Relevant bibliographies by topics / LL-37

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Academic literature on the topic 'LL-37'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 March 2023

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Journal articles on the topic "LL-37"

1

Schauber, J., T. Ruzicka, and R. A. Rupec. "Cathelicidin LL-37." Der Hautarzt 59, no. 1 (December 23, 2007): 72–74. http://dx.doi.org/10.1007/s00105-007-1457-z.

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Tripathi, Shweta, Tesfaldet Tecle, Anamika Verma, Erika Crouch, Mitchell White, and Kevan L. Hartshorn. "The human cathelicidin LL-37 inhibits influenza A viruses through a mechanism distinct from that of surfactant protein D or defensins." Journal of General Virology 94, no. 1 (January 1, 2013): 40–49. http://dx.doi.org/10.1099/vir.0.045013-0.

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LL-37, the only human cathelicidin, is a cationic antimicrobial peptide with antibacterial and antifungal activity. LL-37 is released from neutrophil granules and produced by epithelial cells. It has been implicated in host defence against influenza A virus (IAV) in recent studies. We now demonstrate dose-related neutralizing activity of LL-37 against several seasonal and mouse-adapted IAV strains. The ability of LL-37 to inhibit these IAV strains resulted mainly from direct effects on the virus, since pre-incubation of virus with LL-37 was needed for optimal inhibition. LL-37 bound high-density lipoprotein (HDL), and pre-incubation of LL-37 with human serum or HDL reduced its antiviral activity. LL-37 did not inhibit viral association with epithelial cells as assessed by quantitative RT-PCR or confocal microscopy. This finding contrasted with results obtained with surfactant protein D (SP-D). Unlike collectins or human neutrophil defensins (HNPs), LL-37 did not induce viral aggregation under electron microscopy. In the electron microscopy studies, LL-37 appeared to cause disruption of viral membranes. LL-37 had additive antiviral activity when combined with other innate inhibitors like SP-D, surfactant protein A and HNPs. Unlike HNPs, LL-37 did not bind SP-D significantly. These findings indicate that LL-37 contributes to host defence against IAV through a mechanism distinct from that of SP-D and HNPs.
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Rosen, Graciela, Michael N. Sela, and Gilad Bachrach. "The Antibacterial Activity of LL-37 against Treponema denticola Is Dentilisin Protease Independent and Facilitated by the Major Outer Sheath Protein Virulence Factor." Infection and Immunity 80, no. 3 (December 19, 2011): 1107–14. http://dx.doi.org/10.1128/iai.05903-11.

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Host defense peptides are innate immune effectors that possess both bactericidal activities and immunomodulatory functions. Deficiency in the human host defense peptide LL-37 has previously been correlated with severe periodontal disease.Treponema denticolais an oral anaerobic spirochete closely associated with the pathogenesis of periodontal disease. TheT. denticolamajor surface protein (MSP), involved in adhesion and cytotoxicity, and the dentilisin serine protease are key virulence factors of this organism. In this study, we examined the interactions between LL-37 andT. denticola. The threeT. denticolastrains tested were susceptible to LL-37. Dentilisin was found to inactivate LL-37 by cleaving it at the Lys, Phe, Gln, and Val residues. However, dentilisin deletion did not increase the susceptibility ofT. denticolato LL-37. Furthermore, dentilisin activity was found to be inhibited by human saliva. In contrast, a deficiency of theT. denticolaMSP increased resistance to LL-37. The MSP-deficient mutant bound less fluorescently labeled LL-37 than the wild-type strain. MSP demonstrated specific, dose-dependent LL-37 binding. In conclusion, though capable of LL-37 inactivation, dentilisin does not protectT. denticolafrom LL-37. Rather, the rapid, MSP-mediated binding of LL-37 to the treponemal outer sheath precedes cleavage by dentilisin. Moreover,in vivo, saliva inhibits dentilisin, thus preventing LL-37 restriction and ensuring its bactericidal and immunoregulatory activities.
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Bryzek, Danuta, Anna Golda, Joanna Budziaszek, Dominik Kowalczyk, Alicia Wong, Ewa Bielecka, Priyanka Shakamuri, et al. "Citrullination-Resistant LL-37 Is a Potent Antimicrobial Agent in the Inflammatory Environment High in Arginine Deiminase Activity." International Journal of Molecular Sciences 21, no. 23 (November 30, 2020): 9126. http://dx.doi.org/10.3390/ijms21239126.

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LL-37, the only member of the mammalian cathelicidin in humans, plays an essential role in innate immunity by killing pathogens and regulating the inflammatory response. However, at an inflammatory focus, arginine residues in LL-37 can be converted to citrulline via a reaction catalyzed by peptidyl-arginine deiminases (PAD2 and PAD4), which are expressed in neutrophils and are highly active during the formation of neutrophil extracellular traps (NETs). Citrullination impairs the bactericidal activity of LL-37 and abrogates its immunomodulatory functions. Therefore, we hypothesized that citrullination-resistant LL-37 variants would retain the functionality of the native peptide in the presence of PADs. To test this hypothesis, we synthetized LL-37 in which arginine residues were substituted by homoarginine (hArg-LL-37). Bactericidal activity of hArg-LL-37 was comparable with that of native LL-37, but neither treatment with PAD4 nor exposure to NETs affected the antibacterial and immunomodulatory activities of hArg-LL-37. Importantly, the susceptibilities of LL-37 and hArg-LL-37 to degradation by proteases did not significantly differ. Collectively, we demonstrated that citrullination-resistant hArg-LL-37 is an attractive lead compound for the generation of new agents to treat bacterial infections and other inflammatory diseases associated with enhanced PAD activity. Moreover, our results provide a proof-of-concept for synthesis of therapeutic peptides using homoarginine.
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Zhao, Chengquan, Tung Nguyen, Lee Ming Boo, Teresa Hong, Cesar Espiritu, Dmitri Orlov, Wei Wang, Alan Waring, and Robert I. Lehrer. "RL-37, an Alpha-Helical Antimicrobial Peptide of the Rhesus Monkey." Antimicrobial Agents and Chemotherapy 45, no. 10 (October 1, 2001): 2695–702. http://dx.doi.org/10.1128/aac.45.10.2695-2702.2001.

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ABSTRACT Rhesus monkey bone marrow expresses a cathelicidin whose C-terminal domain comprises a 37-residue alpha-helical peptide (RL-37) that resembles human LL-37. Like its human counterpart, RL-37 rapidly permeabilized the membranes of Escherichia coli ML-35p and lysed liposomes that simulated bacterial membranes. When tested in media whose NaCl concentrations approximated those of extracellular fluids, RL-37 was considerably more active than LL-37 against staphylococci. Whereas human LL-37 contains five acidic residues and has a net charge of +6, rhesus RL-37 has only two acidic residues and a net charge of +8. Speculating that the multiple acidic residues of human LL-37 reduced its efficacy against staphylococci, we made a peptide (LL-37 pentamide) in which each aspartic acid of LL-37 was replaced by an asparagine and each glutamic acid was replaced by a glutamine. LL-37 pentamide's antistaphylococcal activity was substantially greater than that of LL-37. Thus, although the precursor of LL-37 is induced in human skin keratinocytes by injury or inflammation, its insufficiently cationic antimicrobial domain may contribute to the success of staphylococci in colonizing and infecting human skin.
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Rapala-Kozik, Maria, Oliwia Bochenska, Marcin Zawrotniak, Natalia Wolak, Grzegorz Trebacz, Mariusz Gogol, Dominika Ostrowska, Wataru Aoki, Mitsuyoshi Ueda, and Andrzej Kozik. "Inactivation of the Antifungal and Immunomodulatory Properties of Human Cathelicidin LL-37 by Aspartic Proteases Produced by the Pathogenic Yeast Candida albicans." Infection and Immunity 83, no. 6 (April 6, 2015): 2518–30. http://dx.doi.org/10.1128/iai.00023-15.

