Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0024141 (systemic lupus erythematosus)
 44,322 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cathepsin D-like activity was measured in the sera of 62 patients with active systemic lupus erythematosus (SLE), 9 patients with progressive systemic sclerosis, 9 patients with chronic glomerulonephritis and 18 with glomerulonephritis with nephrosis syndrome. The in vitro and in vivo effect of corticosteroid treatment on enzyme activity was also investigated. Cathepsin D-like activity appeared measurably in the sera of all patient groups but not in controls. The highest values were found in SLE patients. The increase in serum activity correlated with renal involvement. In vivo corticosteroid treatment significantly decreased serum activity in all groups except in systemic sclerosis patients. In vitro prednisolone treatment decreased enzyme activity in a dose-dependent manner. Determination of serum cathepsin D-like activity seems to be useful in the establishment of diagnosis and prognosis of SLE. Cathepsin D may be of pathogenetic significance in autoimmune disease especially in SLE.
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PMID:Cathepsin D-like activity in serum of patients with systemic lupus erythematosus. 263 63

The isolated cathepsin D-like enzyme from Atlantic cod (Gadus morhua L.) liver was shown to be a monomer with a molecular mass of approximately 40 kDa. It was inhibited by Pepstatin A and had an optimum for degradation of haemoglobin at pH 3.0. The purified enzyme had lower temperature stability than bovine cathepsin D. Antibodies raised against the purified enzyme and against two C-terminal peptides of cod cathepsin D recognized a 40 kDa protein in immunoblotting of the samples from the purification process. Both antisera showed cross reactivity with a similar sized protein in liver from cod, saithe (Pollachius virens L.), Atlantic herring (Clupea harengus L.) and Atlantic salmon (Salmo salar L.). A protein of same size was detected in wolffish (Anarhichas lupus L.) liver with the antibody directed against the purified enzyme. This antibody also recognized the native enzyme and detected the presence of cathepsin D in muscle of cod, saithe, herring and salmon. These antibodies may be useful in understanding the mechanisms of post mortem muscle degradation in fish by comparing immunohistochemical localization and enzyme activity, in particular in cod with different rate of muscle degradation. They may also be used for comparing muscle degradation in different fish species.
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PMID:Cathepsin D from Atlantic cod (Gadus morhua L.) liver. Isolation and comparative studies. 1742 19