Mouse and rat cystatin C: Escherichia coli production, characterization and tissue distribution
Håkansson, Katarina LU ; Huh, Changgoo ; Grubb, Anders LU
; Karlsson, Stefan
LU
and Abrahamson, Magnus
LU
(1996)
In Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology
114(3).
p.303-311
- Abstract
- Recombinant mouse (Mus musculus) and rat (Rattus norvegicus) cystatin C were produced by expression in Escherichia coli, isolated and functionally characterized. The mouse and rat inhibitors were both fully active in titrations of papain. Determination of equilibrium constants for dissociation (Ki) for their complexes with the target proteinase, cathepsin B, produced values not largely different from that for human cystatin C (Ki 0.07-0.13 nM). Rabbit antisera against mouse and rat cystatin C were produced and used for improved affinity purification of the recombinant inhibitors. Affinity purified immunoglobulins isolated from the antiserum against mouse cystatin C were used for construction of a sensitive enzyme-linked immunosorbent... (More)
- Recombinant mouse (Mus musculus) and rat (Rattus norvegicus) cystatin C were produced by expression in Escherichia coli, isolated and functionally characterized. The mouse and rat inhibitors were both fully active in titrations of papain. Determination of equilibrium constants for dissociation (Ki) for their complexes with the target proteinase, cathepsin B, produced values not largely different from that for human cystatin C (Ki 0.07-0.13 nM). Rabbit antisera against mouse and rat cystatin C were produced and used for improved affinity purification of the recombinant inhibitors. Affinity purified immunoglobulins isolated from the antiserum against mouse cystatin C were used for construction of a sensitive enzyme-linked immunosorbent assay. The assay was used to demonstrate a high degree of immunological cross-reactivity between mouse and rat cystatin C and could be used for cystatin C quantification in mouse and rat tissue homogenates. All tissues analyzed contained cystatin C, with a relative content very similar to that of human tissues. For all species, brain tissue contained the highest cystatin C amounts and liver the lowest, whereas kidney, spleen and muscle tissues were intermediate in content. In the mouse, a notable high cystatin C content in parotid gland tissue was observed. The high degree of similarity in distribution pattern and functional properties for mouse, rat and human cystatin C indicates that a murine model should be relevant for studies of the human disease, hereditary cystatin C amyloid angiopathy. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1111050
- author
- Håkansson, Katarina
LU
; Huh, Changgoo
; Grubb, Anders
LU
; Karlsson, Stefan
LU
and Abrahamson, Magnus
LU
- organization
- publishing date
- 1996
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Cathepsin B, cysteine proteinase inhibitor, cysteine proteinases, E. coli expression, enzymelinkedimmunosorbent assay, hereditary cystatin C amyloid angiopathy, amyloidosis
- in
- Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology
- volume
- 114
- issue
- 3
- pages
- 303 - 311
- publisher
- Pergamon Press Ltd.
- external identifiers
-
- scopus:0029744913
- wos:A1996VA46500011
- ISSN
- 1879-1107
- DOI
- 10.1016/0305-0491(96)00025-9
- language
- English
- LU publication?
- yes
- id
- 80bd862f-f3bc-4073-bbf4-915d0c6fc003 (old id 1111050)
- date added to LUP
- 2016-04-01 11:52:39
- date last changed
- 2023-03-09 20:16:09
@article{80bd862f-f3bc-4073-bbf4-915d0c6fc003,
abstract = {{Recombinant mouse (Mus musculus) and rat (Rattus norvegicus) cystatin C were produced by expression in Escherichia coli, isolated and functionally characterized. The mouse and rat inhibitors were both fully active in titrations of papain. Determination of equilibrium constants for dissociation (Ki) for their complexes with the target proteinase, cathepsin B, produced values not largely different from that for human cystatin C (Ki 0.07-0.13 nM). Rabbit antisera against mouse and rat cystatin C were produced and used for improved affinity purification of the recombinant inhibitors. Affinity purified immunoglobulins isolated from the antiserum against mouse cystatin C were used for construction of a sensitive enzyme-linked immunosorbent assay. The assay was used to demonstrate a high degree of immunological cross-reactivity between mouse and rat cystatin C and could be used for cystatin C quantification in mouse and rat tissue homogenates. All tissues analyzed contained cystatin C, with a relative content very similar to that of human tissues. For all species, brain tissue contained the highest cystatin C amounts and liver the lowest, whereas kidney, spleen and muscle tissues were intermediate in content. In the mouse, a notable high cystatin C content in parotid gland tissue was observed. The high degree of similarity in distribution pattern and functional properties for mouse, rat and human cystatin C indicates that a murine model should be relevant for studies of the human disease, hereditary cystatin C amyloid angiopathy.}},
author = {{Håkansson, Katarina and Huh, Changgoo and Grubb, Anders and Karlsson, Stefan and Abrahamson, Magnus}},
issn = {{1879-1107}},
keywords = {{Cathepsin B; cysteine proteinase inhibitor; cysteine proteinases; E. coli expression; enzymelinkedimmunosorbent assay; hereditary cystatin C amyloid angiopathy; amyloidosis}},
language = {{eng}},
number = {{3}},
pages = {{303--311}},
publisher = {{Pergamon Press Ltd.}},
series = {{Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology}},
title = {{Mouse and rat cystatin C: Escherichia coli production, characterization and tissue distribution}},
url = {{http://dx.doi.org/10.1016/0305-0491(96)00025-9}},
doi = {{10.1016/0305-0491(96)00025-9}},
volume = {{114}},
year = {{1996}},
}