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Folding related dimerization of human cystatin C

In English

Författare

Summary, in English

With the aim to improve our understanding of the structural basis for protein self-association and aggregation, in particular in relationship to protein refolding and amyloid formation, folding-related processes for human cystatin C have been studied. Using NMR spectroscopy together with chromatographic and electrophoretic methods, a self-association process resulting in dimer formation for protein samples treated with denaturing agents as well as for samples subjected to low pH or high temperature conditions could be studied with amino acid resolution. In all three cases, the dimerization involves properly folded molecules and proceeds via the reactive site of the inhibitor, which leads to complete loss of its biological activity. This dimerization process has potential relevance for amyloid formation by the brain hemorrhage-causing Leu-Gln variant of cystatin C. The results also indicate that cystatin C dimerization and inactivation may occur in acidified compartments in vivo, which could be relevant for the physiological regulation of cysteine proteinase activity.

Publiceringsår

1996

Språk

Engelska

Sidor

1314-1321

Publikation/Tidskrift/Serie

Journal of Biological Chemistry

Volym

271

Issue

3

Dokumenttyp

Artikel i tidskrift

Förlag

American Society for Biochemistry and Molecular Biology

Ämne

  • Pharmacology and Toxicology
  • Medicinal Chemistry

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 1083-351X