Chemotactic activity of elastin-derived peptides for human polymorphonuclear leukocytes and their effect on hydrogen peroxide and myeloperoxidase release. 
The chemotactic activity of elastin-derived peptides (EP) for human polymorphonuclear leukocytes (PMNL) was investigated using the under agarose method.  The EP were produced by digesting the bovine ligament elastin with porcine pancreatic elastase.  Thus prepared digest had weak chemotactic activity for PMNL.  The mean chemotactic index for all tested EP concentrations did not exceed 1.30 and was lower than that obtained with zymosan-activated serum (ZAS, n-formyl-methionyl-leucyl-phenylalanine (FMLP) 2.2 +/- 0.40, 3.1 +/- 0.32, (n = 10) respectively.  However, EP (50 micrograms) after injection to the mouse pleural cavity induced PMNL influx.  The mean PMNL number found in this cavity was 0.09 +/- 0.03 x 10(6) for PBS and 0.18 +/- 0.03 +/- 10(6) for EP injection (p less than 0.01 n = 6).  Human PMNL during 60 min incubation with EP (1 to 10 micrograms/ml) or with EP and cytochalasin B (CB 4.8 micrograms/ml) released myeloperoxidase and low amounts of hydrogen peroxide.  At 1 micrograms/ml and in presence of CB elastin digest was nearly as active in myeloperoxidase release as FMLP (300 ng/ml).  The values reached 17.1 +/- 2.5 and 19.7 +/- 2.1% of the total activity of whole cell lysate, respectively.  The obtained results suggest that EP produced in vivo in the site of inflammation could modulate to some extent its course by enhancing PMNL influx and their activation.  It seems that such mechanism of enhancement of the inflammatory response may occur in the lungs which are rich in elastin fibers.