Metabolism and Innate Immunity: FOXO Regulation of Antimicrobial Peptides inDrosophila

2013 ◽  
pp. 103-111 ◽  
Author(s):  
Gerrit Loch ◽  
Eva Jentgens ◽  
Margret Bülow ◽  
Ingo Zinke ◽  
Tetsushi Mori ◽  
...  
Keyword(s):  
Innate Immunity ◽  
Antimicrobial Peptides

IV. Paneth cell antimicrobial peptides and the biology of the mucosal barrier

1999 ◽  
Vol 277 (2) ◽  
pp. G257-G261 ◽  
Author(s):  
Andre J. Ouellette
Keyword(s):  
Innate Immunity ◽  
Epithelial Cells ◽  
Antimicrobial Peptides ◽  
Paneth Cell ◽  
Chloride Ion ◽  
Paneth Cells ◽  
In Vitro Assays ◽  
Mucosal Barrier ◽  
Intermediate Cells

The hypothesis that epithelial cells release preformed antibiotic peptides as components of mucosal innate immunity has gained experimental support in recent years. In the mammalian small intestine, Paneth cells secrete granules that are rich in α-defensins and additional antimicrobial peptides into the lumen of the crypt. The α-defensins are homologues of peptides that function as mediators of nonoxidative microbial cell killing in phagocytic leukocytes, and they are potent microbicidal agents in in vitro assays. Because certain mouse α-defensins stimulate cultured epithelial cells to secrete chloride ion, those peptides appear to be capable of interacting directly with the apical membranes of neighboring cells and perhaps influencing crypt physiology. In instances of crypt disruption or induced Paneth cell deficiency, crypt intermediate cells appear to compensate by accumulating and secreting Paneth cell antimicrobial peptides. Challenges for the future will be to understand the mechanisms of this epithelial plasticity and to show that Paneth cells contribute directly to innate immunity in the crypt microenvironment.

Penaeidins, antimicrobial peptides of shrimp: a comparison with other effectors of innate immunity

Aquaculture ◽  
2000 ◽  
Vol 191 (1-3) ◽  
pp. 71-88 ◽  
Author(s):  
Evelyne Bachère ◽  
Delphine Destoumieux ◽  
Philippe Bulet
Keyword(s):  
Innate Immunity ◽  
Antimicrobial Peptides

Function of Antimicrobial Peptides in Lung Innate Immunity

2015 ◽  
pp. 33-52 ◽  
Author(s):  
Frederik Seiler ◽  
Robert Bals ◽  
Christoph Beisswenger
Keyword(s):  
Innate Immunity ◽  
Antimicrobial Peptides ◽  
Lung Innate Immunity

scholarly journals Actinobacillus actinomycetemcomitans Outer Membrane Protein 100 Triggers Innate Immunity and Production of β-Defensin and the 18-Kilodalton Cationic Antimicrobial Protein through the Fibronectin-Integrin Pathway in Human Gingival Epithelial Cells

2006 ◽  
Vol 74 (9) ◽  
pp. 5211-5220 ◽  
Author(s):  
Kazuhisa Ouhara ◽  
Hitoshi Komatsuzawa ◽  
Hideki Shiba ◽  
Yushi Uchida ◽  
Toshihisa Kawai ◽  
...  
Keyword(s):  
Innate Immunity ◽  
Membrane Protein ◽  
Antimicrobial Peptides ◽  
Inflammatory Cytokines ◽  
Outer Membrane Protein ◽  
Actinobacillus Actinomycetemcomitans ◽  
Antimicrobial Protein ◽  
Gingival Epithelial Cells ◽  
Tnf Α ◽  
Human Gingival Epithelial Cells

