CAP37, a human neutrophil-derived chemotactic factor with monocyte specific activity.

Pereira, H. Anne; Shafer, W M; Pohl, Jan; Martin, Larry E.; Spitznagel, John K.

doi:10.1172/jci114593

Cited by 142 publications

(136 citation statements)

References 32 publications

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“…Experiments with the aim of characterising the haptotaxis and the receptor on the cells are in progress. Recently (Pereira et al, 1990) reported an N-terminal sequence identical to our hHBP and also described the His Ser mutation. They purified the protein, which they have named CAP37 and shown to be antimicrobial, from azurophile granules and showed that the protein was chemotactic for monocytes over the range 1.3 -10 nM.…”

Section: --S G V P P E V F T R V S S F L P W I R T T M R S F K L L Hnsupporting

confidence: 58%

Covalent structure of two novel neutrophile leucocyte‐derived proteins of porcine and human origin

Flodgaard¹,

Østergaard²,

Bayne³

et al. 1991

European Journal of Biochemistry

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The covalent structures of two, novel, neutrophile, leucocyte-derived, strongly basic proteins of porcine and human origin have been determined by microsequencing in combination with time-of-flight plasma desorption mass spectrometry. The porcine protein primary structure of 219 amino acid residues was shown to contain 6 cysteine residues, 2 putative carbohydrate sites and 14% basic residues. The human protein contained 221 amino acid residues of which 8 were cysteine, 4 putative carbohydrate sites and 12% basic. A 47% direct sequence similarity to human neutrophile elastase was found, but due to mutations of two of the three amino acids in the catalytic triad, proteolytic activity is absent. Modelling and alignment studies unveil a close relationship of both proteins to the serine protease family, the greatest similarity being to those serine proteases present in granules from peripheral blood cells. Both proteins have been shown to be chemotactically active for monocytes and fibroblasts in vitro.

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Section: --S G V P P E V F T R V S S F L P W I R T T M R S F K L L Hnsupporting

confidence: 58%

Covalent structure of two novel neutrophile leucocyte‐derived proteins of porcine and human origin

Flodgaard¹,

Østergaard²,

Bayne³

et al. 1991

European Journal of Biochemistry

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“…Azurocidin is released almost completely after granule mobilization. In contrast to, e.g., HNPs, which are released mainly into the phagolysosome [21], 90% of the azurocidin are released upon degranulation [17,19]. These three distinct properties of azurocidin favor the promiscuous mode of action that this protein displays.…”

Section: Azurocidin Is Unique Among the Pmn Granule Proteinsmentioning

confidence: 99%

Neutrophil-derived azurocidin alarms the immune system

Soehnlein

Lindbom

2008

Journal of Leukocyte Biology

102

100

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Azurocidin (heparin-binding protein/ cationic antimicrobial protein of 37 kD) is a protein that is mobilized rapidly from emigrating polymorphonuclear leukocytes (PMN). Initially, this inactive serine protease was recognized for its antimicrobial effects. However, it soon became apparent that azurocidin may act to alarm the immune system in different ways and thus serve as an important mediator during the initiation of the immune response. Azurocidin, released from PMN secretory vesicles or primary granules, acts as a chemoattractant and activator of monocyte and macrophages. The functional consequence is enhancement of cytokine release and bacterial phagocytosis, allowing for a more efficient bacterial clearance. Leukocyte activation by azurocidin is mediated via ␤ 2 -integrins, and azurocidin-induced chemotaxis is dependent on formyl-peptide receptors. In addition, azurocidin activates endothelial cells leading to vascular leakage and edema formation. For these reasons, targeting azurocidin release and its actions may have therapeutic potential in inflammatory disease conditions. J. Leukoc. Biol. 85: 344 -351; 2009.

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“…26 Briefly, paraffin sections were deparaffinized in xylene, and rehydrated, and quenched for endogenous peroxidase. Cryostat sections were placed on gelatinized slides, and fixed in cold acetone.…”

Section: Immunohistochemical Studymentioning

confidence: 99%

Endothelial progenitor cells in pterygium pathogenesis

Lee

Song

et al. 2006

Eye

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Purpose The pathogenesis of pterygium is not well known, and controversy exists about the cell origins and the nature of initial trigger required for its development. We investigated whether endothelial progenitor cells (EPCs) are involved in pathogenesis of pterygium and the mechanism underlying the selective recruitment of EPCs during this process. Methods We studied 13 normal controls and 28 pterygium patients (primary (n ¼ 15), recurrent (n ¼ 13)). Substance-P, vascular endothelial growth factor (VEGF), and stem cell factor (SCF) were measured in plasma and tears using ELISA, and circulating CD34 þ and c-kit þ mononuclear cells (MNCs) by flow cytometry. Anterior segment fluorescein angiography (FAG) was performed to evaluate hypoxic conditions in the early stage of pterygium. Surgically removed pterygial tissues were analyzed immunohistochemically using the progenitor cell markers, CD34, c-kit, VEGFR-1, and VEGFR-2. Results Anterior segment FAG findings showed an increase in non-perfusion areas and attenuated vessels in the nasal limbus during early-stage pterygium. Circulating CD34 þ MNCs and c-kit þ MNCs were increased in pterygium groups compared with normal controls. Systemic and local cytokines including SP, VEGF, and SCF in pterygium groups were also elevated and showed positive correlations with CD34 þ and c-kit þ MNC numbers. Immunohistochemical analysis of pterygium showed strong progenitor cell marker immunoreactivities. Conclusions EPCs might be involved in pterygium development, and ocular hypoxia triggers this neovascularization by recruiting EPCs derived from the bone marrow via the production of systemic and local cytokines.

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CAP37, a human neutrophil-derived chemotactic factor with monocyte specific activity.

Cited by 142 publications

References 32 publications

Covalent structure of two novel neutrophile leucocyte‐derived proteins of porcine and human origin

Covalent structure of two novel neutrophile leucocyte‐derived proteins of porcine and human origin

Neutrophil-derived azurocidin alarms the immune system

Endothelial progenitor cells in pterygium pathogenesis

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