Cationic antimicrobial protein of M(r) 37 kDa (CAP37) is a multifuncti
onal protein isolated from the granules of human neutrophils, which ha
s important implications in host defense and inflammation, CAP37 was i
nitially recognized for its strong antibiotic activity against Gram-ne
gative bacteria and was viewed as a component of the oxygen-independen
t killing mechanism of the neutrophil, However, we now know that CAP37
has more far reaching and important functions, It is a physiological
protein released during inflammation with a high potential of regulati
ng monocyte/macrophage functions, such as chemotaxis, increased surviv
al, and differentiation, Recently, it has been demonstrated that CAP37
binds endotoxin, It has the structure of a serine esterase but lacks
enzymatic activity, The bactericidal and endotoxin binding domains of
the molecule have been delineated, The identification of functional pe
ptides should provide new insight into the mechanisms of endotoxin bin
ding, antimicrobial activity, and chemotaxis and in the long term prov
ide key insights into therapies for treating infections and endotoxic
shock.