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Constant cross talk betweenCandida albicansyeast cells and their human host determines the outcome of fungal colonization and, eventually, the progress of infectious disease (candidiasis). An effective weapon used byC. albicansto cope with the host defense system is the release of 10 distinct secreted aspartic proteases (SAPs). Here, we validate a hypothesis that neutrophils and epithelial cells use the antimicrobial peptide LL-37 to inactivateC. albicansat sites of candidal infection and thatC. albicansuses SAPs to effectively degrade LL-37. LL-37 is cleaved into multiple products by SAP1 to -4, SAP8, and SAP9, and this proteolytic processing is correlated with the gradual decrease in the antifungal activity of LL-37. Moreover, a major intermediate of LL-37 cleavage—the LL-25 peptide—is antifungal but devoid of the immunomodulatory properties of LL-37. In contrast to LL-37, LL-25 did not affect the generation of reactive oxygen species by neutrophils upon treatment with phorbol esters. Stimulating neutrophils with LL-25 (rather than LL-37) significantly decreased calcium flux and interleukin-8 production, resulting in lower chemotactic activity of the peptide against neutrophils, which may decrease the recruitment of neutrophils to infection foci. LL-25 also lost the function of LL-37 as an inhibitor of neutrophil apoptosis, thereby reducing the life span of these defense cells. This study indicates thatC. albicanscan effectively use aspartic proteases to destroy the antimicrobial and immunomodulatory properties of LL-37, thus enabling the pathogen to survive and propagate.
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Honda, Jennifer R., Elizabeth Connick, Samantha MaWhinney, Edward D. Chan, and Sonia C. Flores. "Plasma LL-37 correlates with vitamin D and is reduced in human immunodeficiency virus-1 infected individuals not receiving antiretroviral therapy." Journal of Medical Microbiology 63, no. 7 (July 1, 2014): 997–1003. http://dx.doi.org/10.1099/jmm.0.070888-0.

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Low levels of the vitamin D-regulated antimicrobial peptide cathelicidin (LL-37) may negatively impact the immune status of human immunodeficiency virus-1 (HIV-1) infected individuals (HIV+). We compared plasma LL-37 levels in healthy controls (HIV−) and HIV+ individuals on or off antiretroviral therapies (ARTs) (ART+ and ART−, respectively), and evaluated the relationship between vitamin D and LL-37 levels. In this cross-sectional study, levels of LL-37, 25-hydroxycholecalciferol [25(OH)D3] and 1,25-dihydroxycholecalciferol [1,25(OH)2D3] were measured from an initial cohort of 18 healthy controls and 10 HIV+/ART− individuals. Because this cohort lacked HIV+/ART+ subjects, LL-37 was also quantified from a second cohort of 10 HIV+/ART− and 13 HIV+/ART+ individuals. LL-37 levels were significantly lower in the HIV+/ART− group compared to the healthy controls (P = 0.01). A direct relationship was observed between LL-37 and both 25(OH)D3 and 1,25(OH)2D3. The level of 25(OH)D3 was predictive of higher LL-37 (P = 0.04) and for any given level of 25(OH)D3, HIV+/ART− subjects averaged 20 % lower LL-37 compared to the healthy controls (P = 0.045). For any given level of 1,25(OH)2D3, HIV+/ART− subjects averaged 25 % lower LL-37 compared to the healthy controls (P = 0.018), although 1,25(OH)2D3 was not predictive of higher LL-37 (P = 0.28). Finally, LL-37 levels were significantly lower in the HIV+/ART− group compared to the HIV+/ART+ group from the second cohort (P = 0.045). Untreated HIV infection may contribute to lower LL-37 levels, independent of vitamin D levels. ART treatment may potentially mitigate this decrease in LL-37 levels.
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Sigurdardottir, Thorgerdur, Pia Andersson, Mina Davoudi, Martin Malmsten, Artur Schmidtchen, and Mikael Bodelsson. "In Silico Identification and Biological Evaluation of Antimicrobial Peptides Based on Human Cathelicidin LL-37." Antimicrobial Agents and Chemotherapy 50, no. 9 (September 2006): 2983–89. http://dx.doi.org/10.1128/aac.01583-05.

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ABSTRACT Bacterial lipopolysaccharides (LPS) are important triggers of the widespread inflammatory response, which contributes to the development of multiple organ failure during sepsis. The helical 37-amino-acid-long human antimicrobial peptide LL-37 not only possesses a broad-spectrum antimicrobial activity but also binds and neutralizes LPS. However, the use of LL-37 in sepsis treatment is hampered by the fact that it is also cytotoxic. To find a less toxic analog of LL-37, we used in silico analysis to identify amphipathic helical regions of LL-37. A 21-amino-acid fragment (GKE) was synthesized, the biological actions of which were compared to those of two equally long peptides derived from the N and C termini of LL-37 as well as native LL-37. GKE displayed antimicrobial activity against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, Candida albicans, and Candida parapsilosis that was similar to or even stronger than LL-37. GKE, as well as the equally long control peptides, attracted granulocytes in a fashion similar to that of LL-37, while only GKE was as potent as LL-37 in inhibiting LPS-induced vascular nitric oxide production. GKE caused less hemolysis and apoptosis in human cultured smooth muscle cells than LL-37. In summary, we have identified an active domain of LL-37, GKE, which displays antimicrobial activity in vitro and LPS-binding activity similar to those of LL-37 but is less toxic. GKE therefore holds promise as a template for the development of peptide antibiotics for the treatment of sepsis.
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Sieprawska-Lupa, Magdalena, Piotr Mydel, Katarzyna Krawczyk, Kinga Wójcik, Magdalena Puklo, Boguslaw Lupa, Piotr Suder, et al. "Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus-Derived Proteinases." Antimicrobial Agents and Chemotherapy 48, no. 12 (December 2004): 4673–79. http://dx.doi.org/10.1128/aac.48.12.4673-4679.2004.

