Human Leukocyte Elastase Inhibition

Dual inhibition of 5-LO and HLE enzymes is unique to the Boswellic acids

Boswellic acids have been studied for their ability to interact with 5-lipoxygenase (5-LO) and human leukocyte elastase (HLE), enzymes involved in the body’s natural inflammatory response. These enzymes, produced by polymorphonuclear leukocytes (PMNLs), play a role in the body’s defense mechanisms. Research suggests that Boswellic acids may support the body’s maintenance of normal enzyme activity, contributing to overall health and well-being.

This dual inhibitory action of two pathophysiologically important enzyme activities (HLE and 5-LO) is unique to the pentacyclic triterpenes from the boswellic acid series. Several leukotriene biosynthesis inhibitors furnished no HLE inhibitory activity (as shown below). The β-boswellic acid, acetyl-11-keto-β-boswellic acid (AKBBA), ursolic acid, and amyrin significantly inhibited HLE. The HLE inhibition activity of AKBBA and ursolic acid were comparable; however, ursolic acid’s mode of inhibition is competitive (Safayhi et al., 1997).

Boswellin-human-leukocyte-elastase-inhibition
HLE activity in the presence of leukotriene synthesis inhibitors and cyclic as well as noncyclic hydrophobic compounds