Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.23.5 (cathepsin D)
 4,130 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of anti-inflammatory drugs on the biochemical changes in the Arthus reaction have been studied and correlated to changes in the pathology of the reaction. In the Arthus reaction all the non-steroidal anti-inflammatory drugs inhibited the migration of cells into the lesion and reduced the lysosomal enzyme concentration at the Arthus site. The steroids did not inhibit the cellular inflitration or the total lysosomal enzyme concentration in the skin but did reduce the concentration of cathepsin D in the oedema fluid. In addition, prednisolone and, to a lesser extent, hydrocortisone reduced the degree of oedema formation. The results suggest that non-steroidal anti-inflammatory drugs inhibit the Arthus reaction by reducing the cellular infiltration whereas anti-inflammatory steroids act by preventing these cells secreting their lysosomal enzymes and thus causing tissue damage.
 ...
PMID:The effect of anti-inflammatory compounds on the biochemical changes in the Arthus reaction. 13 38

The papain inhibitor isolated from chicken egg white inhibits the enzymatic activity of cathepsin B1 and cathepsin C. The inhibitor bears two nonoverlapping reactive sites: one binds cathepsin B1, papain, ficin, and bromelain, the other one cathepsin C. The inhibitor decreases the degree of an immunologic hypersensitive reaction, the so-called Arthus reaction. A statistically significant inhibition of this immunologically developed inflammation occurs only if the inhibitor is applied intradermally and simultaneously with the provoking dose of the antigen to rabbits sensitized to the same antigen. The pepsin inhibitor from the body walls of the roundworm Ascaris lumbricoides inhibits the proteolytic activity of cathepsin E. This inhibitor covalently bound to Sepharose 4B was used for affinity chromatography of cathepsin E. A cathepsin D inhibitor was isolated from potato tubers and its inhibitory and chemical characteristics were studied. The inhibitor does not inhibit either cathepsin E or pepsin yet inhibits trypsin in the alkaline pH-range. The molecular weight of the inhibitor is 21 790 and its molecule consists of 199 amino acid residues. The sequence of 17 amino acid residues was determined by Edman degradation of the inhibitor molecule.
 ...
PMID:Naturally occurring inhibitors of intracellular proteinases. 61 34