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ABSTRACT Cathelicidin LL-37 is one of the few human bactericidal peptides with potent antistaphylococcal activity. In this study we examined the susceptibility of LL-37 to proteolytic degradation by two major proteinases produced by Staphylococcus aureus, a metalloproteinase (aureolysin) and a glutamylendopeptidase (V8 protease). We found that aureolysin cleaved and inactivated LL-37 in a time- and concentration-dependent manner. Analysis of the generated fragments by mass spectroscopy revealed that the initial cleavage of LL-37 by aureolysin occurred between the Arg19-Ile20, Arg23-Ile24, and Leu31-Val32 peptide bonds, instantly annihilating the antibacterial activity of LL-37. In contrast, the V8 proteinase hydrolyzed efficiently only the Glu16-Phe17 peptide bond, rendering the C-terminal fragment refractory to further degradation. This fragment (termed LL-17-37) displayed antibacterial activity against S. aureus at a molar level similar to that of the full-length LL-37 peptide, indicating that the antibacterial activity of LL-37 resides in the C-terminal region. In keeping with LL-37 degradation by aureolysin, S. aureus strains that produce significant amounts of this metalloprotease were found to be less susceptible to LL-17-37 than strains expressing no aureolysin activity. Taken together, these data suggest that aureolysin production by S. aureus contributes to the resistance of this pathogen to the innate immune system of humans mediated by LL-37.
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Ohuchi, Kentaro, Tetsuya Ikawa, Ryo Amagai, Toshiya Takahashi, Yuna Roh, Junko Endo, Yumi Kambayashi, Yoshihide Asano, and Taku Fujimura. "LL-37 Might Promote Local Invasion of Melanoma by Activating Melanoma Cells and Tumor-Associated Macrophages." Cancers 15, no. 6 (March 9, 2023): 1678. http://dx.doi.org/10.3390/cancers15061678.

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LL-37 can stimulate various skin-resident cells to contribute to tumor development. Since tumor (T) stage is determined by the vertical invasion of tumor cells in melanoma, we hypothesized that the LL-37 expression level is correlated with the T stage in melanoma patients. Immunohistochemical staining of LL-37 was performed in each stage of melanoma (Tis-T4), suggesting the ratio of LL-37-expressing cells correlate positively to T stage severity. Next, to examine pro-angiogenetic factors induced by LL-37 stimulation, the B16F10 melanoma model was used. Intra-tumorally administered CRAMP, the mouse ortologe of LL-37, significantly increased the mRNA expression of CXCL5, IL23A, MMP1a, and MMP9 in B16F10 melanoma. To confirm the induction of pro-angiogenic factors, A375 human melanoma cells were stimulated by LL-37 in vitro. The mRNA expression of CXCL5, IL23A, and MMP9, but not MMP1, were significantly increased by LL-37 stimulation. Moreover, LL-37-stimulated A375 culture supernatant promoted tube networks, suggesting that these tumor-derived factors promote the pro-angiogenic effect on tumor development. In contrast to melanoma cell lines, M2 macrophages stimulated by LL-37 in vitro significantly increased their expression and secretion of MMP-1, but not MMP-9 expression. Collectively, these results suggest that LL-37 stimulates both tumor cells and macrophages to promote melanoma invasion by the induction of pro-angiogenic factors.
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Dissertations / Theses on the topic "LL-37"

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Filewod, Niall Christopher Jack. "Immunomodulatory effects of LL-37 in the epithelia." Thesis, University of British Columbia, 2008. http://hdl.handle.net/2429/927.

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The cationic host defence peptide LL-37 is an immunomodulatory agent that plays an important role in epithelial innate immunity. Previously, concentrations of LL-37 thought to represent levels present during inflammation have been shown to elicit the production of cytokines and chemokines by epithelial cells. To investigate the potential of lower concentrations of LL-37 to alter epithelial cell responses, normal primary keratinocytes and bronchial epithelial cells were treated with pro-inflammatory stimuli in the presence or absence of 1 – 3 μg/ml LL-37. Low, physiologically relevant concentrations of LL-37 synergistically increased IL-8 production by both proliferating and differentiated keratinocytes in response to IL-1β and the TLR5 agonist flagellin, and synergistically increased IL-8 production by bronchial epithelial cells in response to IL-1β, flagellin, and the TLR2/1 agonist PAM3CSK4. Treatment of bronchial epithelial cells with LL-37 and the TLR3 agonist poly(I:C) resulted in synergistic increases in IL-8 release and cytotoxicity. The synergistic increase in IL-8 production observed when keratinocytes were co-stimulated with flagellin and LL-37 was suppressed by pretreatment with inhibitors of Src-family kinase signalling and NF-κB translocation. These data suggest that low concentrations of LL-37 may alter epithelial responses to microbes in vivo. Microarray analysis of keratinocyte transcriptional responses after LL-37 treatment suggest that LL-37 may alter the expression of growth factors and a number of genes important to innate immune responses. LL-37 may thus play a more important role than previously suspected in the regulation of epithelial inflammation; an improved understanding of the mechanisms by which LL-37 alters chemokine responses could lead to the development of novel anti-infective and anti-inflammatory therapeutics.
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El, Abbouni Sarah. "Microencapsulation of LL-37 Antimicrobial Peptide in PLGA." Digital WPI, 2016. https://digitalcommons.wpi.edu/etd-theses/235.

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Antimicrobial peptides are key actors in organisms€™ immune systems. They play an important role in phagocytosis, breaking bacteria membranes. They destroy the microbes, keeping them from repairing themselves, and therefore do not promote antimicrobial resistance. LL37 is a peptide produced by the human body. It is a short amino acid chain that is particularly active on the skin and mucous membranes. It has antimicrobial and fungal activity as well as wound healing properties, which makes it a very interesting active substance in wound treatment. However, its fragile and sensitive structure is a challenge to its use. Nowadays, encapsulation in a biocompatible polymer system is a promising technique in drug delivery, and presents a solution to LL37 administration and delivery. LL37 is a hydrophilic active substance, it will be trapped in PLGA (poly (lactic-co-glycolic acid)) by double emulsion and the microspheres will be shaped and stabilized by solvent evaporation. The capsules will be characterized by Dynamic Light Scattering (DLS) and Scanning Electron Microscopy. Their main features, drug loading, encapsulation efficiency and release profile, are determined using the Bradford assay. Since the peptide is expensive and delicate, it is important to optimize its encapsulation. For that reason, we will adapt the process to have the best drug loading as possible using water in oil in oil emulsions. For an external use, the capsules would be used over a few days, so having a fast release is very relevant. The larger the specific surface area, the faster the diffusion. For that reason, we will also study the impact of porosity on the release profile. As a result, different types of capsules will be synthesized, with higher porosity and by two processes: aqueous double emulsion and oil double emulsion. Their characteristic features and impact on bacterial pathogens will be determined and compared in order to determine their optimal synthesis process and formulation in given conditions of use.
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Currie, Silke Maria. "Antiviral function of LL-37 on respiratory syncytial virus." Thesis, University of Edinburgh, 2016. http://hdl.handle.net/1842/25954.

