Modulation of cytokine gene expression by cathelicidin BMAP-28 in LPS-stimulated and -unstimulated macrophages

D'Este, Francesca; Tomasinsig, Linda; Skerlavaj, Barbara; Zanetti, Margherita

doi:10.1016/j.imbio.2012.01.010

Cited by 19 publications

(25 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Previous investigations revealed that a number of cationic and amphipathic AMPs derived from animals, including LL37 (human) [25,27], ␤-defensins (human) [24,41], a cathelicidin-derived AMP of 37 amino acid residues [CAP18(106-142); rabbit] [18], a proline-rich AMP of 39 amino acid residues, (PR-39; porcine) [10], a bovine myeloid AMP of 28 amino acid residues (BMAP-28; bovine) [8], and a tryptophan-rich AMP of 13 amino acid residues (indolicidin; bovine) [36], both exhibited antimicrobial activity against pathogens and exerted significant anti-inflammatory effects by inhibiting LPS-induced TLR4 signaling. These peptides are potent, dual-function, host defense peptides because they can protect against infection by pathogens and express immunomodulatory activity.…”

Section: Discussionmentioning

confidence: 99%

Endotoxin-neutralizing activity and mechanism of action of a cationic α-helical antimicrobial octadecapeptide derived from α-amylase of rice

et al. 2016

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Endotoxin-neutralizing activity and mechanism of action of a cationic α-helical antimicrobial octadecapeptide derived from α-amylase of rice

et al. 2016

View full text Add to dashboard Cite

“…The OD value between 0 and 6 min was calculated for the control (containing peptide but no LPS), and this value was subtracted from the OD values between 0 and 6 min for the samples, which contained peptide plus LPS. The percentage reduction in procoagulant activation is directly proportional to the percentage of LPS bound [3,5,8]. Each experiment was performed in triplicate, and repeated three times independently.…”

Section: Measurement Of Lps Bindingmentioning

confidence: 99%

Enhancement of the antimicrobial activity and selectivity of GNU7 against Gram-negative bacteria by fusion with LPS-targeting peptide

et al. 2016

View full text Add to dashboard Cite

“…Antimicrobial peptides that reduce or prevent the presentation of LPS to its predominant receptors can be applied to ease the immunological response to sepsis caused by Gram-negative bacteria (27, 28). Therefore, BMAP-28’s inhibitory effect on Leptospira infections was tested at the cellular level, and we found that it is capable of inhibiting L-LPS-induced cellular cytokine release in BFF_NCC1 cells, which was supported by earlier research (28).…”

Section: Discussionmentioning

confidence: 99%

Inhibitory effect of BMAP-28 on Leptospiral Lipopolysaccharide-Induced TLR2-Dependent Immune Response in Bovine Cells

Guo

Zhang

et al. 2016

Jundishapur J Microbiol

View full text Add to dashboard Cite

BackgroundBovine leptospirosis is a widespread zoonotic disease, leading to serious economic losses in animal production and causing potential hazards to human health. Leptospiral lipopolysaccharide (L-LPS) plays an important role in leptospirosis pathogenicity.ObjectivesWith respect to L-LPS endotoxin-like activity, we examined bovine immune response to L-LPS and the inhibitory ability of bovine myeloid antimicrobial peptide-28 (BMAP-28) against L-LPS-induced immune activation in bovine cells.Materials and MethodsIn this study, L-LPS-induced proinflammatory cytokine production in bovine cells was quantitatively measured with real-time PCR and ELISA, and we determined which cell membrane receptors (toll-like receptor [TLR]2 and TLR4) played a major role. In addition, the ability of BMAP-28 to inhibit L-LPS-induced endotoxin-like immune activation in bovine cells was determined by the decrease in cytokine secretion.ResultsL-LPS showed the ability to induce cytokine production in bovine cells, and its induction was TLR2-dependent. BMAP-28 was used to inhibit L-LPS-induced endotoxin-like activity. The function of BMAP-28 was to inhibit LPS-induced TLR2 expression and cytokine production.ConclusionsIn this study, the L-LPS immune response of bovine cells was significant, indicating that TLR2 is the predominant receptor for L-LPS. Due to L-LPS endotoxin-like activity, we found a strategy through using BMAP-28 to prevent L-LPS-induced TLR2-dependent immune activation in bovine cells.

show abstract

Modulation of cytokine gene expression by cathelicidin BMAP-28 in LPS-stimulated and -unstimulated macrophages

Cited by 19 publications

References 56 publications

Endotoxin-neutralizing activity and mechanism of action of a cationic α-helical antimicrobial octadecapeptide derived from α-amylase of rice

Endotoxin-neutralizing activity and mechanism of action of a cationic α-helical antimicrobial octadecapeptide derived from α-amylase of rice

Enhancement of the antimicrobial activity and selectivity of GNU7 against Gram-negative bacteria by fusion with LPS-targeting peptide

Inhibitory effect of BMAP-28 on Leptospiral Lipopolysaccharide-Induced TLR2-Dependent Immune Response in Bovine Cells

Contact Info

Product

Resources

About