques of Alzheimer's disease
    • Perlmutter L. S., Chui H. C., Saperia D., and Athanikar J. (1990) Microangiopathy and the colocalization of heparan sulfate proteoglycan with amyloid in senile plaques of Alzheimer's disease. Brain Res. 508, 13-19.
    • (1990) Brain Res. , vol.508 , pp. 13-19
    • Perlmutter, L.S.1    Chui, H.C.2    Saperia, D.3    Athanikar, J.4
  • 55
    • 0001521232 scopus 로고
    • Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites in Alzheimer's disease brain
    • Perry G., Freidman R., Shaw G., and Chau V. (1987) Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites in Alzheimer's disease brain. Proc. Natl. Acad. Sci. USA 84, 3033-3036.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3033-3036
    • Perry, G.1    Freidman, R.2    Shaw, G.3    Chau, V.4
  • 56
    • 0027441601 scopus 로고
    • Distribution and origin of the basement membrane component perlecan in rat liver and primary hepatocyte culture
    • Rescan P. Y., Loreal O., Hassell J. R., Yamada Y., Guillouzo A., and Clement B. (1993) Distribution and origin of the basement membrane component perlecan in rat liver and primary hepatocyte culture. Am. J. Pathol 142, 199-208.
    • (1993) Am. J. Pathol , vol.142 , pp. 199-208
    • Rescan, P.Y.1    Loreal, O.2    Hassell, J.R.3    Yamada, Y.4    Guillouzo, A.5    Clement, B.6
  • 57
    • 0000952440 scopus 로고
    • Inflammation and Alzheimer's disease
    • Rogers J. (1994) Inflammation and Alzheimer's disease. CNS Drugs 4, 241-244.
    • (1994) CNS Drugs , vol.4 , pp. 241-244
    • Rogers, J.1
  • 58
    • 0027491355 scopus 로고
    • Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer's disease brain tissue
    • Roher A. E., Palmer K. C., Yurewicz E. C., Ball M. J., and Greenberg B. D. (1993) Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer's disease brain tissue. J. Neurochem. 61, 1916-1926.
    • (1993) J. Neurochem. , vol.61 , pp. 1916-1926
    • Roher, A.E.1    Palmer, K.C.2    Yurewicz, E.C.3    Ball, M.J.4    Greenberg, B.D.5
  • 59
    • 0024593482 scopus 로고
    • Characterization of the major heparan sulfate proteoglycan secreted by bovine aortic endothelial cells in culture
    • Saku T. and Furthmayr H. (1989) Characterization of the major heparan sulfate proteoglycan secreted by bovine aortic endothelial cells in culture. J. Biol. Chem. 264, 3514-3523.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3514-3523
    • Saku, T.1    Furthmayr, H.2
  • 60
  • 62
    • 0028101047 scopus 로고
    • Characterization of proteoglycans synthesized by murine embryonal carcinoma cells (P19) reveals increased expression of perlecan (heparan sulfate proteoglycan) during neuronal differentiation
    • Sekiguchi R. T., Potter-Perigo S., Braun K., Miller J., Ngo C., Fukuchi K., Wight T. N., Kimata K., and Snow A. D. (1994) Characterization of proteoglycans synthesized by murine embryonal carcinoma cells (P19) reveals increased expression of perlecan (heparan sulfate proteoglycan) during neuronal differentiation. J. Neurosci. Res. 38, 670-686.
    • (1994) J. Neurosci. Res. , vol.38 , pp. 670-686
    • Sekiguchi, R.T.1    Potter-Perigo, S.2    Braun, K.3    Miller, J.4    Ngo, C.5    Fukuchi, K.6    Wight, T.N.7    Kimata, K.8    Snow, A.D.9
  • 63
    • 0022962480 scopus 로고
    • Isolation of paired helical filaments and amyloid fibers from human brain
    • Selkoe D. J. and Abraham C. (1986) Isolation of paired helical filaments and amyloid fibers from human brain. Methods Enzymol. 134, 388-404.