ABSTRACT Antimicrobial peptides, human β-defensin (hBD), and the 18-kDa cationic antimicrobial protein (CAP18) are components of innate immunity. These peptides have antimicrobial activity against bacteria, fungi, and viruses. Actinobacillus actinomycetemcomitans is a gram-negative facultative anaerobe implicated in the initiation of periodontitis. The innate immunity peptides have antibacterial activity against A. actinomycetemcomitans. We investigated the molecular mechanism of human gingival epithelial cells (HGEC) responding to exposure to A. actinomycetemcomitans. HGEC constitutively express hBD1 and inducibly express hBD2, hBD3, and CAP18 on exposure to A. actinomycetemcomitans. The level of expression varies among clinical isolates. In the signaling pathway for hBD2 induction by the bacterial contact, we demonstrate that the mitogen-activated protein (MAP) kinase and not the NF-κB transcription factor pathway is used. We found the outer membrane protein 100 (Omp100; identified by molecular mass) is the component inducing the hBD2 response. Omp100 binds to fibronectin, an extracellular matrix inducing hBD2 via the MAP kinase pathway. Anti-integrin α5β1, antifibronectin, genistein, and PP2 suppress the Omp100-induced expression of hBD2, suggesting that Src kinase is involved through integrin α5β1. The inflammatory cytokines, tumor necrosis factor α (TNF-α), interleukin-1β (IL-1β), IL-6 and IL-8, produced by HGEC on contact with A. actinomycetemcomitans also stimulate expression of hBD2. Further, neutralizing antibody against TNF-α or IL-8 partially inhibits the induction of hBD2 on bacterial contact. Therefore, we found that the induction of the antimicrobial peptides is mediated by a direct response principally through an Omp100-fibronectin interaction, and using secondary stimulation by inflammatory cytokines induced by the bacterial exposure.

Antimicrobial peptides: a key component of honey bee innate immunity

2015 ◽  
Vol 54 (2) ◽  
pp. 123-136 ◽  
Author(s):  
Jiří Danihlík ◽  
Kate Aronstein ◽  
Marek Petřivalský
Keyword(s):  
Innate Immunity ◽  
Antimicrobial Peptides ◽  
Honey Bee

The role of salivary histatin and the human cathelicidin LL-37 in wound healing and innate immunity

2010 ◽  
Vol 391 (5) ◽  
pp. 541-548 ◽  
Author(s):  
Menno J. Oudhoff ◽  
Marjolein E. Blaauboer ◽  
Kamran Nazmi ◽  
Nina Scheres ◽  
Jan G.M. Bolscher ◽  
...  
Keyword(s):  
Wound Healing ◽  
Innate Immunity ◽  
Antimicrobial Peptides ◽  
Wound Repair ◽  
Neutrophil Migration ◽  
Fibroblast Migration ◽  
Initial Stage ◽  
Epithelial Cell Migration ◽  
Oral Wound Healing ◽  
Multicellular Organisms

Abstract Antimicrobial peptides are multifunctional in innate immunity and wound repair of multicellular organisms. We were the first to discover that histatins, a family of salivary antimicrobial peptides, enhance epithelial cell migration, suggesting a role in oral wound healing. It is unknown whether histatins display innate-immunity activities, similar to other antimicrobial peptides such as LL-37. Therefore, we compared the effect of Histatin-2 and LL-37 on several activities within the context of wound healing and innate immunity. We found that Histatin-2 enhances fibroblast migration, but only weakly induces proliferation. LL-37 enhances both fibroblast migration and proliferation, but only at a narrow concentration optimum (approximately 1 μm). At higher concentrations LL-37 causes cell death, whereas Histatin-2 is not cytotoxic. Both peptides do not alter fibroblast-to-myofibroblast differentiation. Histatin-2 does not alter interleukin-8 (IL-8) expression and lipopolysaccharide (LPS)-elevated cytokine and chemokine expression. In contrast, LL-37 induces IL-8 expression, but dampens the LPS-induced immune response. Neither Histatin-2 nor LL-37 affects human-neutrophil migration. Histatins are, unlike other antimicrobial peptides, not cytotoxic or proinflammatory. It seems that they are important for the initial stage of wound healing in which fast wound coverage is important for healing without infection, inflammation, or fibrosis development. Interestingly, these characteristics are more typical for the mouth than for skin.

scholarly journals Antimicrobial Peptides Initiate IL-1β Posttranslational Processing: A Novel Role Beyond Innate Immunity

2002 ◽  
Vol 168 (6) ◽  
pp. 3024-3032 ◽  
Author(s):  
David G. Perregaux ◽  
Kanan Bhavsar ◽  
Len Contillo ◽  
Jishu Shi ◽  
Christopher A. Gabel
Keyword(s):  
Innate Immunity ◽  
Antimicrobial Peptides ◽  
Posttranslational Processing

The antimicrobial peptides derived from chromogranin/secretogranin family, new actors of innate immunity

2010 ◽  
Vol 165 (1) ◽  
pp. 102-110 ◽  
Author(s):  
Peiman Shooshtarizadeh ◽  
Dan Zhang ◽  
Jean-François Chich ◽  
Claire Gasnier ◽  
Francis Schneider ◽  
...  
Keyword(s):  
Innate Immunity ◽  
Antimicrobial Peptides
Sign in / Sign up

Export Citation Format

Share Document