LOCAL KALLIKREIN AND TRYPSIN RESPONSES IN THE RAT

Article date: August 1980

By: A.J. BENNETT, G.B. WEST, in Volume 69, Issue 4, pages 625-629

Locally administered commercial hog pancreatic kallikrein (Depot‐Glumorin) and bovine pancreatic tyrpsin both increased vascular permeability in the skin and paws of rats.

By the use of numerous antagonists and enzyme inhibitors, this vascular response was found to be the result not of kinin formation but of a direct action mostly on histamine receptors.

Highly purified kallikrein did not increase vascular permeability in rats, suggesting either that the effect was due to an impurity in the commercial preparation or that a structural change in the enzyme occurred on purification.

Soya bean trypsin inhibitor prevented the trypsin response when both were injected locally. On intraperitoneal injection, the inhibitor was effective only against local kallikrein.

The kallikrein inhibitor, aprotinin (Trasylol), was not effective against local kallikrein but it reduced the trypsin response when both were injected locally.

Locally administered commercial hog pancreatic kallikrein (Depot‐Glumorin) and bovine pancreatic tyrpsin both increased vascular permeability in the skin and paws of rats.

By the use of numerous antagonists and enzyme inhibitors, this vascular response was found to be the result not of kinin formation but of a direct action mostly on histamine receptors.

Highly purified kallikrein did not increase vascular permeability in rats, suggesting either that the effect was due to an impurity in the commercial preparation or that a structural change in the enzyme occurred on purification.

Soya bean trypsin inhibitor prevented the trypsin response when both were injected locally. On intraperitoneal injection, the inhibitor was effective only against local kallikrein.

The kallikrein inhibitor, aprotinin (Trasylol), was not effective against local kallikrein but it reduced the trypsin response when both were injected locally.

DOI: 10.1111/j.1476-5381.1980.tb07913.x

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