    • (1986) Methods Enzymol. , vol.134 , pp. 388-404
    • Selkoe, D.J.1    Abraham, C.2
  • 64
    • 0024387388 scopus 로고
    • Proteoglycans in the pathogenesis of Alzheimer's disease
    • Snow A. D. and Wight T. N. (1989) Proteoglycans in the pathogenesis of Alzheimer's disease. Neurobiol. Aging 10, 481-497.
    • (1989) Neurobiol. Aging , vol.10 , pp. 481-497
    • Snow, A.D.1    Wight, T.N.2
  • 65
    • 0023128689 scopus 로고
    • Sulfated glycos-aminoglycans: A common constituent of all amyloids
    • Snow A. D., Willmer J., and Kisilevsky R. (1987) Sulfated glycos-aminoglycans: a common constituent of all amyloids. Lab. Invest. 56, 120-123.
    • (1987) Lab. Invest. , vol.56 , pp. 120-123
    • Snow, A.D.1    Willmer, J.2    Kisilevsky, R.3
  • 66
    • 0024273721 scopus 로고
    • The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy of Alzheimer's disease
    • Snow A. D., Mar H., Nochlin D., Kimata K., Kato M., Suzuki S., Hassell J., and Wight T. N. (1988) The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy of Alzheimer's disease. Am. J. Pathol. 133, 456-463.
    • (1988) Am. J. Pathol. , vol.133 , pp. 456-463
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Kimata, K.4    Kato, M.5    Suzuki, S.6    Hassell, J.7    Wight, T.N.8
  • 68
    • 0025223441 scopus 로고
    • Early accumulation of heparan sulfate in neurons and in the beta-amyloid protein containing lesions of Alzheimer's disease and Down's syndrome
    • Snow A. D., Mar H., Nochlin D., Sekiguchi R. T., Kimata K., Koike Y., and Wight T. N. (1990a) Early accumulation of heparan sulfate in neurons and in the beta-amyloid protein containing lesions of Alzheimer's disease and Down's syndrome. Am. J. Puthol 137, 1253-1270.
    • (1990) Am. J. Puthol , vol.137 , pp. 1253-1270
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Sekiguchi, R.T.4    Kimata, K.5    Koike, Y.6    Wight, T.N.7
  • 69
    • 0025243737 scopus 로고
    • Immunolocalization of heparan sulfate proteoglycans to prion protein amyloid plaques of Gerstmann-Straussler syndrome, Creutzfeldt-Jakob disease and scrapie
    • Snow A. D., Wight T. N., Nochlin D., Koike Y., Kimata K., DeArmond S. J., and Prusiner S. B. (1990b) Immunolocalization of heparan sulfate proteoglycans to prion protein amyloid plaques of Gerstmann-Straussler syndrome, Creutzfeldt-Jakob disease and scrapie. Lab. Invest. 63, 601-611.
    • (1990) Lab. Invest. , vol.63 , pp. 601-611
    • Snow, A.D.1    Wight, T.N.2    Nochlin, D.3    Koike, Y.4    Kimata, K.5    DeArmond, S.J.6    Prusiner, S.B.7
  • 70
    • 8044228785 scopus 로고
    • A temporal and ultrastructural relationship between heparan sulfate proteoglycans and AA amyloid in experimental amyloidosis
    • Snow A. D., Wight T. N., Mar H., Bramson R., and Kisilevsky R. (1991) A temporal and ultrastructural relationship between heparan sulfate proteoglycans and AA amyloid in experimental amyloidosis. J. Histochem. Cytochem. 40, 105-113.
    • (1991) J. Histochem. Cytochem. , vol.40 , pp. 105-113
    • Snow, A.D.1    Wight, T.N.2    Mar, H.3    Bramson, R.4    Kisilevsky, R.5
  • 71
    • 0026548436 scopus 로고
    • Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease
    • Snow A. D., Mar H., Nochlin D., Kresse H., and Wight T. N. (1992) Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease. J. Histochem. Cytochem. 40, 105-113.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 105-113
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Kresse, H.4    Wight, T.N.5
  • 72
    • 0028362886 scopus 로고
    • Heparan sulfate proteoglycan in diffuse plaques of hippocampus but not in cerebellum of Alzheimer's disease brain
    • Snow A. D., Sekiguchi R., Nochlin D., Kalaria R. N., and Kimata K. (1994a) Heparan sulfate proteoglycan in diffuse plaques of hippocampus but not in cerebellum of Alzheimer's disease brain. Am. J. Pathol. 144, 337-347.
