Tryptase and kinin generation: tryptase from human mast cells does not activate human urinary prokallikrein.
The effect of tryptase, a neutral protease released from human lung mast cell secretory granules, on the tissue prokallikrein present in human urine was examined. Tryptase has been shown previously to lack activity against plasma prokallikrein. Purified tryptase was incubated with a concentrated preparation of urinary prokallikrein. No increase in kallikrein-like enzymatic activity or immunoreactive tissue kallikrein was detected. Activation of urinary prokallikrein with trypsin served as a positive control. Furthermore, preincubation of urinary prokallikrein with tryptase did not diminish the subsequent activation of urinary prokallikrein by trypsin. Therefore, tryptase neither activates nor destroys human tissue or plasma prokallikreins.
Alter
S C
SC
Yates
P
P
Margolius
H S
HS
Schwartz
L B
LB
D004792:Enzyme Precursors / Q000652:urine*; D006801:Humans; D007610:Kallikreins / Q000378:metabolism / Q000652:urine*; D008407:Mast Cells / Q000378:metabolism; D010447:Peptide Hydrolases / Q000494:pharmacology*; D011288:Prekallikrein / Q000652:urine*; D014357:Trypsin / Q000494:pharmacology
D004792:Enzyme Precursors; D011288:Prekallikrein; D010447:Peptide Hydrolases; C023073:tosylarginine methyl ester hydrolase; D007610:Kallikreins; C052910:prokallikrein, tissue; D014357:Trypsin