메뉴 건너뛰기




Volumn 77, Issue 4, 1997, Pages 299-304

Identification of the circulating amyloid precursor and other gelsolin metabolites in patients with G654A mutation in the gelsolin gene (Finnish familial amyloidosis): Pathogenetic and diagnostic implications

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; GELSOLIN;

EID: 0030661879     PISSN: 00236837     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (27)

References (23)
  • 1
    • 0026764358 scopus 로고
    • Familial amyloidosis, Finnish type: G654-A mutation of the gelsolin gene in Finnish families and an unrelated American family
    • de la Chapelle A, Kere J, Sack GH, Tolvanen R, and Maury CPJ (1992a). Familial amyloidosis, Finnish type: G654-A mutation of the gelsolin gene in Finnish families and an unrelated American family. Genomics 13:898-901.
    • (1992) Genomics , vol.13 , pp. 898-901
    • De La Chapelle, A.1    Kere, J.2    Sack, G.H.3    Tolvanen, R.4    Maury, C.P.J.5
  • 3
    • 0028070084 scopus 로고
    • Serum amyloid a protein in mink during endotoxin induced inflammation and amyloidogenesis
    • Foyn-Bruun C, Rygg M, Nordstoga K, Sletten K, and Marhaug G (1994). Serum amyloid A protein in mink during endotoxin induced inflammation and amyloidogenesis. Scand J Immunol 40:337-344.
    • (1994) Scand J Immunol , vol.40 , pp. 337-344
    • Foyn-Bruun, C.1    Rygg, M.2    Nordstoga, K.3    Sletten, K.4    Marhaug, G.5
  • 4
    • 0029817405 scopus 로고    scopus 로고
    • In vitro expression analysis shows that the secretory form of gelsolin is the sole source of amyloid in gelsolin-related amyloidosis
    • Kangas H, Paunio T, Kalkkinen N, Jalanko A, and Peltonen L (1996). In vitro expression analysis shows that the secretory form of gelsolin is the sole source of amyloid in gelsolin-related amyloidosis. Hum Mol Genet 5:1237-1243.
    • (1996) Hum Mol Genet , vol.5 , pp. 1237-1243
    • Kangas, H.1    Paunio, T.2    Kalkkinen, N.3    Jalanko, A.4    Peltonen, L.5
  • 5
    • 0022487183 scopus 로고
    • Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain
    • Kwiatkowski DJ, Stossel TP, Orkin SH, Mole JE, Colten HR, and Yin HL (1986). Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature 323:455-458.
    • (1986) Nature , vol.323 , pp. 455-458
    • Kwiatkowski, D.J.1    Stossel, T.P.2    Orkin, S.H.3    Mole, J.E.4    Colten, H.R.5    Yin, H.L.6
  • 7
    • 0025779730 scopus 로고
    • Gelsolin-related amyloidosis: Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin
    • Maury CPJ (1991a). Gelsolin-related amyloidosis: Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin. J Clin Invest 87:1195-1199.
    • (1991) J Clin Invest , vol.87 , pp. 1195-1199
    • Maury, C.P.J.1
  • 8
    • 0025854054 scopus 로고
    • Immunohistochemical localization of amyloid in Finnish hereditary amyloidosis with antibodies to gelsolin peptides
    • Maury CPJ (1991b). Immunohistochemical localization of amyloid in Finnish hereditary amyloidosis with antibodies to gelsolin peptides. Lab Invest 64:400-404.
    • (1991) Lab Invest , vol.64 , pp. 400-404
    • Maury, C.P.J.1
  • 9
    • 0025139469 scopus 로고
    • Finnish hereditary amyloidosis: Amino acid sequence homology between the amyloid fibril protein and human plasma gelsolin
    • Maury CPJ, Alli K, and Baumann M (1990a). Finnish hereditary amyloidosis: Amino acid sequence homology between the amyloid fibril protein and human plasma gelsolin. FEBS Lett 260:85-87.
    • (1990) FEBS Lett , vol.260 , pp. 85-87
    • Maury, C.P.J.1    Alli, K.2    Baumann, M.3
  • 10
    • 0025966199 scopus 로고
    • Isolation and characterization of cardiac amyloid in familial amyloid polyneuropathy type IV (Finnish): Relation of the amyloid protein to variant gelsolin
    • Maury CPJ and Baumann M (1990). Isolation and characterization of cardiac amyloid in familial amyloid polyneuropathy type IV (Finnish): Relation of the amyloid protein to variant gelsolin. Biochim Biophys Acta 1096:84-86.
    • (1990) Biochim Biophys Acta , vol.1096 , pp. 84-86
    • Maury, C.P.J.1    Baumann, M.2
  • 11
    • 0025666454 scopus 로고
    • Finnish hereditary amyloidosis is caused by a single nucleotide substitution in the gelsolin gene
    • Maury CPJ, Kere J, Tolvanen R, and de la Chapelle A (1990b). Finnish hereditary amyloidosis is caused by a single nucleotide substitution in the gelsolin gene. FEBS Lett 276: 75-77.
    • (1990) FEBS Lett , vol.276 , pp. 75-77
    • Maury, C.P.J.1    Kere, J.2    Tolvanen, R.3    De La Chapelle, A.4
  • 12
    • 0026729321 scopus 로고
    • Homozygosity for the Asn 187 gelsolin mutation in Finnish-type familial amyloidosis is associated with severe renal disease
