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Calprotectin‐Mediated Zinc Chelation as a Biostatic Mechanism in Host Defence
Author(s) -
CLOHESSY P. A.,
GOLDEN B. E.
Publication year - 1995
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1995.tb03695.x
Subject(s) - calprotectin , zinc , chelation , chemistry , incubation , in vitro , corpus albicans , candida albicans , growth inhibition , microbiology and biotechnology , biochemistry , biology , medicine , inflammatory bowel disease , disease , organic chemistry
The S‐100 Ca 2+ binding protein, calprotectin, isolated from neutrophil lysates, has been reported to exhibit zinc reversible biostatic activity in vitro . We verified these findings with C. albicans and investigated whether the growth inhibition resulted from zinc deprivation due to chelation by calprotectin. Calprotectin concentrations of 250 μg/ml significantly inhibited the growth of C. albicans . This was reversed by supplementing culture medium with 10 μM ZnSO 4 . Incubation of calprotectin in culture medium for 24 h prior to inoculation significantly reduced the minimum inhibitory concentration. When this latter medium was ultrafiltered to remove the calprotectin and then inoculated with C. albicans , significant growth inhibition was still present: again it was reversed by zinc. These findings implicate zinc chelation as a novel, potentially important host defence function of an abundant neutrophil protein.