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Sökning: WFRF:(Frangione B)

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1.
  • Kanai, M, et al. (författare)
  • 2023
  • swepub:Mat__t
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  • Jensson, O, et al. (författare)
  • Hereditary cystatin C (gamma-trace) amyloid angiopathy of the CNS causing cerebral hemorrhage
  • 1987
  • Ingår i: Acta Neurologica Scandinavica. - : Hindawi Limited. - 0001-6314 .- 1600-0404. ; 76:2, s. 102-114
  • Tidskriftsartikel (refereegranskat)abstract
    • Hereditary CNS amyloid angiopathy occurring in Icelanders is the first human disorder known to be caused by deposition of cystatin C amyloid fibrils in the walls of the brain arteries leading to single or or multiple strokes with fatal outcome. One or more affected members have been verified by histological examination in 8 families containing 127 affected. These originated from the same geographic area. Abnormally low value of cystatin C found in the cerebrospinal fluid of those affected can be used to support or make diagnosis of this disease, also in asymptomatic relatives. By amino acid sequence analysis the amyloid fibrils in the patients are found to be a variant of cystatin C (gamma-trace), a major cysteine proteinase inhibitor. The variant protein has an amino acid substitution (glutamine for leucine) at position 58 in the amyloid molecule. It is postulated that a point mutation has occurred leading to production of amyloidogenic protein causing the disorder.
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  • Mendez, E, et al. (författare)
  • Human complex-forming glycoprotein, heterogeneous in charge : the primary structure around the cysteine residues and characterization of a disulfide bridge
  • 1982
  • Ingår i: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861. ; 213:1, s. 50-240
  • Tidskriftsartikel (refereegranskat)abstract
    • The amino acid sequence of the cysteine-containing regions of human complex-forming glycoprotein, heterogeneous in charge (protein HC) was determined by studies of the tryptic peptides of the completely reduced and radioalkylated protein. One of the cysteines was located in the amino-terminal part of the molecule at position 34....Diagonal map electrophoresis showed that the cysteine residue in the carboxy-terminal region was bridged to the cysteine containing sequence in the middle of the molecule. The function of the cysteine residue at position 34 remains elusive since the residue was not found on the diagonal maps. The release of cysteic acid and a small cysteic acid containing peptide after oxidation of the native protein HC molecule suggests that this cysteine residue may be involved in disulfide bridges with cysteine and small cysteine containing peptides.
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  • Resultat 1-6 av 6

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