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Recurrent infection with human respiratory syncytial virus (RSV) is one of the most common causes for lower respiratory tract illness (LRI) in infants, the elderly, and immunocompromised individuals. Due to lack of vaccines and therapeutic interventions, medical care of acute RSV bronchiolitis is mostly limited to supportive measures. Thus, novel treatment options to control RSV infection are desperately required. The cationic host defence peptide human cathelicidin LL-37 possesses both microbicidal and immunomodulatory properties. This essential effector of the innate immune system holds potent antiviral activity against a variety of viruses, including influenza virus, and has been proposed as a promising candidate for antiviral drug development. Previous studies revealed that lower cathelicidin levels put RSV infected infants at risk for more severe RSV disease, while infection of lung epithelial cells induced cathelicidin up-regulation. These findings suggest that LL-37 might possess antiviral activity against RSV. However, its potential antiviral function on RSV remains to be elucidated. This thesis therefore aimed to evaluate the antiviral activity of cathelicidins against RSV, by assessing its relevance in vitro and in vivo and elucidating the underlying antiviral mechanism. Firstly, the antiviral effects of human cathelicidin LL-37 against RSV were addressed in vitro. Presence of LL-37 during infection potently reduced viral titres and protected cells against virus-associated cytopathic effects. Experiments revealed that only the core region of LL-37 holds antiviral activity against RSV. Antiviral effects were also observed for the murine LL-37 orthologue mCRAMP. Administration of LL-37 at different stages in the infection cycle provided evidence that LL-37 can be used preventatively, protecting against RSV infection by directly acting on both cells and viral particles. When given therapeutically, once an infection was established, LL-37 also limited viral spread. Next, the molecular mechanism mediating the peptide’s antiviral activity was investigated. It was demonstrated that LL-37 does not affect the interferon-mediated cellular antiviral immune response to RSV. Experiments established that LL-37 does not contribute to viral clearance by inducing epithelial cell death. Further mechanistic studies revealed that the peptide directly binds to RSV particles, destabilises the integrity of the viral envelope, and prevents adsorption of RSV to epithelial cells during the entry stage of infection. Finally, the in vivo relevance of LL-37 treatment and endogenous cathelicidin expression was examined, employing both murine and human model systems. It was established that LL-37 has protective antiviral effects against RSV in vivo. In contrast to the cell culture model, only co-administration of LL-37 and RSV, but not treatment prior or post infection, protects mice from clinical signs of infection. Levels of the murine LL-37 orthologue mCRAMP were increased in RSV infected lungs, pointing towards its importance in antiviral defence. In keeping with this, mCRAMP-deficient mice were more susceptible to RSV induced disease. Equally, individuals with low nasal LL-37 baseline levels that were experimentally challenged with RSV, were more susceptible to infection. This highlights the importance of endogenous cathelicidin expression to fight and control RSV infection. Overall, these results identify LL-37 as an important antiviral agent against RSV in vitro and in vivo, and emphasise the role of endogenous cathelicidins in the defence against this pathogen. Moreover, unravelling the underlying antiviral mechanism of LL-37 against RSV adds to our understanding of how CHDP act on enveloped viruses, thus supporting the development of new antiviral treatment options.
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Frew, Lorraine. "The production and function of cervical hCAP18/LL-37 in pregnancy." Thesis, University of Edinburgh, 2014. http://hdl.handle.net/1842/18000.

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Antimicrobial peptides (AMPs) are small proteins produced by epithelial surfaces, which have broad-spectrum antimicrobial and immunomodulatory activities. In the lung, skin and alimentary tract AMPs are known to be important in infectious and inflammatory conditions. Far less is known regarding the role of AMPs within the female reproductive tract, but as infection and inflammation are causes of preterm labour, AMPs may have a key function in maintain and protecting pregnancy. The major groups of human AMPs include the human beta defensins (HBDs), two antileukoproteinases (secretory leukocyte protease inhibitor (SLPI) and Trappin-2/Elafin), and the human cathelicidin hCAP18/LL-37, with several studies identifying their presence at sites throughout the reproductive tract. The cervix in pregnancy is positioned between the upper genital tract containing the developing fetus and the lower tract where infections usually arise. I hypothesise that AMPs are fundamental to mucosal immune defence of the cervix in pregnancy, preventing ascending infection and excessive inflammation that can cause preterm labour. This thesis focused on the human cathelicidin hCAP18/LL-37 and its role within the cervix and vagina. The aims of this thesis were to; investigate the inflammatory effects of LL-37 from cervical and vaginal derived epithelial cells and determine the pathways and receptors in which LL-37 may elicit its effects and how production may be regulated; investigate the role of CRAMP in a mouse model of preterm birth; and determine the production of AMPs by the pregnant cervix whilst investigating the relationship between AMP concentrations in cervicovaginal secretions and preterm labour. The inflammatory effect of LL-37 was investigated using cell lines derived from endocervical, ectocervical and vaginal epithelium. The study of these cell lines suggests divergent responses of cervical and vaginal epithelial cells. LL-37 mediated induction of IL-8 and IL-6 production from endocervical epithelial cells was observed in a dose-dependent and time-dependent manner, whilst ectocervical and vaginal cells also respond to treatment with LL-37 through IL-8 and IL-6 production. To determine a possible mechanism of action of LL-37 on IL-8 and IL-6 in the three cell lines, inhibitors against MAPK cascades, ERK, p38 MAPK and JNK, and known LL-37 receptors were investigated. In endocervical cells LL-37 mediated IL-8 occurs via activation of unidentified GPCRs, whilst in ectocervical cells this effect on IL‐8 and IL-6 is via the activation of ERK and p38 MAPK cascades. The mechanism by which LL-37 induces IL-8 secretion in vaginal epithelial cells remains unknown. Expression of LL-37 was shown to be mediated by vitamin D3 in vitro in cervical and vaginal epithelial cells. However when this relationship was investigated in vivo, using matched serum and cervicovaginal secretions from woman at early pregnancy, no correlation was observed between circulating vitamin D and cervicovaginal or circulating hCAP18/LL-37. However, the majority of women in this study reported with insufficient levels of vitamin D, which may effect the relationship observed with hCAP18/LL-37. Using a mouse model of LPS-induced preterm labour, to mimic the presence of intrauterine infection bacterial infection, I aimed to characterise the role of CRAMP, the mouse orthologue of hCAP18/LL-37, in the lower inflammatory and immune response that results in preterm labour. Wild type C57Bl/6J mice receiving an intrauterine injection of LPS deliver prematurely, within 24 hours of injection. However mice deficient in CRAMP (Camp -/-) receiving an intrauterine injection of LPS deliver significantly later and have a non-significant increase in pup survival compared to wild type C57Bl/6J mice. Cervical tissue collected post partum showed no difference in inflammatory markers between wild type C57Bl/6J and Camp -/- mice, however there was increased expression of the neutrophil chemoattractant marker, Cxcl5, and the neutrophil marker, Ngp in Camp -/- mice. In the lower genital tract, levels of antimicrobial peptides were determined in samples of cervicovaginal secretions collected from pregnant women. AMPs, hCAP18/LL-37, HBD-2 and SLPI were found in cervicovaginal secretions, and levels of hCAP18/LL-37 were increased in women with the common vaginal infection bacterial vaginosis. However no relationship was identified between the concentration of AMPs and preterm birth in this study. This work has shown that the lower genital tract, where infections that are associated with preterm labour originate, expresses the human cathelicidin hCAP18/LL-37. It may play an important role in modulating the immune response to invading infection associated with preterm labour. Further investigation of these responses may increase understanding of the physiology and pathophysiology of labour, and lead to strategies for the prevention of premature delivery.
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Oliveira, Junior Luiz Roberto de. "Vitamina D e LL-37 em Pacientes com Doença de Chagas." Botucatu, 2018. http://hdl.handle.net/11449/153022.

