We are analyzing https://link.springer.com/article/10.1007/s00005-009-0057-2.

Title:
Cathelicidin LL-37: A Multitask Antimicrobial Peptide | Archivum Immunologiae et Therapiae Experimentalis
Description:
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 D3. 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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Keywords {🔍}

google, scholar, article, pubmed, cas, human, antimicrobial, peptide, cathelicidin, peptides, expression, cells, immunol, cell, bucki, host, defense, bacterial, invest, activity, dermatol, infection, biol, immune, antibacterial, epithelial, cancer, med, vitamin, neutrophils, response, cationic, innate, antimicrob, agents, chemother, chem, skin, privacy, cookies, function, content, namiot, expressed, neutrophil, release, dna, factin, factor, protein,

Topics {✒️}

month download article/chapter peptide antibiotic ll-37/hcap-18 cathelicidin-related antimicrobial peptide granulocyte colony-stimulating factor cathelicidin-derived ll-37 peptide epithelial cell-derived cathelicidin multidrug-resistant acinetobacter baumannii inflammatory mediator il-1beta mammalian cathelicidin-derived peptides leukotriene b4-mediated release antimicrobial protein hcap18/ll-37 tlr-mediated inflammatory response human cathelicidin cap18/ll-37 article archivum immunologiae minimal membrane-targeting antimicrobial conformation-dependent antibacterial activity antimicrobial host defense human beta-defensin 1 host defence peptides ll-37 peptide enhances host defense cells antibacterial peptide ll-37 multitask antimicrobial peptide full article pdf bactericidal cationic peptides cathelicidin ll-37 induces antimicrobial peptide ll-37 actin bundle formation antimicrobial cathelicidin peptide cationic steroid csa-13 antimicrobial protein hcap-18 including bacterial products dna/f-actin bundles human cathelicidin ll-37 modulates cellular response anti-fungal activity antibacterial peptides cap18 human cap18/ll-37 innate defense system cathelicidin antimicrobial peptides suppresses neutrophil apoptosis privacy choices/manage cookies human alpha-defensins human ll-37 fragments formyl-peptide receptors human epithelial cells human immune response human plasma gelsolin formyl-peptide receptor article bucki

Questions {❓}

Brogden KA (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Ginsburg I (2004) Bactericidal cationic peptides can also function as bacteriolysis-inducing agents mimicking beta-lactam antibiotics?

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         description: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 D3. 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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