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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Azurocidin 1

CAP37, AZU
Azurophil granules, specialized lysosomes of the neutrophil, contain at least 10 proteins implicated in the killing of microorganisms. The protein encoded by this gene is an azurophil granule antibiotic protein, with monocyte chemotactic and antibacterial activity. It is also an important multifunctional inflammatory mediator. This encoded protein is a member of the serine protease gene family but it is not a serine proteinase, because the active site serine and histidine residues are replaced. The genes encoding this protein, neutrophil elastase 2, and proteinase 3 are in a cluster located at chromosome 19pter. All 3 genes are expressed coordinately and their protein products are packaged together into azurophil granules during neutrophil differentiation. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, elastase, Inactive
Papers on CAP37
The antimicrobial protein, CAP37, is upregulated in pyramidal neurons during Alzheimer's disease.
New
Anne Pereira et al., Oklahoma City, United States. In Histochem Cell Biol, Oct 2015
The cationic antimicrobial protein of 37 kDa (CAP37) is an inflammatory mediator constitutively expressed in neutrophils (PMNs).
The lipooligosaccharide-modifying enzyme LptA enhances gonococcal defence against human neutrophils.
New
Criss et al., Charlottesville, United States. In Cell Microbiol, Jun 2015
(ii) lptA mutant Gc is more sensitive to killing by components found in neutrophil granules, including CAP37/azurocidin, human neutrophil peptide 1 and the serine protease cathepsin G. (iii) lptA mutant Gc is more susceptible to killing by antimicrobial components that are exocytosed from neutrophils, including those decorating neutrophil extracellular traps.
A multifunctional peptide based on the neutrophil immune defense molecule, CAP37, has antibacterial and wound-healing properties.
New
Pereira et al., Oklahoma City, United States. In J Leukoc Biol, Feb 2015
CAP37, a protein constitutively expressed in human neutrophils and induced in response to infection in corneal epithelial cells, plays a significant role in host defense against infection.
Azurocidin-induced inhibition of oxygen metabolism in mitochondria is antagonized by heparin.
Ma et al., Shenyang, China. In Exp Ther Med, 2014
Azurocidin (AZU), a protein with strong heparin-binding potential that induces inflammatory responses and apoptosis, has been shown to increase the permeability of endothelial cells and induce the prognosis of sepsis.
Fusion protein bilayer fabrication composed of recombinant azurin/cytochrome P450 by the sortase-mediated ligation method.
Choi et al., Seoul, South Korea. In Colloids Surf B Biointerfaces, 2014
The Azu-P450 (recombinant azurin-cytochrome P450) fusion protein layer was confirmed by AFM (Atomic Force Microscopy) and SERS (Surface-enhanced Raman Spectroscopy), to confirm the fusion protein bilayer orientation.
Corneal wound healing, a newly identified function of CAP37, is mediated by protein kinase C delta (PKCδ).
Pereira et al., Oklahoma City, United States. In Invest Ophthalmol Vis Sci, 2014
PURPOSE: The neutrophil-derived granular protein, CAP37, an innate immune system molecule, has antibiotic and immunomodulatory effects on host cells, including corneal epithelial cells.
[Relationship between dental caries and salivary proteome by electrospray ionization ion-trap tandem mass spectrometry in children aged 6 to 8 years].
Yang et al., In Hua Xi Kou Qiang Yi Xue Za Zhi, 2014
The detected proteins included matrix metalloproteinase-9 (MMP9), mucin-7 (MUC7), lactotransferrin (LTF), carbonic anhydrase 6 (CA6), azurocidin (AZU), and cold agglutinin.
Heparin-binding protein (HBP/CAP37) - a link to endothelin-1 in endotoxemia-induced pulmonary oedema?
Oldner et al., Sweden. In Acta Anaesthesiol Scand, 2014
During sepsis, neutrophils release heparin-binding protein (HBP) known to increase vascular permeability and to be a promising biomarker of human sepsis.