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Orientador: Cilmery Suemi Kurokawa
Resumo: O texto apresentado faz parte dos estudos sobre doença de Chagas (DC), suas formas clínicas e correlação com morbidades associadas à obesidade e envelhecimento e confeccionado para obtenção do título de Mestre em Doenças Tropicais. Ele é dividido em dois capítulos, no qual o primeiro texto compreende uma revisão bibliográfica sobre a doença de Chagas, vitamina D3 e catelicidina LL-37; e, no segundo capítulo, um artigo com dados descritivos da população de estudo intitulado de “FATORES DE RISCO CARDIOVASCULAR ASSOCIADOS À DOENÇA DE CHAGAS CRÔNICA” e um artigo intitulado de “VITAMINA D3, CATELICIDINA LL-37 E POLIMORFISMOS DO GENE VDR EM PACIENTES COM A FORMA INDETERMINADA E CARDÍACA DA DOENÇA DE CHAGAS”. Atualmente a DC é uma doença tropical negligenciada em todo o mundo e endêmica em 21 países latino-americanos, com mais de 25 milhões de pessoas em área de risco de transmissão. Afeta de 8 a 10 milhões de pessoas, sendo que no Brasil estima-se que existam 3 milhões de infectados, com 6 mil mortes por ano. Em sua fase crônica, tem a forma cardíaca como a manifestações mais importante da doença, tanto por sua frequência quanto por sua gravidade, com impacto social e financeiro, já que afetam os indivíduos na fase mais produtiva da vida (entre 30 e 50 anos), com altos índices de morbimortalidade. Além dos distúrbios no sistema de condução cardíaco, pode evoluir para manifestações mais graves como cardiomegalia, falência cardíaca e morte súbita. A inexistência de drogas eficazes pa... (Resumo completo, clicar acesso eletrônico abaixo)
Abstract: The text presented is part of the studies on Chagas disease (CD), its clinical forms and correlation with morbidities associated with obesity and aging and made for the title of Masters in Tropical Diseases. It is divided into two chapters, in which the first text comprises a literature review on Chagas disease, vitamin D3 and catatelicidin LL-37; and in the second chapter an article with descriptive data from the study population entitled "CARDIOVASCULAR RISK FACTORS ASSOCIATED WITH CHRONIC CHAGAS DISEASE" and an article entitled "VITAMIN D3, CATELICIDINE LL-37 AND VDR GENE POLYMORPHOSMS IN PATIENTS WITH THE UNDETERMINED AND HEART CHAGAS DISEASE FORM". Currently, CD is a neglected tropical disease worldwide and endemic in 21 Latin American countries, with more than 25 million people at risk of transmission. It affects 8 to 10 million people, and in Brazil it is estimated that there are 3 million infected, with 6 thousand deaths a year. In its chronic phase, it has the cardiac form as the most important manifestations of the disease, as much by its frequency as by its gravity, with social and financial impact, since they affect the individuals in the most productive phase of the life (between 30 and 50 years), with high morbidity and mortality rates. In addition to disturbances in the cardiac conduction system, it can progress to more serious manifestations such as cardiomegaly, heart failure and sudden death. The lack of effective drugs to treat the disease in its chronic ph... (Complete abstract click electronic access below)
Mestre
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Carlsson, Martin, and Johan Humlén. "Effekter av den antimikrobiella peptiden LL-37 på humana osteoblasters viabilitet." Thesis, Malmö högskola, Odontologiska fakulteten (OD), 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:mau:diva-19902.

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Den antimikrobiella peptiden LL-37 finns uttryckt i alla kroppens slemhinnor och lagras i stora mängder i sekundära granula hos neutrofiler och monocyter. Förutom dess antimikrobiella effekt uppvisar LL-37 pro- alternativt anti-apoptotisk effekt på eukaryota celler beroende på celltyp. I denna studie visar vi för första gången den pro-apoptotiska effekten av LL-37 på den humana osteoblastcellinjen MG63. Vid stimulering med 4μM iakttogs en reduktion av cellantalet med 40% och en utbredd celldöd kunde fastställas genom Trypan Blue-infärgning. Genom flödescytometri sågs en förhöjd andel annexin V-positiva celler och en ökning aktivt kaspas-3 kunde påvisas genom ELISA efter stimulering med 4μM LL-37. Tillsammans med morfologiska tecken såsom skrumpning kan den pro-apoptotiska effekten av LL-37 fastställas. En kraftig och ihållande ökning av intracellulära Ca2+-koncentrationer kunde ses i Fluo 4-AM-infärgade celler i konfokalmikroskop efter stimulering med 4μM LL-37 men inte då Ca2+ exkluderades från mediet. Blockering av den dominerande spänningsberoende Ca2+- kanalen av L-typ med nifedipin hade ingen effekt på de tilltagande intracellulära Ca2+-koncentrationerna vilket påvisar en mekanism som ej involverar den kanalen. I efterföljande försök sågs dessutom att LL-37 reducerade cellantalet oberoende om Ca2+ fanns närvarande i mediet eller ej. Sammanfattningsvis visar data från denna studie att LL-37 reducerar antalet MG63-celler genom pro-apoptotisk effekt i koncentrationer som associerats med kronisk parodontit. Vi föreslår att verkningsmekanismen för apoptos sker via en permeabilisering av plasmamembranet, där tilltagande Ca2+-koncentrationer snarare får ses som en bieffekt av den förlorade membranintegriteten än en central faktor vid den apoptotiska signaleringen i detta system.
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Scott, Aaron. "Functional studies of the human antimicrobial proteins LL-37 and Eppin." Thesis, Queen's University Belfast, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.546424.

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Cassin, Margaret Emily. "The Design of Antimicrobial Detachable Thin Films for the Study of Hepatic Infections." Thesis, Virginia Tech, 2015. http://hdl.handle.net/10919/77426.

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Microbial infections are a global problem. Due to the over and misuse of antibiotics, drug-resistant pathogens are becoming more common. It is imperative to explore broad spectrum antimicrobial approaches. In this work, we modified collagen/hyaluronic acid polyelectrolyte multilayers (PEMs) with the natural antimicrobial peptide, LL-37 to study hepatic infections. LL-37 was physisorbed and covalently linked to the surface of the PEMs. Escherichia coli DH10B were cultured in the presence of LL-37modified PEMs in bacterial adhesion and contact killing models. Physisorbed LL-37 PEMs prevented bacterial adhesion and could also kill pathogens in the surrounding environment due to the release of LL-37 from the film. Immobilized LL-37 PEMs resulted in less bacterial adhesion on the surface due to the presence of the peptide. Films were then placed in contact with primary rat hepatocytes as well as in hepatocyte/bacteria co-cultures. LL-37 input concentrations up to of 16μM did not exhibit cytotoxic effects on hepatocytes. The LL-37 modified PEMs exhibited a hepatoprotective effect on albumin and urea secretion functions in co-cultures. The hepatoprotective effects were dependent on the ratio of hepatocytes and bacteria as well as the concentration of LL-37. These findings are encouraging and demonstrate that LL-37 modified PEMs can be used to investigate hepatic infections caused by bacteria.
Master of Science
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Dannehl, Claudia. "Fragments of the human antimicrobial LL-37 and their interaction with model membranes." Phd thesis, Universität Potsdam, 2013. http://opus.kobv.de/ubp/volltexte/2013/6814/.