    • (1994) Am. J. Pathol. , vol.144 , pp. 337-347
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, D.3    Kalaria, R.N.4    Kimata, K.5
  • 73
    • 0028082136 scopus 로고
    • An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar Aβ amyloid in rat brain
    • Snow A. D., Sekiguchi R., Nochlin D., Fraser P., Kimata K., Mitzutani A., Arai M., Schreier W. A., and Morgan D. G. (1994b) An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar Aβ amyloid in rat brain. Neuron 12, 219-234.
    • (1994) Neuron , vol.12 , pp. 219-234
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, D.3    Fraser, P.4    Kimata, K.5    Mitzutani, A.6    Arai, M.7    Schreier, W.A.8    Morgan, D.G.9
  • 74
    • 0029047722 scopus 로고
    • Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin and versican) to the beta-amyloid protein of Alzheimer's disease
    • Snow A. D., Kinsella M. G., Parks E., Sekiguchi R. T., Miller J. D., Kimata K., and Wight T. N. (1995a) Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin and versican) to the beta-amyloid protein of Alzheimer's disease. Arch. Biochem. Biophys. 320, 84-95.
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 84-95
    • Snow, A.D.1    Kinsella, M.G.2    Parks, E.3    Sekiguchi, R.T.4    Miller, J.D.5    Kimata, K.6    Wight, T.N.7
  • 75
    • 0345124322 scopus 로고
    • Further studies implicating the importance of perlecan (a specific heparan sulfate proteoglycan) in an animal model of fibrillar Aβ amyloid deposition in vivo: Comparison of Aβ (1-42) versus Aβ (1-40)
    • Snow A. D., Cummings J. A., Ngo C. T., Yang W., Nochlin D., Rimvall K., Sheardown M. J., and Judge M. (1995b) Further studies implicating the importance of perlecan (a specific heparan sulfate proteoglycan) in an animal model of fibrillar Aβ amyloid deposition in vivo: comparison of Aβ (1-42) versus Aβ (1-40). Soc. Neurosci. Abstr. 21, 1282.
    • (1995) Soc. Neurosci. Abstr. , vol.21 , pp. 1282
    • Snow, A.D.1    Cummings, J.A.2    Ngo, C.T.3    Yang, W.4    Nochlin, D.5    Rimvall, K.6    Sheardown, M.J.7    Judge, M.8
  • 76
    • 0029881267 scopus 로고    scopus 로고
    • Identification and immunolocalization of a new class of proteoglycan (keratan sulfate) to the neuritic plaques of Alzheimer's disease
    • Snow A. D., Nochlin D., Sekiguchi R., and Carlson S. S. (1996) Identification and immunolocalization of a new class of proteoglycan (keratan sulfate) to the neuritic plaques of Alzheimer's disease. Exp. Neurol. 138, 305-317.
    • (1996) Exp. Neurol. , vol.138 , pp. 305-317
    • Snow, A.D.1    Nochlin, D.2    Sekiguchi, R.3    Carlson, S.S.4
  • 79
    • 0026468915 scopus 로고
    • Localization of heparan sulfate glycosaminoglycan and proteoglycan core protein in aged brain and Alzheimer's disease
    • Su J. H., Cummings B. J., and Cotman C. W. (1992) Localization of heparan sulfate glycosaminoglycan and proteoglycan core protein in aged brain and Alzheimer's disease. Neuroscience 51, 801-813.
