Expression and Secretion of Cathelicidin LL-37 in Human Epithelial Cells after Infection by<i>Mycobacterium bovis</i>Bacillus Calmette-Guérin

Méndez-Samperio, Patricia; Miranda, Elena; Trejo, Artemisa

doi:10.1128/cvi.00178-08

Cited by 46 publications

(33 citation statements)

References 35 publications

(29 reference statements)

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“…Cell type-specific differences in the pathways leading to cathelicidin gene induction have also been suggested by experiments showing that the MEK-ERK inhibitor U0126 blocked the butyrate-induced expression of LL-37 in gastric and colon carcinoma cell lines, but not in hepatocellular carcinoma cells [46]. Other studies indicate that the induction of LL-37 expression in epidermal keratinocytes by enforced expression of ASK1, a regulator of keratinocyte differentiation, is dependent on p38 activity [47] and that the induction of LL-37 expression in an epithelial cell line by exposure to Mycobacterium bovis BCG requires MEK1/2 and p38 activation [48]. …”

Section: Discussionmentioning

confidence: 99%

NF-κB-Dependent Induction of Cathelicidin-Related Antimicrobial Peptide in Murine Mast Cells by Lipopolysaccharide

Domenico

Jia

et al. 2009

Int Arch Allergy Immunol

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Background: An important aspect of the innate immune response to pathogens is the production of anti-microbial peptides such as cathelicidin-related antimicrobial peptide (CRAMP), the murine homologue of human cathelicidin LL-37. In this study, mechanisms regulating LPS-induction of CRAMP gene expression in mast cells were investigated. NF-κB and MAPK pathways were the focus of investigation. Methods: Mouse bone marrow-derived mast cells were grown in culture and stimulated with LPS. MAPKs and NF-κB were monitored by immunoblot analysis. ERK, JNK and p38 MAPK were inhibited using siRNAs or a pharmacological inhibitor. Accumulation of the p65 component of NF-κB was inhibited by siRNA and NF-κB activation was inhibited by overexpression of IκBα. MEKK2 or MEKK3 were overexpressed by transfection. The effects of all of these treatments on CRAMP gene expression were monitored by RT-PCR. Results: Inhibition of ERK, JNK or p38 MAPK had little discernible effect on LPS-inducible CRAMP gene expression. Overexpression of MEKK2 or MEKK3 likewise had little impact. However, inhibition of the accumulation of p65 NF-κB prevented LPS-induced CRAMP mRNA. An important role for NF-κB in CRAMP gene expression was confirmed by overexpression of IκBα, which reduced both basal and induced levels of CRAMP mRNA. Conclusions: NF-κB, but not MAPKs, plays an important role in LPS-mediated induction of CRAMP gene in mast cells. Defects which inhibit NF-κB activity may increase susceptibility to bacterial and viral pathogens which are sensitive to cathelicidins.

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Section: Discussionmentioning

confidence: 99%

NF-κB-Dependent Induction of Cathelicidin-Related Antimicrobial Peptide in Murine Mast Cells by Lipopolysaccharide

Domenico

Jia

et al. 2009

Int Arch Allergy Immunol

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“…This inflammatory correlate may be related to cell death because apoptosis of respiratory epithelial cells has been observed with physiologically relevant levels of LL-37 (244). LL-37 is induced by bacterial and mycobacterial infections, and this is dependent on MAPK (245)(246)(247). LL-37 is also capable of activating MAPK to induce CXCL8 secretion via activation of EGFR and IL-6 via NF-kB (248,249).…”

Section: Ll37mentioning

confidence: 99%

Innate Immunity in the Respiratory Epithelium

Parker

Prince

2011

Am J Respir Cell Mol Biol

386

404

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The airway epithelium represents the first point of contact for inhaled foreign organisms. The protective arsenal of the airway epithelium is provided in the form of physical barriers and a vast array of receptors and antimicrobial compounds that constitute the innate immune system. Many of the known innate immune receptors, including the Toll-like receptors and nucleotide oligomerization domain-like receptors, are expressed by the airway epithelium, which leads to the production of proinflammatory cytokines and chemokines that affect microorganisms directly and recruit immune cells, such as neutrophils and T cells, to the site of infection. The airway epithelium also produces a number of resident antimicrobial proteins, such as lysozyme, lactoferrin, and mucins, as well as a swathe of cationic proteins. Dysregulation of the airway epithelial innate immune system is associated with a number of medical conditions that can result in compromised immunity and chronic inflammation of the lung. This review focuses on the innate immune capabilities of the airway epithelium and its role in protecting the lung from infection as well as the outcomes when its function is compromised.

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“…This last TLR was strongly activated by M. tuberculosis DNA (Liu et al 2006;RivasSantiago et al 2008). Additionally, it was found that the MEK1/2 and p38 MAPK signaling pathways play a critical role in the regulation of inducible LL-37 gene expression in A549 cells infected with Mycobacterium bovis bacillus Calmette-Guerin, the world's most widely used tuberculosis vaccine (Mendez-Samperio et al 2008).…”

mentioning

confidence: 99%

Cathelicidin LL-37: A Multitask Antimicrobial Peptide

Bucki

Leszczyńska

Namiot

et al. 2010

Arch. Immunol. Ther. Exp.

180

174

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The antimicrobial peptide LL-37 is the only known member of the cathelicidin family of peptides expressed in humans. LL-37 is a multifunctional host defense molecule essential for normal immune responses to infection and tissue injury. LL-37 peptide is a potent killer of different microorganisms with the ability to prevent immunostimulatory effects of bacterial wall molecules such as lipopolysaccharide and can therefore protect against lethal endotoxemia. Additional reported activities of LL-37 include chemoattractant function, inhibition of neutrophil apoptosis, and stimulation of angiogenesis, tissue regeneration, and cytokine release (e.g. IL-8). Cellular production of LL-37 is affected by multiple factors, including bacterial products, host cytokines, availability of oxygen, and sun exposure through the activation of CAP-18 gene expression by vitamin D(3). At infection sites, the function of LL-37 can be inhibited by charge-driven interactions with DNA and F-actin released from dead neutrophils and other cells lysed as the result of inflammation. A better understanding of LL-37's biological properties is necessary for its possible therapeutic application for immunomodulatory purposes as well as in treating bacterial infection.

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Expression and Secretion of Cathelicidin LL-37 in Human Epithelial Cells after Infection byMycobacterium bovisBacillus Calmette-Guérin

Cited by 46 publications

References 35 publications

NF-κB-Dependent Induction of Cathelicidin-Related Antimicrobial Peptide in Murine Mast Cells by Lipopolysaccharide

NF-κB-Dependent Induction of Cathelicidin-Related Antimicrobial Peptide in Murine Mast Cells by Lipopolysaccharide

Innate Immunity in the Respiratory Epithelium

Cathelicidin LL-37: A Multitask Antimicrobial Peptide

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