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Neuronal CAP37 may modulate the neuroinflammatory response in Alzheimer disease.
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Plasma levels of heparin-binding protein were significantly higher in patients with acute respiratory distress syndrome.
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identified a multifunctional bioactive peptide, based on CAP37, that induces cell migration, possesses antibacterial and LPS-binding activity, and is effective at healing infected and noninfected corneal wounds in vivo.
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Azurocidin 1 displays antimicrobial activity against E. coli, S. faecalis, and C. albicans.
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Low levels of azurocidin in maternal serum in the first trimester were associated with subsequent preterm prelabor rupture of membranes.
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AZU1 exhibited high affinity binding to PTX3 in a calcium ion-dependent manner
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Heparin-binding protein is elevated in patients with shock from septic and non-septic etiologies.
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The TAASC motif in a cyclizised 20-44 amino acid peptide is part of the ligand in HBP responsible for activation of the HBP receptor on monocytes. Monocytes release HBP constitutively in small amounts and more so in the presence of lipopolysaccharide.
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Proliferating bile ductules may play a role in the inflammatory response in biliary atresia through expression of CAP37.
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group A streptococci induce contact activation and HBP release during skin infection, which likely contribute to the symptoms seen in erysipelas: fever, pain, erythema, and edema
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Secretion of heparin-binding protein (CAP37) from human neutrophils is determined by its localization in azurophilic granules and secretory vesicles
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CAP37 is localized within the vascular endothelium associated with atherosclerotic plaques. CAP37 is induced in endothelial cells in response to inflammatory mediators
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structural analysis of N-glycans
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A comparison of proforms and mature forms of azurocidin in regulating granulopoiesis
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arginine-rich residues of CAP37 amplify lipopolysaccharide-induced monocyte activation
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CAP37 is a neutrophil-derived inflammatory mediator that augments leukocyte adhesion to endothelial monolayers
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Azurocidin 1 (cationic antimicrobial protein 37)is a multifunctional inflammatory mediator causing an increase of vascular permeability [review].
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Due to its localization to atherosclerotic plaques and its ability to modulate smooth muscle cells, CAP37 may play a role in the progression of this disease.
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Secretion of CAP37, a neutrophil granule protein accumulating on the endothelial cell surface and promoting arrest of monocytes, could contribute to the recruitment of monocytes at inflammatory loci.
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HBP appears to be one of the primary effector molecules of antibody-mediated nonhemolytic transfusion reactions including transfusion acute lung injury