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A detailed description of the characteristics of antimicrobial peptides (AMPs) is highly demanded, since the resistance against traditional antibiotics is an emerging problem in medicine. They are part of the innate immune system in every organism, and they are very efficient in the protection against bacteria, viruses, fungi and even cancer cells. Their advantage is that their target is the cell membrane, in contrast to antibiotics which disturb the metabolism of the respective cell type. This allows AMPs to be more active and faster. The lack of an efficient therapy for some cancer types and the evolvement of resistance against existing antitumor agents make AMPs promising in cancer therapy besides being an alternative to traditional antibiotics. The aim of this work was the physical-chemical characterization of two fragments of LL-37, a human antimicrobial peptide from the cathelicidin family. The fragments LL-32 and LL-20 exhibited contrary behavior in biological experiments concerning their activity against bacterial cells, human cells and human cancer cells. LL-32 had even a higher activity than LL-37, while LL-20 had almost no effect. The interaction of the two fragments with model membranes was systematically studied in this work to understand their mode of action. Planar lipid films were mainly applied as model systems in combination with IR-spectroscopy and X-ray scattering methods. Circular Dichroism spectroscopy in bulk systems completed the results. In the first approach, the structure of the peptides was determined in aqueous solution and compared to the structure of the peptides at the air/water interface. In bulk, both peptides are in an unstructured conformation. Adsorbed and confined to at the air-water interface, the peptides differ drastically in their surface activity as well as in the secondary structure. While LL-32 transforms into an α-helix lying flat at the water surface, LL-20 stays partly unstructured. This is in good agreement with the high antimicrobial activity of LL-32. In the second approach, experiments with lipid monolayers as biomimetic models for the cell membrane were performed. It could be shown that the peptides fluidize condensed monolayers of negatively charged DPPG which can be related to the thinning of a bacterial cell membrane. An interaction of the peptides with zwitterionic PCs, as models for mammalian cells, was not clearly observed, even though LL-32 is haemolytic. In the third approach, the lipid monolayers were more adapted to the composition of human erythrocyte membranes by incorporating sphingomyelin (SM) into the PC monolayers. Physical-chemical properties of the lipid films were determined and the influence of the peptides on them was studied. It could be shown that the interaction of the more active LL-32 is strongly increased for heterogeneous lipid films containing both gel and fluid phases, while the interaction of LL-20 with the monolayers was unaffected. The results indicate an interaction of LL-32 with the membrane in a detergent-like way. Additionally, the modelling of the peptide interaction with cancer cells was performed by incorporating some negatively charged lipids into the PC/SM monolayers, but the increased charge had no effect on the interaction of LL-32. It was concluded, that the high anti-cancer activity of the peptide originates from the changed fluidity of cell membrane rather than from the increased surface charge. Furthermore, similarities to the physical-chemical properties of melittin, an AMP from the bee venom, were demonstrated.
Aufgrund der steigenden Resistenzen von Zellstämmen gegen traditionelle Therapeutika sind alternative medizinische Behandlungsmöglichkeiten für bakterielle Infektionen und Krebs stark gefragt. Antimikrobielle Peptide (AMPs) sind Bestandteil der unspezifischen Immunabwehr und kommen in jedem Organismus vor. AMPs lagern sich von außen an die Zellmembran an und zerstören ihre Integrität. Das macht sie effizient und vor allem schnell in der Wirkung gegen Bakterien, Viren, Pilzen und sogar Krebszellen. Das Ziel dieser Arbeit lag in der physikalisch-chemischen Charakterisierung zweier Peptidfragmente die unterschiedliche biologische Aktivität aufweisen. Die Peptide LL-32 und LL-20 waren Teile des humanen LL-37 aus der Kathelizidin-Familie. LL-32 wies eine stärke Aktivität als das Mutterpeptid auf, während LL-20 kaum aktiv gegen die verschiedenen Zelltypen war. In dieser Arbeit wurde die Wechselwirkung der Peptide mit Zellmembranen systematisch anhand von zweidimensionalen Modellmembranen in dieser Arbeit untersucht. Dafür wurden Filmwaagenmessungen mit IR-spektroskopischen und Röntgenstreumethoden gekoppelt. Circulardichroismus-Spektroskopie im Volumen komplementierte die Ergebnisse. In der ersten Näherung wurde die Struktur der Peptide in Lösung mit der Struktur an der Wasser/Luft-Grenzfläche verglichen. In wässriger Lösung sind beide Peptidfragmente unstrukturiert, nehmen jedoch eine α-helikale Sekundärstruktur an, wenn sie an die Wasser/Luft-Grenzfläche adsorbiert sind. Das biologisch unwirksamere LL-20 bleibt dabei teilweise ungeordnet. Das steht im Zusammenhang mit einer geringeren Grenzflächenaktivität des Peptids. In der Zweiten Näherung wurden Versuche mit Lipidmonoschichten als biomimetisches Modell für die Wechselwirkung mit der Zellmembran durchgeführt. Es konnte gezeigt werden, dass sich die Peptide fluidisierend auf negativ geladene Dipalmitylphosphatidylglycerol (DPPG) Monoschichten auswirken, was einer Membranverdünnung an Bakterienzellen entspricht. Eine Interaktion der Peptide mit zwitterionischem Phosphatidylcholin (PC), das als Modell für Säugetierzellen verwendet wurde, konnte nicht klar beobachtet werden, obwohl biologische Experimente das hämolytische Verhalten zumindest von LL-32 zeigten. In der dritten Näherung wurde das Membranmodell näher an die Membran von humanen Erythrozyten angepasst, indem gemischte Monoschichten aus Sphingomyelin (SM) und PC hergestellt wurden. Die physikalisch-chemischen Eigenschaften der Lipidfilme wurden zunächst ausgearbeitet und anschließend der Einfluss der Peptide untersucht. Es konnte anhand verschiedener Versuche gezeigt werden, dass die Wechselwirkung von LL-32 mit der Modellmembran verstärkt ist, wenn eine Koexistenz von fluiden und Gelphasen auftritt. Zusätzlich wurde die Wechselwirkung der Peptide mit der Membran von Krebszellen imitiert, indem ein geringer Anteil negativ geladener Lipide in die Monoschicht eingebaut wurde. Das hatte allerdings keinen nachweislichen Effekt, so dass geschlussfolgert werden konnte, dass die hohe Aktivität von LL-32 gegen Krebszellen ihren Grund in der veränderten Fluidität der Membran hat und nicht in der veränderten Oberflächenladung. Darüber hinaus wurden Ähnlichkeiten zu Melittin, einem AMP aus dem Bienengift, dargelegt. Die Ergebnisse dieser Arbeit sprechen für einen Detergenzien-artigen Wirkmechanismus des Peptids LL-32 an der Zellmembran.
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Neto, Guilherme Tude Coelho. "Peptídeo antimicrobiano LL-37 e seus efeitos em stemness de diferentes células tumorais." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/5/5164/tde-06032017-104147/.