    • Maury CPJ, Kere J, Tolvanen R, and de la Chapelle A (1992). Homozygosity for the Asn 187 gelsolin mutation in Finnish-type familial amyloidosis is associated with severe renal disease. Genomics 13:903-903.
    • (1992) Genomics , vol.13 , pp. 903-903
    • Maury, C.P.J.1    Kere, J.2    Tolvanen, R.3    De La Chapelle, A.4
  • 13
    • 0026537985 scopus 로고
    • Creation of amyloid fibrils from mutant Asn-187 gelsolin peptides
    • Maury CPJ and Nurmiaho-Lassila E-L (1992). Creation of amyloid fibrils from mutant Asn-187 gelsolin peptides. Biochem Biophys Res Commun 183:227-231.
    • (1992) Biochem Biophys Res Commun , vol.183 , pp. 227-231
    • Maury, C.P.J.1    Nurmiaho-Lassila, E.-L.2
  • 14
    • 0028263333 scopus 로고
    • Amyloid fibril formation in gelsolin-derived amyloidosis: Definition of the amyloidogenic region and evidence of accelerated amyloid formation of mutant Asn-187 and Tyr-187 gelsolin peptides
    • Maury CPJ, Nurmiaho-Lassila E-L, and Rossi H (1994). Amyloid fibril formation in gelsolin-derived amyloidosis: Definition of the amyloidogenic region and evidence of accelerated amyloid formation of mutant Asn-187 and Tyr-187 gelsolin peptides. Lab Invest 70:558-564.
    • (1994) Lab Invest , vol.70 , pp. 558-564
    • Maury, C.P.J.1    Nurmiaho-Lassila, E.-L.2    Rossi, H.3
  • 15
    • 0027338270 scopus 로고
    • Demonstration of a circulating 65K gelsolin variant specific for familial amyloidosis, Finnish type
    • Maury CPJ and Rossi H (1993). Demonstration of a circulating 65K gelsolin variant specific for familial amyloidosis, Finnish type. Biochem Biophys Res Commun 191:41-44.
    • (1993) Biochem Biophys Res Commun , vol.191 , pp. 41-44
    • Maury, C.P.J.1    Rossi, H.2
  • 16
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin PJ, Gooch JT, Mannherz H-G, and Weeds AG (1993). Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 364:685-692.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.-G.3    Weeds, A.G.4
  • 17
    • 0014640130 scopus 로고
    • Familial systemic paramyloidosis with lattice dystrophy of the cornea, progressive cranial neuropathy, skin changes and various internal symptoms: A previously unrecognized heritable syndrome
    • Meretoja J (1969). Familial systemic paramyloidosis with lattice dystrophy of the cornea, progressive cranial neuropathy, skin changes and various internal symptoms: A previously unrecognized heritable syndrome. Ann Clin Res 1:314-324.
    • (1969) Ann Clin Res , vol.1 , pp. 314-324
    • Meretoja, J.1
  • 18
    • 0028567731 scopus 로고
    • Toward understanding the pathogenetic mechanisms in gelsolin-related amyloidosis: In vitro expression reveals an abnormal gelsolin fragment
    • Paunio T, Kangas H, Kalkkinen N, Haltia M, Palo J, and Peltonen L (1994). Toward understanding the pathogenetic mechanisms in gelsolin-related amyloidosis: In vitro expression reveals an abnormal gelsolin fragment. Hum Mol Genet 3:2223-2229.
    • (1994) Hum Mol Genet , vol.3 , pp. 2223-2229
    • Paunio, T.1    Kangas, H.2    Kalkkinen, N.3    Haltia, M.4    Palo, J.5    Peltonen, L.6
  • 19
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional hgel electrophoresis
    • Rosenfeld J, Capdevielle J, Guillemot JC, and Ferrara P (1992). In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional hgel electrophoresis. Anal Biochem 203:173-179.
    • (1992) Anal Biochem , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 20
    • 0027068052 scopus 로고
    • Accelerated high-sensitivity microsequencing of proteins and peptides using a miniature reaction cartridge
    • Totty NF, Waterfield MD, and Hsuan J (1992). Accelerated high-sensitivity microsequencing of proteins and peptides using a miniature reaction cartridge. J Prot Sci 1:1215-1224.
    • (1992) J Prot Sci , vol.1 , pp. 1215-1224
    • Totty, N.F.1    Waterfield, M.D.2    Hsuan, J.3
  • 21
    • 0024318706 scopus 로고
    • Expression of human plasma gelsolin in Eschericia Coli and dissection of actin binding sites by segmental deletion mutagenesis
    • Way M, Gooch J, Pope B, and Weeds AG (1989). Expression of human plasma gelsolin in Eschericia Coli and dissection of actin binding sites by segmental deletion mutagenesis. J Cell Biol 109:593-605.
    • (1989) J Cell Biol , vol.109 , pp. 593-605
    • Way, M.1    Gooch, J.2    Pope, B.3    Weeds, A.G.4
  • 22
    • 0027525430 scopus 로고
    • Variant gelsolin responsible for familial amyloidosis (Finnish type) has defective actin severing activity
    • Weeds AG, Gooch J, McLaughlin P, and Maury CPJ (1993). Variant gelsolin responsible for familial amyloidosis (Finnish type) has defective actin severing activity. FEBS Lett 335: 119-123.
    • (1993) FEBS Lett , vol.335 , pp. 119-123
    • Weeds, A.G.1    Gooch, J.2    McLaughlin, P.3    Maury, C.P.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.