    • (1992) Neuroscience , vol.51 , pp. 801-813
    • Su, J.H.1    Cummings, B.J.2    Cotman, C.W.3
  • 80
    • 0019494341 scopus 로고
    • Some morphometric aspects of the brain in senile dementia of the Alzheimer type
    • Terry R. D., Peck A., DeTeresa R., Schecter R., and Horoupian D. S. (1981) Some morphometric aspects of the brain in senile dementia of the Alzheimer type. Ann. Neurol. 10, 184-192.
    • (1981) Ann. Neurol. , vol.10 , pp. 184-192
    • Terry, R.D.1    Peck, A.2    DeTeresa, R.3    Schecter, R.4    Horoupian, D.S.5
  • 81
    • 0026060658 scopus 로고
    • Acidic fibroblast growth factor-like immunoreactivity in brain of Alzheimer's disease patients
    • Tooyama I., Akiyama H., McGeer P. L., Hara Y., Yasuhara D., and Kimura H. (1991) Acidic fibroblast growth factor-like immunoreactivity in brain of Alzheimer's disease patients. Neurosci. Lett. 121, 155-158.
    • (1991) Neurosci. Lett. , vol.121 , pp. 155-158
    • Tooyama, I.1    Akiyama, H.2    McGeer, P.L.3    Hara, Y.4    Yasuhara, D.5    Kimura, H.6
  • 82
    • 0027524964 scopus 로고
    • Heparan sulfate expression patterns in the amyloid deposits of patients with Alzheimer's and Lewy body type dementia
    • Van Gool D., David G., Lammens M., Baro F., and Dom R. (1993) Heparan sulfate expression patterns in the amyloid deposits of patients with Alzheimer's and Lewy body type dementia. Dementia 4, 308-314.
    • (1993) Dementia , vol.4 , pp. 308-314
    • Van Gool, D.1    David, G.2    Lammens, M.3    Baro, F.4    Dom, R.5
  • 83
    • 0028122463 scopus 로고
    • Differences in the pattern of hippocampal neuronal loss in normal ageing and Alzheimer's disease
    • West M. J., Coleman P. D., Flood D. G., and Troncoso J. C. (1994) Differences in the pattern of hippocampal neuronal loss in normal ageing and Alzheimer's disease. Lancet 344, 769-772.
    • (1994) Lancet , vol.344 , pp. 769-772
    • West, M.J.1    Coleman, P.D.2    Flood, D.G.3    Troncoso, J.C.4
  • 84
    • 0029049168 scopus 로고
    • The extracellular matrix and atherosclerosis
    • Wight T. N. (1995) The extracellular matrix and atherosclerosis. Curr. Opin. Lipidol. 6, 326-334.
    • (1995) Curr. Opin. Lipidol. , vol.6 , pp. 326-334
    • Wight, T.N.1
  • 85
    • 0025201985 scopus 로고
    • In situ hybridization to human chromosome 1 of a cDNA probe for the gene encoding the basement membrane heparan sulfate proteoglycan (HSPG)
    • Wintle R. F., Kisilevsky R., Noonan D., and Duncan A. M. V. (1990) In situ hybridization to human chromosome 1 of a cDNA probe for the gene encoding the basement membrane heparan sulfate proteoglycan (HSPG). Cytogenet. Cell Genet. 54, 60-61.
    • (1990) Cytogenet. Cell Genet. , vol.54 , pp. 60-61
    • Wintle, R.F.1    Kisilevsky, R.2    Noonan, D.3    Duncan, A.M.V.4
  • 86
    • 0026688125 scopus 로고
    • Localization of the basement membrane heparan sulfate proteoglycan in islet amyloid deposits in type II diabetes mellitus
    • Young I. D., Ailles L., Narindrasorasak S., Tan R., and Kisilevsky R. (1992) Localization of the basement membrane heparan sulfate proteoglycan in islet amyloid deposits in type II diabetes mellitus. Arch. Pathol. Lab. Med. 116, 951-954.
    • (1992) Arch. Pathol. Lab. Med. , vol.116 , pp. 951-954
    • Young, I.D.1    Ailles, L.2    Narindrasorasak, S.3    Tan, R.4    Kisilevsky, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.