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Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C. Use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C

Nilsson, M. (författare)
Department of Clinical Chemistry, University Hospital, S-22185 Lund, Sweden
Wang, Xin (författare)
Lund University,Lunds universitet,Avdelningen för klinisk kemi och farmakologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Clinical Chemistry and Pharmacology,Department of Laboratory Medicine,Faculty of Medicine,Department of Clinical Chemistry, University Hospital, S-22185 Lund, Sweden
Rodziewicz-Motowidlo, S. (författare)
Department of Organic Chemistry, Faculty of Chemistry, University of Gdansk, J. Sobieskiego 18, 80-952 Gdansk, Poland
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Janowski, R. (författare)
Department of Crystallography, A. Mickiewicz University, Polish Academy of Sciences, Grunwaldzka 6, 60-780 Poznan, Poland,Adam Mickiewicz University in Poznań
Lindström, Veronica (författare)
Lund University,Lunds universitet,Avdelningen för klinisk kemi och farmakologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Clinical Chemistry and Pharmacology,Department of Laboratory Medicine,Faculty of Medicine,Lindström, V., Department of Clinical Chemistry, University Hospital, S-22185 Lund, Sweden
Önnerfjord, Patrik (författare)
Lund University,Lunds universitet,Reumatologi och molekylär skelettbiologi,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Rheumatology,Section III,Department of Clinical Sciences, Lund,Faculty of Medicine,Önnerfjord, P., Dept. of Cell and Molecular Biology, University of Lund, S-22184 Lund, Sweden
Westermark, Gunilla (författare)
Linköping University,Linköpings universitet,Hälsouniversitetet,Cellbiologi
Grzonka, Z. (författare)
Department of Organic Chemistry, Faculty of Chemistry, University of Gdansk, J. Sobieskiego 18, 80-952 Gdansk, Poland
Jaskolski, M. (författare)
Department of Crystallography, A. Mickiewicz University, Polish Academy of Sciences, Grunwaldzka 6, 60-780 Poznan, Poland,Adam Mickiewicz University in Poznań
Grubb, Anders (författare)
Lund University,Lunds universitet,Avdelningen för klinisk kemi och farmakologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Clinical Chemistry and Pharmacology,Department of Laboratory Medicine,Faculty of Medicine,Department of Clinical Chemistry, University Hospital, S-22185 Lund, Sweden
Wahlbom, Maria (författare)
Lund University,Lunds universitet,Avdelningen för klinisk kemi och farmakologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Clinical Chemistry and Pharmacology,Department of Laboratory Medicine,Faculty of Medicine
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 (creator_code:org_t)
2004
2004
Engelska.
Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 279:23, s. 24236-24245
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http://www.ncbi.nlm.... (free)
http://dx.doi.org/10... (free)
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https://doi.org/10.1...
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  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • Amyloidogenic proteins like cystatin C and prion proteins have been shown to form dimers by exchange of subdomains of the monomeric proteins. This process, called "three-dimensional domain swapping," has also been suggested to play a part in the generation of amyloid fibrils. One variant of cystatin C, L68Q cystatin C, is highly amyloidogenic, and persons carrying the corresponding gene suffer from massive cerebral amyloidosis leading to brain hemorrhage and death in early adult life. The present work describes the production of two variants of wild type and L68Q cystatin C with disulfide bridges at positions selected to inhibit domain swapping without affecting the biological function of the four cystatin C variants as cysteine protease inhibitors. The capacity of the four variant proteins to form dimers was tested and compared with that of wild type and L68Q cystatin C. In contrast to the latter two proteins, all four protein variants stabilized by disulfide bridges were resistant toward the formation of dimers. The capacity of the two stabilized variants of wild type cystatin C to form amyloid fibrils was investigated and found to be reduced by 80% compared with that of wild type cystatin C. In an effort to investigate whether exogenous agents could also suppress the formation of dimers of wild type and L68Q cystatin C, a monoclonal antibody or carboxymethylpapain, an inactivated form of a cysteine protease, was added to systems inducing dimerization of wild type and L68Q cystatin C. It was observed that catalytic amounts of both the monoclonal antibody and carboxymethylpapain could suppress dimerization.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)

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MEDICINE
MEDICIN

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