The aminoterminal portion of cerebrospinal fluid cystatin C in hereditary cystatin C amyloid angiopathy is not truncated. Direct sequence analysis from agarose gel electropherograms
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1105537
- author
- Olafsson, I ; Gudmundsson, G ; Abrahamson, Magnus LU ; Jensson, O and Grubb, Anders LU
- organization
- publishing date
- 1990
- 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
- 2016-04-01 15:37:46
- date last changed
- 2021-01-03 06:30:57
@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}}, keywords = {{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}}, doi = {{10.3109/00365519009091569}}, volume = {{50}}, year = {{1990}}, }