In vitro tumor cell cytolysis mediated by peptide defensins of human and rabbit granulocytes

Lichtenstein, A; Ganz, T; Selsted, ME; Lehrer, RI

doi:10.1182/blood.v68.6.1407.bloodjournal6861407

Cited by 73 publications

(87 citation statements)

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“…When released into the extracellular environment, these peptides can exert other activities that increase host defense but may also be potentially harmful. Soon after their initial characterization as human neutrophil antimicrobials [30], the cytotoxic and chemotactic activities of neutrophil defensins were discovered [31,32]. Subsequently, various other activities were discovered, which indicate a broad role for neutrophil defensins in innate and adaptive immunity and in wound repair (reviewed in refs.…”

Section: Antimicrobial Peptides Of the Neutrophil: Neutrophil Defensimentioning

confidence: 99%

Interactions between neutrophil-derived antimicrobial peptides and airway epithelial cells

Wetering

Tjabringa

Hiemstra

2004

Journal of Leukocyte Biology

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Most antimicrobial peptides have been discovered based on activity-guided purification procedures, which used assays to determine their antimicrobial activity. Nevertheless, recent studies have shown that antimicrobial peptides also exert a range of other functions. Based on these observations, antimicrobial peptides are now not only implicated in host defense against infection but also in other immune reactions, inflammation, and wound-repair processes. The activities of neutrophil defensins and the cathelicidin hCAP-18/LL-37, antimicrobial peptides that are abundantly expressed in the human neutrophil, are the subject of an increasing number of studies. Exposure to neutrophil defensins and hCAP-18/LL-37 results in increases in mediator expression and release, chemotaxis, and proliferation of inflammatory and epithelial cells and fibroblasts, and the mechanisms underlying these effects have been partly elucidated. This review is focused on the effects of neutrophil defensins and hCAP-18/LL-37 on airway epithelial cells.

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Section: Antimicrobial Peptides Of the Neutrophil: Neutrophil Defensimentioning

confidence: 99%

Interactions between neutrophil-derived antimicrobial peptides and airway epithelial cells

Wetering

Tjabringa

Hiemstra

2004

Journal of Leukocyte Biology

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“…In vitro, defensins have been shown to be toxic to bacteria (Greenwald & Ganz, 1987;Lehrer et al, 1989), fungi (Lehrer et al, 1985b), and enveloped viruses (Daher et al, 1986). Defensins also display cytotoxicity toward several normal and neoplastic cell lines (Lichtenstein et al, 1986). Studies with planar lipid bilayers (Kagan et al, 1990) indicate that the defensins' primary mode of action is by direct association with the lipid components in membranes.…”

Section: ~~ ~ ~~~~mentioning

confidence: 99%

“…Native defensins were isolated from rabbit (Selsted et al, 1984;Lichtenstein et al, 1986) and human neutrophils (Ganz et al, 1985), as described, and quantitated by amino acid analysis. Linearized defensins were produced by reduction with dithiothreitol and S-carboxamidomethylation with iodoacetamide as described previously and were purified by reverse-phase HPLC.…”

Section: Peptidesmentioning

confidence: 99%

Defensins promote fusion and lysis of negatively charged membranes

Fujii

Selsted

Eisenberg³

1993

Protein Science

156

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Defensins, a family of cationic peptides isolated from mammalian granulocytes and believed to permeabilize membranes, were tested for their ability to cause fusion and lysis of liposomes. Unlike a-helical peptides whose lytic effects have been extensively studied, the defensins consist primarily of 0-sheet. Defensins fuse and lyse negatively charged liposomes but display reduced activity with neutral liposomes. These and other experiments suggest that fusion and lysis is mediated primarily by electrostatic forces and to a lesser extent, by hydrophobic interactions.Circular dichroism and fluorescence spectroscopy of native defensins indicate that the amphiphilic 0-sheet structure is maintained throughout the fusion process. Taken together, these results support the idea that proteinmediated membrane fusion depends not only on hydrophobic and electrostatic forces but also on the spatial arrangement of the amino acid residues to form a three-dimensional amphiphilic structure, which promotes the efficient mixing of the lipids between membranes. A molecular model for membrane fusion by defensins is presented, which takes into account the contributions of electrostatic forces, hydrophobic interactions, and structural amphiphilicity.

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“…aureus and E. coli , fungi , and viruses (Daher et al, 1986). Defensins are also cytotoxic to tumor cell lines such as human lung-derived cell lines and human umbilical vein endothelial cells (Lichtenstein et al, 1986;Okrent et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

Defensin‐1, an antimicrobial peptide present in the saliva of patients with oral diseases

et al. 1999

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OBJECTIVES AND DESIGN: A preceding paper has noted a detection of defensin‐1 (HNP‐1), a peptide with antimicrobial and cytotoxic properties, in the saliva of patients with oral squamous cell carcinoma. The present study deals with the presence of HNP‐1 in the saliva of patients with various oral diseases. METHODS: Whole saliva samples were obtained from the patientS. HNP‐1 in the saliva was isolated and purified by HPLC and the amino acid sequence of the peptide was determined. The molecular weight of HNP‐1 was measured by mass spectrometry. The concentration of HNP‐1 in saliva was determined by comparing the height of eluted HNP‐1 with that of a synthetic HNP‐1 standard. RESULTS: The concentrations of HNP‐1 in the saliva of patients with oral lichen planus (n= 5), leukoplakia (n= 4), and glossitis associated with iron deficiency (n= 4) were 8.3± 4.3μg ml‐1, 13.2± 7.9/w.g ml ‐1, and 11.4± 4.9 μg ml‐1, (mean± S. d.), respectively. These concentrations were significantly higher than those in healthy subjects (0.8 μg ml‐1) (P < 0.01). In contrast, salivary HNP‐1 concentrations in patients with glossodynia (n= 4) and oral discomfort (n= 4) were similar to those in healthy subjects. CONCLUSIONS: Since HNP‐1 is a non‐specific defensive peptide present in neutrophils, it may play an important role in the protection against diseases such as oral lichen planus, leukoplakia, and glossitis associated with iron deficiency.

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In vitro tumor cell cytolysis mediated by peptide defensins of human and rabbit granulocytes

Cited by 73 publications

References 0 publications

Interactions between neutrophil-derived antimicrobial peptides and airway epithelial cells

Interactions between neutrophil-derived antimicrobial peptides and airway epithelial cells

Defensins promote fusion and lysis of negatively charged membranes

Defensin‐1, an antimicrobial peptide present in the saliva of patients with oral diseases

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