Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Human dermal endothelial cells treated with sno U1 dsRNA and antimicrobial peptide LL-37

ABSTRACT: Next generation sequencing (RAN-seq) was used to study the global effects of co-treatment of endothelial cells with U1 and LL-37. This lead to identification of differentially regulated genes and enriched pathways

ORGANISM(S): Homo sapiens

PROVIDER: GSE129160 | GEO | 2019/04/02

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Similar Datasets

Human dermal endothelial cells co-treated with dsRNA mimic poly IC and antimicrobial peptide LL-37

Project description:Next generation sequencing (RNA-seq) was used to study the global effects of co-treatment of endothelial cells with poly IC and LL-37. This lead to identification of differentially regulated genes and enriched pathways

2019-04-02 | GSE129152 | GEO

Human dermal endothelial cells treated with sno U1 dsRNA and antimicrobial peptide LL-37

Project description:Human dermal endothelial cells treated with sno U1 dsRNA and antimicrobial peptide LL-37

| PRJNA530257 | ENA

Proteomic adaptation of Streptococcus pneumoniae to the human antimicrobial peptide LL-37

Project description:Secreted antimicrobial peptides (AMPs) are an important part of the human innate immune system and prevent local and systemic infections by inhibiting bacterial growth in a concentration dependent manner. In the respiratory tract, the cationic peptide LL-37 is one of the most abundant AMPs and capable of building pore complexes in usually negatively charged bacterial membranes, leading to destruction of bacteria. However, adaptation mechanisms of several pathogens to LL-37 are already described and are known to weaken the antimicrobial effect of the AMP, for instance, by repulsion, export or degradation of the peptide. This study examines proteome wide changes in Streptococcus pneumoniae D39, the leading cause of bacterial pneumonia, in response to physiological concentrations of LL-37 by high resolution mass spectrometry. Our data indicate that pneumococci may use some of the known adaptation mechanisms to reduce the effect of LL-37 on their physiology, too. Additionally, several proteins seem to be involved in resistance to AMPs which have not been related to this process before, such as the teichoic acid flippase TacF (SPD_1128). Understanding colonization and infection relevant adaptations of the pneumococcus to AMPs, especially LL-37, could finally uncover new drug targets to weaken the burden of this widespread pathogen.

2020-03-19 | PXD016511 | Pride

The human cathelicidin antimicrobial peptide LL-37 promotes the growth of the pulmonary pathogen Aspergillus fumigatus.

Project description:Aspergillus fumigatus contributes to invasive and allergic pulmonary disease in immunocompromised individuals. The pulmonary mucus of cystic fibrosis (CF) patients displays elevated levels of the pleiotropic cathelicidin antimicrobial peptide LL-37 and the aim of this work was to assess the effect of LL-37 on the growth A. fumigatus. Exposure of A. fumigatus conidia to high concentrations of intact LL-37 (100 μg/ml) for 24 hours had a positive effect on growth (277.45 ± 22.59% (p < 0.01)) whereas scrambled LL-37 (76.45 ± 7.46%) did not. Exposure of 24 hour pre-formed mycelium to 5 μg/ml LL-37 for 48 hours increased hyphal wet weight significantly (4.37 ± 0.23 g, p < 0.001) compared to the control (2.67 ± 0.05 g). Amino acid leakage from mycelium was observed in the presence of LL-37 and gliotoxin secretion was increased at 24 hours from LL-37 exposed hyphae (169.1 ± 6.36 ng/mg hyphae, p < 0.05) compared to the control (102 ± 18.81 ng/mg hyphae). Quantitative proteomic analysis of 24 hour LL-37 treated hyphae revealed an increase in the abundance of proteins associated with growth (eIF-5A (16.3 fold increased), tissue degradation (aspartic endopeptidase (4.7 fold increased)) and allergic reactions (Asp F13 (10 fold increased)). By 48 hours there was an increase in proteins indicative of cellular stress (glutathione peroxidase (9 fold increased)), growth (eIF-5A (6 fold increased), and virulence (ribonuclease mitogillin (3.7 fold increased). These results indicate that LL-37 stimulates A. fumigatus growth and this may result in increased fungal growth and secretion of toxins in the lungs of CF patients.

2018-05-22 | PXD008143 | Pride

RNA-seq analysis of growth factor response of NHEKs to antimicrobial petide LL-37 and dsRNA mimic Poly(I:C)

Project description:In this study, we analyzed how non-coding double stranded RNA (dsRNAs) act as a damage associated molecular pattern (DAMP) in the skin, and how the human cathelicidin AMP LL-37 might influence growth factor production in response to this DAMP.

2016-05-23 | GSE79343 | GEO

Collagen synthesis is suppressed in dermal fibroblasts by the human antimicrobial peptide LL-37.

Project description: Not available

| S-EPMC2665190 | biostudies-literature

Transcriptional profiling of THP-1 cells on treatment with LL-37 and nano conjugated LL-37

Project description:Gene expression in THP-1 cells treated for 6 hours with CNT and GNP conjugated with LL-37, LL-37 spiked as well as free LL-37: Reference (Total RNA Mixture of all samples) vs. treated cells

2017-06-17 | GSE98630 | GEO

Human dermal endothelial cells co-treated with dsRNA mimic poly IC and antimicrobial peptide LL-37

Project description:Human dermal endothelial cells co-treated with dsRNA mimic poly IC and antimicrobial peptide LL-37

| PRJNA530247 | ENA

Transcriptional response of Pseudomonas aeruginosa PAO1 to human host defense peptide LL-37

Project description:In this experiment the transcriptional response of the opportunistic human pathogen Pseudomonas aeruginosa towards physiological concentrations of the major human host defense peptide LL-37 was investigated using microarrays. To this aim, three independent cultures of P. aeruginosa PAO1 were grown until mid-log phase in Mueller-Hinton broth and subsequently incubated with either sublethal LL-37 concencentrations (20 M-5g/ml) or without peptide for 2 h at 37 M-0C following RNA extraction and microarray analysis.

2013-12-20 | E-MEXP-3970 | biostudies-arrayexpress

Antimicrobial peptide LL-37 is bactericidal against Staphylococcus aureus biofilms.

Project description: Not available

| S-EPMC6553709 | biostudies-literature