CAP37 activation of PKC promotes human corneal epithelial cell chemotaxis.
Pereira et al., Oklahoma City, United States. In Invest Ophthalmol Vis Sci, 2013
PURPOSE: The objective of this study was to elucidate the signaling pathway through which cationic antimicrobial protein of 37 kDa (CAP37) mediates human corneal epithelial cell (HCEC) chemotaxis.
The proteomic profile of circulating pentraxin 3 (PTX3) complex in sepsis demonstrates the interaction with azurocidin 1 and other components of neutrophil extracellular traps.
GeneRIF
Hamakubo et al., Tokyo, Japan. In Mol Cell Proteomics, 2012
AZU1 exhibited high affinity binding to PTX3 in a calcium ion-dependent manner
Increased plasma levels of heparin-binding protein in patients with shock: a prospective, cohort study.
GeneRIF
Thorlacius et al., Malmö, Sweden. In Inflamm Res, 2012
Heparin-binding protein is elevated in patients with shock from septic and non-septic etiologies.
Identifying the functional part of heparin-binding protein (HBP) as a monocyte stimulator and the novel role of monocytes as HBP producers.
GeneRIF
Flodgaard et al., Copenhagen, Denmark. In Innate Immun, 2011
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.
Neutrophils in biliary atresia. A study on their morphologic distribution and expression of CAP37.
GeneRIF
Ahmed et al., Kansas City, United States. In Pathol Res Pract, 2010
Proliferating bile ductules may play a role in the inflammatory response in biliary atresia through expression of CAP37.
Erysipelas caused by group A streptococcus activates the contact system and induces the release of heparin-binding protein.
GeneRIF
Akesson et al., Lund, Sweden. In J Invest Dermatol, 2010
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
Roles of heparin-binding protein in bacterial infections.
Review
Akesson et al., Lund, Sweden. In J Innate Immun, 2009
Heparin-binding protein (HBP) is also called azurocidin, or cationic antimicrobial protein of 37 kDa (CAP37).
Expression and regulation of antimicrobial peptides in articular joints.
Review
Paulsen et al., Kiel, Germany. In Ann Anat, 2005
In this review, we focus on the most prominent antimicrobial proteins in articular joints, which we have identified as lysozyme, lactoferrin, secretory phospholipase A2, RNase 7, CAP37, the cathelicidin LL37, and especially the human beta-defensin-2 and -3 (HBD-2/-3).
Azurocidin -- inactive serine proteinase homolog acting as a multifunctional inflammatory mediator.
Review
GeneRIF
Watorek, Wrocław, Poland. In Acta Biochim Pol, 2002
Azurocidin 1 (cationic antimicrobial protein 37)is a multifunctional inflammatory mediator causing an increase of vascular permeability [review].
AINT/ERIC/TACC: an expanding family of proteins with C-terminal coiled coil domains.
Review
Maxwell et al., Belfast, United Kingdom. In Leuk Lymphoma, 2002
TACC2, located at 10q26, is similar to anti-zuai-1 (AZU-1), a candidate breast tumour suppressor gene, and ECTACC, an endothelial cell TACC which is upregulated by erythropoietin (Epo).
Heparin-binding protein (HBP/CAP37): a missing link in neutrophil-evoked alteration of vascular permeability.
Impact
Lindbom et al., Stockholm, Sweden. In Nat Med, 2001
We show that upon neutrophil adhesion to the endothelial lining, leukocytic beta2 integrin signaling triggers the release of neutrophil-borne heparin-binding protein (HBP), also known as CAP37/azurocidin, a member of the serprocidin family of neutrophil cationic proteins.
Cationic antimicrobial protein of Mr 37 kDa: a multifunctional inflammatory protein.
Review
Pereira, United States. In Chin Med J (engl), 2001
PURPOSE: To investigate the role of cationic antimicrobial protein of Mr 37 kDa (CAP37) a neutrophil-derived inflammatory mediator on endothelial cell function.
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