Elastase--does this enzyme play any role in bladder cancer invasion?
Elastase activity in bladder cancer tissue and normal bladder epithelium was assayed with succinyl trialanine paranitroanilide (Suc-Ala3-NA), a synthetic substrate of elastase. Elastase in the tissue extract liberated paranitroanilide (NA) from Suc-Ala3-NA and coexistant endopeptidases produced alanine-NA and dialanine-NA. These products were detected by high performance liquid chromatography. All activities of elastase and endopeptidases in bladder cancer tissues from 20 patients are significantly higher than those in 17 normal bladder epithelia. In 20 bladder cancer cases evaluated, the relation between the activities of elastase and endopeptidases and the background factors of each bladder cancer case was examined. There was a significantly different activity of elastase between the superficial bladder cancer group (less than or equal to T1) and the invasive group (T2 less than or equal to). Elastase is assumed to play an important role in cancer invasion.
D002295:Carcinoma, Transitional Cell / Q000201:enzymology* / Q000473:pathology; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000378:metabolism; D006801:Humans; D009361:Neoplasm Invasiveness; D009842:Oligopeptides; D010196:Pancreatic Elastase / Q000378:metabolism*; D001743:Urinary Bladder / Q000201:enzymology*; D001749:Urinary Bladder Neoplasms / Q000201:enzymology* / Q000473:pathology
D009842:Oligopeptides; C015516:succinyl-trialanine-4-nitroanilide; D010450:Endopeptidases; D010196:Pancreatic Elastase