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Os peptídeos antimicrobianos desempenham papéis protetores críticos em uma gama de doenças humanas, incluindo o câncer. Vários estudos demonstraram funções - tais como proliferação, angiogênese, apoptose e imunomodulação - desses peptídeos em vias cancerígenas cruciais. Investigamos o papel do Peptídeo antimicrobiano LL-37 sobre stemness em câncer de mama (SKBR3) e células de melanoma (A375). Análise por PCR array da expressão diferencial de genes em SKBR3 e A375 com knockdown por siRNA para o mRNA de LL-37 revelou uma regulação negativa de genes relacionados com stemness, incluindo transcriptase reversa da telomerase, forkhead box D3 e para o fator indiferenciado de transcrição de células embrionárias 1, notavelmente em células de câncer de mama.Além disso, as células SKBR3 com knockdown para a expressão de LL-37 mostraram uma diminuição da produção de oncosferas em comparação com controles negativos, enquanto as células A375 exibiram uma produção aumentada. Tomados em conjunto, nossos achados indicam um papel para LL- 37 em stemness, dependendo do tipo de celular analisado
Antimicrobial peptides play critical protective roles in a range of human diseases, including cancer. Multiple studies have demonstrated functions -- such as proliferation, angiogenesis, apoptosis and immunomodulation -- of these peptides in crucial cancer pathways. We investigated the role of the antimicrobial peptide LL-37 on stemness in breast cancer (SKBR3) and melanoma cells (A375). PCR array analysis of differential gene expression in SKBR3 and A375 cancer cell lines downregulated for LL-37 expression by siRNA revealed downregulation of genes related to stemness, including telomerase reverse transcriptase, forkhead box D3 and undifferentiated embryonic cell transcription factor 1, remarkably in breast cancer cells. Furthermore, SKBR3 cells knocked down for LL-37 expression showed a decreased production of oncospheres in comparison with negative controls, while A375 cells exhibited increased production. Taken collectively, our findings indicate a role for LL-37 in cancer cell stemness depending on the cell type
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Book chapters on the topic "LL-37"

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Beaumont, Paula E., Hsin-Ni Li, and Donald J. Davidson. "LL-37: An Immunomodulatory Antimicrobial Host Defence Peptide." In Antimicrobial Peptides and Innate Immunity, 97–121. Basel: Springer Basel, 2012. http://dx.doi.org/10.1007/978-3-0348-0541-4_4.

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Nylén, Frank, Peter Bergman, Gudmundur H. Gudmundsson, and Birgitta Agerberth. "Assays for Identifying Inducers of the Antimicrobial Peptide LL-37." In Methods in Molecular Biology, 271–81. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6737-7_19.

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Wang, Guangshun, Jayaram Lakshmaiah Narayana, Biswajit Mishra, Yingxia Zhang, Fangyu Wang, Chunfeng Wang, D. Zarena, Tamara Lushnikova, and Xiuqing Wang. "Design of Antimicrobial Peptides: Progress Made with Human Cathelicidin LL-37." In Advances in Experimental Medicine and Biology, 215–40. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-3588-4_12.

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Sorkin, M., F. Jacobsen, D. Mittler, T. Hirsch, A. Gerhards, M. Lehnhardt, H. U. Steinau, and L. Steinstraesser. "Kutane adenovirale Gentherapie mit humanem Host Defense Peptid LL-37 in infizierten Verbrennungswunden der Ratte." In Chirurgisches Forum 2006, 357–58. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/3-540-34668-6_123.

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"“Come in Peace, O Day of Fasting” (SL, 62–63 [ll. 1–36], 666 [ll. 37–44]; RPH, 238–41)." In Classical Samaritan Poetry, 192–95. Penn State University Press, 2022. http://dx.doi.org/10.5325/j.ctv296mt0g.52.

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"Of Land, Ancestral Property and Prophecy in Corinna PMG 654 col. iii ll. 37–39." In The Paths of Greek, 125–48. De Gruyter, 2019. http://dx.doi.org/10.1515/9783110621747-007.

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"The Hardships of a Man with an Unlimited Income." In The Philosophy of Mr. B*rtr*nd R*ss*ll, 70–72. Routledge, 2013. http://dx.doi.org/10.4324/9780203074244-37.

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"Ellen Schrumpf FROMFU LL -T IME TO PA RT-T IME: WORKING CHILDREN I N NOR WAY FROMTHE N I NE TEE NT H TO THE T WE NT IETH C E NT URY." In The Global History of Childhood Reader, 439–59. Routledge, 2013. http://dx.doi.org/10.4324/9780203723753-37.

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"acroencdeirsnceud ss w ed i th fur ological drough t u . n th d er Weer st ian Chapter 1. This chapter is progress with parts of the epic problem of drought understanding and pr are ndi edi cctonngcearnndedpriendipcrtiinncg meteor­ prediction may finally be within our grasp. from the n ing deficiencies in ip lreaiw nf i a th ll cha A ra ct deirscoufsspiroenc ip o it f a ti dornou ti gmhet se sro ie osn . Etxuarm ns i na tto io nthoefd fr uorm at isoenvserfarl orm owmeaeoklsetxopdeecc ta atd io ens, tfhoorupgehriw od e s em th paht as liasset any long ne season (three months) to a few v ar a g ri uaebd il i ( ty tiomneaslel ri t e im sreev sc eaallessa ( cFo ig muprleex2 . a1n ) d . S ri ocmhemihxavoefp se rae sons, as these have shown the most potential for of the co e m .g p ., o M ne ann ts d elbrot and Wallis diction so far. of the hydrologi c1a9l6c8y ) clteha ar temsaen lf y ­ tem Tphoeradleb si erheatvoi understand similar -i.e., that they our of rainfal alnhdasprbeede ic ntathmeocto iv map ti lnegxtchhuas ra m cte ay ri s h ti acvseoaflam rg aenuynp ar reedfircatcatballeacnodmcphoanoetn ic t , . K an edyfOon rc eeo in f c th li emaetaerlp ie rsetdikcn ti oownnsirnecfeereean rl cyesretcooraderda in hi gsa to urgye . roacicnu fa rrence rainfall time series are (1) was made in administrative chronicles in India written somet lilmaensosmo al fyvearny large extremes, of either sign, in more than two thousand years ago (Kautilya ‘climate’. Tbheeseexta re smde ( l2y ) lpoenrg io adnsd of extremes that can c. BC). Raingauges were needed because it had to 1704 near Bur , ed Foh ll is anmdeaansd Wales- (1970) gives f." In Droughts, 52–53. Routledge, 2016. http://dx.doi.org/10.4324/9781315830896-37.

