Bactericidal, proteolytic and signal proteins released by activated neutrop
hils play a major role in infection fighting and inflammatory processes. Th
ese proteins are mainly stored in organelles called granules until inductio
n of their controlled exocytosis. The present work deals with the character
ization of the proteins which are secreted upon activation of human neutrop
hils by ionomycin and calcium. Proteins were separated by two-dimensional g
el electrophoresis and identified by peptide mass fingerprinting. Almost al
l the previously described soluble components of neutrophil granules could
be identified. Moreover, several additional proteins were shown to be secre
ted by activated neutrophils, namely calgranulins, human cartilage glycopro
tein of 39 kDa (HC gp-39), chitotriosidase, and annexin XI. Their subcellul
ar localization and possible functions are discussed.