Title : Neutrophil gelatinase-associated lipocalin expresses antimicrobial activity by interfering with L-norepinephrine-mediated bacterial iron acquisition.

Pub. Date : 2010 Apr

PMID : 20086155






6 Functional Relationships(s)
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1 Neutrophil gelatinase-associated lipocalin expresses antimicrobial activity by interfering with L-norepinephrine-mediated bacterial iron acquisition. Iron lipocalin 2 Homo sapiens
2 Iron complexes of NE resemble those of bacterial siderophores that are scavenged by human neutrophil gelatinase-associated lipocalin (NGAL) as part of the innate immune defense. Iron lipocalin 2 Homo sapiens
3 Iron complexes of NE resemble those of bacterial siderophores that are scavenged by human neutrophil gelatinase-associated lipocalin (NGAL) as part of the innate immune defense. Iron lipocalin 2 Homo sapiens
4 Here, we show that NGAL binds iron-complexed NE, indicating physiological relevance for both bacterial and human iron metabolism. Iron lipocalin 2 Homo sapiens
5 Here, we show that NGAL binds iron-complexed NE, indicating physiological relevance for both bacterial and human iron metabolism. Iron lipocalin 2 Homo sapiens
6 This study demonstrates for the first time that human NGAL not only neutralizes pathogen-derived virulence factors but also can effectively scavenge an iron-chelate complex abundant in the host. Iron lipocalin 2 Homo sapiens