Human cathepsin B and cysteine proteinase inhibitors (CPIs) in inflammatory and metabolic joint diseases

Biol Chem Hoppe Seyler. 1988 May:369 Suppl:257-61.

Abstract

Synovial fluid of patients with different inflammatory and metabolic joint diseases contains low-molecular CPIs (stefins and cystatins) and high-molecular CPIs (kininogens). An additional inhibitory fragment with a molecular mass of about 20 kDa, which is a part of the kininogen molecule, has been detected. Cathepsin B and cystatin C were determined by ELISA test in 47 patients with rheumatoid arthritis, seronegative spondylarthritis, osteoarthritis, undifferentiated arthritis and gout. A significantly higher amount of cathepsin B was found in patients with rheumatoid arthritis. The elevation of cathepsin B was accompanied by an increased amount of cystatin C.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cathepsin B / physiology*
  • Chromatography, Affinity
  • Cysteine Proteinase Inhibitors
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme-Linked Immunosorbent Assay
  • Humans
  • Inflammation / physiopathology
  • Joint Diseases / physiopathology*
  • Metabolic Diseases / physiopathology
  • Molecular Sequence Data
  • Protease Inhibitors / analysis
  • Protease Inhibitors / isolation & purification
  • Protease Inhibitors / physiology*
  • Synovial Fluid / analysis

Substances

  • Cysteine Proteinase Inhibitors
  • Protease Inhibitors
  • Cathepsin B