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The aminoterminal portion of cerebrospinal fluid cystatin C in hereditary cystatin C amyloid angiopathy is not truncated. Direct sequence analysis from agarose gel electropherograms

Olafsson, I; Gudmundsson, G; Abrahamson, Magnus LU ; Jensson, O and Grubb, Anders LU (1990) In Scandinavian Journal of Clinical & Laboratory Investigation 50(1). p.85-93
Abstract
The isolated amyloid substance in hereditary cystatin C amyloid angiopathy (HCCAA) is mainly composed of a cystatin C variant devoid of the 10 amino terminal amino acid residues of extracellular cystatin C from healthy individuals. We have developed a procedure for protein sequencing directly from agarose gel electropherograms and used this in conjunction with isoelectric focusing to investigate the amino terminal sequence of cerebrospinal fluid (CSF) cystatin C in HCCAA patients. The amino-terminal sequence determined for cystatin C from a HCCAA patient CSF sample, Xaa-Ser-Pro-Gly-Lys-Pro-Pro-Xaa-Leu-Val-Gly-Gly-Pro-Met-Xaa-Ala-Xaa-Val, showed that the protein was not amino-termi-nally truncated. CSF cystatin C from all nine HCCAA... (More)
The isolated amyloid substance in hereditary cystatin C amyloid angiopathy (HCCAA) is mainly composed of a cystatin C variant devoid of the 10 amino terminal amino acid residues of extracellular cystatin C from healthy individuals. We have developed a procedure for protein sequencing directly from agarose gel electropherograms and used this in conjunction with isoelectric focusing to investigate the amino terminal sequence of cerebrospinal fluid (CSF) cystatin C in HCCAA patients. The amino-terminal sequence determined for cystatin C from a HCCAA patient CSF sample, Xaa-Ser-Pro-Gly-Lys-Pro-Pro-Xaa-Leu-Val-Gly-Gly-Pro-Met-Xaa-Ala-Xaa-Val, showed that the protein was not amino-termi-nally truncated. CSF cystatin C from all nine HCCAA patients investigated was found to have an isoelectric point identical to that of native cystatin C, and the truncated form of cystatin C isolated from amyloid deposits was shown to contribute to less than 1 % of the total amount of cystatin C in CSF. The total cysteine proteinase inhibitory capacity of CSF from HCCAA patients was lower than that of CSF from other patients. This decreased CSF inhibitory capacity in HCCAA patients was caused by decreased levels of cystatin C, since the levels of the other two cysteine proteinase inhibitors found in CSF, oc2-macroglobulin and kininogen, were significantly higher than in CSF from non-HCCAA patients. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
agarose gel electrophoresis, amino acid sequence analysis, amyloidosis, cerebral haemorrhage, cystatin C, cysteine proteinase inhibitor
in
Scandinavian Journal of Clinical & Laboratory Investigation
volume
50
issue
1
pages
85 - 93
publisher
Informa Healthcare
external identifiers
  • scopus:0025157221
ISSN
1502-7686
DOI
10.3109/00365519009091569
language
English
LU publication?
yes
id
d863f6c4-aa6b-480f-bdd7-99fc8c255a71 (old id 1105537)
date added to LUP
2008-08-05 17:16:17
date last changed
2017-07-30 04:28:07
@article{d863f6c4-aa6b-480f-bdd7-99fc8c255a71,
  abstract     = {The isolated amyloid substance in hereditary cystatin C amyloid angiopathy (HCCAA) is mainly composed of a cystatin C variant devoid of the 10 amino terminal amino acid residues of extracellular cystatin C from healthy individuals. We have developed a procedure for protein sequencing directly from agarose gel electropherograms and used this in conjunction with isoelectric focusing to investigate the amino terminal sequence of cerebrospinal fluid (CSF) cystatin C in HCCAA patients. The amino-terminal sequence determined for cystatin C from a HCCAA patient CSF sample, Xaa-Ser-Pro-Gly-Lys-Pro-Pro-Xaa-Leu-Val-Gly-Gly-Pro-Met-Xaa-Ala-Xaa-Val, showed that the protein was not amino-termi-nally truncated. CSF cystatin C from all nine HCCAA patients investigated was found to have an isoelectric point identical to that of native cystatin C, and the truncated form of cystatin C isolated from amyloid deposits was shown to contribute to less than 1 % of the total amount of cystatin C in CSF. The total cysteine proteinase inhibitory capacity of CSF from HCCAA patients was lower than that of CSF from other patients. This decreased CSF inhibitory capacity in HCCAA patients was caused by decreased levels of cystatin C, since the levels of the other two cysteine proteinase inhibitors found in CSF, oc2-macroglobulin and kininogen, were significantly higher than in CSF from non-HCCAA patients.},
  author       = {Olafsson, I and Gudmundsson, G and Abrahamson, Magnus and Jensson, O and Grubb, Anders},
  issn         = {1502-7686},
  keyword      = {agarose gel electrophoresis,amino acid sequence analysis,amyloidosis,cerebral haemorrhage,cystatin C,cysteine proteinase inhibitor},
  language     = {eng},
  number       = {1},
  pages        = {85--93},
  publisher    = {Informa Healthcare},
  series       = {Scandinavian Journal of Clinical & Laboratory Investigation},
  title        = {The aminoterminal portion of cerebrospinal fluid cystatin C in hereditary cystatin C amyloid angiopathy is not truncated. Direct sequence analysis from agarose gel electropherograms},
  url          = {http://dx.doi.org/10.3109/00365519009091569},
  volume       = {50},
  year         = {1990},
}