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Kinin-forming enzymes in vascular tissue
Advances in Experimental Medicine and Biology
|January 1, 1983
Summary
Vascular tissue contains two kinin-generating enzymes: a cathepsin-like protease and a glandular kallikrein-like enzyme. Both enzymes release bradykinin-like peptides from plasma substrates.
Area of Science:
- Biochemistry
- Physiology
- Enzymology
Background:
- Vascular tissue's enzymatic activity is not fully understood.
- Kinin generation plays a role in vascular function.
Purpose of the Study:
- To investigate the presence and characteristics of kallikrein-like enzymes in rat mesenteric arteries.
- To identify and differentiate enzymes responsible for kinin generation in vascular tissue.
Main Methods:
- Saline-perfused rat mesenteric arteries were used.
- CM-cellulose chromatography separated enzymes.
- Optimal pH and substrate activity were analyzed.
- Antibodies were used to inhibit kinin activity.
Main Results:
- Two enzymes were isolated: a kallikrein-like enzyme (optimal pH 7-9) and an acid protease (optimal pH 4-5).
- Both enzymes released bradykinin-like peptides from plasma substrates.
- Antibody inhibition confirmed the kinin-like nature of the released peptides.
Conclusions:
- Rat arterial tissue contains two distinct kinin-generating enzymes.
- One enzyme resembles lysosomal cathepsin-like proteases.
- The other enzyme exhibits physicochemical properties similar to glandular kallikreins, differing from plasma kallikreins.