The cerebral hemorrhage-producing cystatin C variant (L68Q) in extracellular fluids
Bjarnadottir, M. ; Nilsson, C. ; Lindström, Veronica LU
; Westman, A.
; Davidsson, P.
; Thormodsson, F.
; Blondal, H.
; Gudmundsson, G.
and Grubb, Anders
LU
(2001)
In Amyloid
8(1).
p.41284-41284
- Abstract
- A variant of the normal extracellular cysteine protease inhibitor cystatin C (L68Q-cystatin C), is the amyloid precursor in hereditary cystatin C amyloid angiopathy (HCCAA). It has been suggested that the mutation causes cellular entrapment of L68Q-cystatin C in vivo and that the variant protein is not secreted to extracellular fluids. In order to test this hypothesis, we used matrix-assisted laser desorption ionization time-of-flight mass spectrometry in an effort to demonstrate the presence of L68Q- along with wildtype cystatin C in plasma and cerebrospinal fluid (CSF) of HCCAA-patients. Plasma from all five investigated HCCAA-patients contained both L68Q- and wildtype cystatin C. The presence of approximately equal amounts of cystatin C... (More)
- A variant of the normal extracellular cysteine protease inhibitor cystatin C (L68Q-cystatin C), is the amyloid precursor in hereditary cystatin C amyloid angiopathy (HCCAA). It has been suggested that the mutation causes cellular entrapment of L68Q-cystatin C in vivo and that the variant protein is not secreted to extracellular fluids. In order to test this hypothesis, we used matrix-assisted laser desorption ionization time-of-flight mass spectrometry in an effort to demonstrate the presence of L68Q- along with wildtype cystatin C in plasma and cerebrospinal fluid (CSF) of HCCAA-patients. Plasma from all five investigated HCCAA-patients contained both L68Q- and wildtype cystatin C. The presence of approximately equal amounts of cystatin C dimers and monomers was demonstrated in plasma from HCCAA-patients, whereas only monomers could be found in normal plasma. L68Q-wildtype-cystatin C heterodimers seem to be present in the dimeric cystatin C population. CSF from six HCCAA-patients also contained cystatin C-dimers and monomers, bur the dimeric fraction was minute. CSF from control patients did not contain dimeric cystatin C. These results suggest that the milieu of L68Q-cystatin C is important for its stability and dimerization status and that certain milieus might hinder its further development into oligomers, amyloid fibrils and other precipiting aggregates. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1119177
- author
- Bjarnadottir, M.
; Nilsson, C.
; Lindström, Veronica
LU
; Westman, A.
; Davidsson, P.
; Thormodsson, F.
; Blondal, H.
; Gudmundsson, G.
and Grubb, Anders
LU
- organization
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Amyloid
- volume
- 8
- issue
- 1
- pages
- 41284 - 41284
- publisher
- Informa Healthcare
- external identifiers
-
- wos:000169107300001
- scopus:0035093468
- ISSN
- 1350-6129
- language
- English
- LU publication?
- yes
- id
- 5ada0d3c-0bc6-4072-ae7d-bec9c66305cf (old id 1119177)
- date added to LUP
- 2016-04-01 16:02:22
- date last changed
- 2025-04-04 14:39:58
@article{5ada0d3c-0bc6-4072-ae7d-bec9c66305cf,
abstract = {{A variant of the normal extracellular cysteine protease inhibitor cystatin C (L68Q-cystatin C), is the amyloid precursor in hereditary cystatin C amyloid angiopathy (HCCAA). It has been suggested that the mutation causes cellular entrapment of L68Q-cystatin C in vivo and that the variant protein is not secreted to extracellular fluids. In order to test this hypothesis, we used matrix-assisted laser desorption ionization time-of-flight mass spectrometry in an effort to demonstrate the presence of L68Q- along with wildtype cystatin C in plasma and cerebrospinal fluid (CSF) of HCCAA-patients. Plasma from all five investigated HCCAA-patients contained both L68Q- and wildtype cystatin C. The presence of approximately equal amounts of cystatin C dimers and monomers was demonstrated in plasma from HCCAA-patients, whereas only monomers could be found in normal plasma. L68Q-wildtype-cystatin C heterodimers seem to be present in the dimeric cystatin C population. CSF from six HCCAA-patients also contained cystatin C-dimers and monomers, bur the dimeric fraction was minute. CSF from control patients did not contain dimeric cystatin C. These results suggest that the milieu of L68Q-cystatin C is important for its stability and dimerization status and that certain milieus might hinder its further development into oligomers, amyloid fibrils and other precipiting aggregates.}},
author = {{Bjarnadottir, M. and Nilsson, C. and Lindström, Veronica and Westman, A. and Davidsson, P. and Thormodsson, F. and Blondal, H. and Gudmundsson, G. and Grubb, Anders}},
issn = {{1350-6129}},
language = {{eng}},
number = {{1}},
pages = {{41284--41284}},
publisher = {{Informa Healthcare}},
series = {{Amyloid}},
title = {{The cerebral hemorrhage-producing cystatin C variant (L68Q) in extracellular fluids}},
volume = {{8}},
year = {{2001}},
}