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"M 18 a3c ( L 3) e : a2n07L -D 21 , 7 M , e1a9k7i5n . s TL, Taguchi K, Duignan TP, Dhillon KS, Gordon J. Ann Surg 4. Nielsen HJ, Hammer JH, Moesgaard F, Kehlet H. Surgery 105(6):711-719, 1989. 5. B 67 ro 6 w , n19R8 , 2 . Bancewicz J, Hamid J, Tillotson G, Ward C, Irving M. Ann Surg 196(6):672-6. Fernandez LA, MacSween JM, You CK, Gorelick M. Am J Surg 1613:263-270, 1992. 7. H 57 a , m 1 id 98J4 , . Bancewicz J, Brown R, Ward C, Irving MH, Ford WL. Clin Exp Immunol 56:49-8. Tartter PI, Steinberg B, Barron DM, Martinelli G. Arch Surg 122:1264-1268. 1987. 9. J M en o s ll eenr -N LS ie , ls A en ndCe , rsH en anAbJe , rg C -S hr oirse ti nasnesnenF , PHMo , klH an odk la M n . dBP, r J Ju Shul rg CO7 , 9 M :51 ad 3 s -5 en 16G , , 19M 92 o . rtensen J, 10. Fisher E, Lennard V, Siefert P Kluge A, Johannsen R. Human Immunol 3:187-194, 1980. 11. L 10 e1n5n , ar1d9V 83 , . Maassen G, Grosse-Wilde H, Wernet P, Opelz G. Transplant Proc 15(1): 1011-12. F1o9r8d7 . CD, Warnick CT, Sheets S, Quist R, Stevens LE. Transplant Proc 19( 1): 1:456-457, 13. Cox DR. Analysis of binary data, Methuen: London, 1970. 14. Murphy PJ, Connery C, Hicks GL Jr, Blumberg N. J Thoracic Cardiovasc Surgery (in press). 15. A Pa rc tc hheSnu rg Deerlyl in 1g2e3r ( E 1 , 1 ) M : 1i3 ll 2e0r -1 S3D2 , 7 , W1e9r8 tz 8 . MJ, Grypma M, Droppert B and Anderson PA. 16. D 12 e 3 ll : i1n3g2e0r -1 E3P2 , 5 M , 1 il 9 le 8r8 , SD, Wertz MJ, Grypha M, Droppert B, Anderson PA. Arch Surg 17. Dawes LG, Aprahamian C, Condon RE and Malongi MA. Surgery 100:796-803, 1986. 18. Tartter PI. Br J Surg 75:789-792,1988. 19. A Lo gsarAwnagleN le , s , MAuprrpihly1J9G 92 , . Cayten CG, Stahl WM. Presented to the Surgical Infection Society, 20. Truilzi DJ, Vanek K, Ryan DH and Blumberg N. Transfusion (accepted for publication). 21. Murphy P, Heal JM and Blumberg N. Transfusion 31:212-217,1991. 22. Mezrow CK, Berstein I and Tartter PI. Transfusion 32:27-30, 1992. 23. BMuesdch3R2C8 , : 1 H 37 o2p , W 19 C9J3 , . Hoynck van Zpapendrecht MAW, Marquet RL, Jeekel J. N Engl J 24. W 19 a8y7m . ackJP, Warden GD, Miskell P, Gonce S, Alexander JW. World J Surg 11:387-391, 25. WaymackJP, Robb E, Alexander JW. Arch Surg 122:935-939, 1987." In Transfusion Immunology and Medicine, 301. CRC Press, 1995. http://dx.doi.org/10.1201/9781482273441-30.

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Conference papers on the topic "LL-37"

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Tripathi, Shweta, Matthew Fleming, and Kevan L. Hartshorn. "LL-37 Has Broad Spectrum Inhibitory Activity For Influenza Viruses." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2633.

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Biondi, Barbara, Silvia Millan, Fernando Formaggio, Alessandra Semenzato, and Cristina Peggion. "Synthesis and conformationof short peptides modeled after peptide LL-37." In 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.195.

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Lee, Jia-Yi, Chung-Yih Wang, Chi-Fang Huang, and An-Ting Cheng. "Interdigitated electrodes based on impedance biosensor for sensing peptide LL-37." In 2011 33rd Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2011. http://dx.doi.org/10.1109/iembs.2011.6089899.

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Smith, Margaretha, Marit Stockfelt, Sara Tengvall, Peter Bergman, Anders Linden, and Ingemar Qvarfordt. "Endotoxin exposure increases LL-37, but not calprotectin, in healthy human airways." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa3554.

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Cha, Ha-Ram, Anandi Sawant, Carnella Lee, Jonathan Hensel, George Tsuladze, and Selvarangan Ponnazhagan. "Abstract B86: Immunomodulatory effects of LL-37/CRAMP in prostate cancer progression." In Abstracts: AACR Special Conference on Tumor Immunology: Multidisciplinary Science Driving Basic and Clinical Advances; December 2-5, 2012; Miami, FL. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.tumimm2012-b86.

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Valencia, Yeny Y. P., Gabriel C. A. da Hora, and Thereza A. Soares. "INTERAÇÃO DE AGREGADOS DE POPG NA PRESENÇA DE PEPTIDEO ANTIMICROBIANOS LL 37." In Encontro Anual da biofisica 2019. São Paulo: Editora Blucher, 2019. http://dx.doi.org/10.5151/biofisica2019-23.

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Porter, Ross J., Graeme I. Murray, Ji M. Wang, Teizo Yoshimura, and Mairi H. McLean. "PTU-056 Loss of cathelicidin (LL-37) is associated with colorectal cancer progression." In British Society of Gastroenterology, Annual General Meeting, 4–7 June 2018, Abstracts. BMJ Publishing Group Ltd and British Society of Gastroenterology, 2018. http://dx.doi.org/10.1136/gutjnl-2018-bsgabstracts.397.

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Li, K., N. Tao, L. Zheng, and T. Sun. "LL-37 Restored Glucocorticoid Sensitivity Impaired by RNA Virus in Lung Epithelial Cells." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a7430.

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Lu, Xiuxiu, Qi Zhang, Guowei Song, Xiaodai Cui, Jian Yang, and Baoyuan Zhang. "The Changes of Plasma Antibacterial Peptide ll-37 in the Bloodstream Infected Children." In Selection of Abstracts From NCE 2016. American Academy of Pediatrics, 2018. http://dx.doi.org/10.1542/peds.141.1_meetingabstract.331.

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Keir, Holly Rachael, Hollian Richardson, Amy Gilmour, Daniela Alferes De Lima, Abirami Veluchamy, Chandani Hennayake, Merete B. Long, Diane Cassidy, Amelia Shoemark, and James D. Chalmers. "The Cathelicidin LL-37 and microbial dysbiosis in COPD patients receiving inhaled corticosteroids." In ERS Lung Science Conference 2022 abstracts. European Respiratory Society, 2022. http://dx.doi.org/10.1183/23120541.lsc-2022.185.

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