Results 11 to 20 of about 191,557 (278)

Antimicrobial peptide LL-37 increases rhinovirus-induced interferon β expression in human airway epithelial cells through a Ca2+-dependent mechanism [PDF]

open access: yesBiochemistry and Biophysics Reports
The human cathelicidin LL-37 is active against both bacteria and viruses, but it also shows immunomodulatory properties. Here, we assess the impact of LL-37 on viral signaling in human airway epithelial BEAS-2B cells infected with the respiratory ...
Samuel Cerps   +6 more
doaj   +2 more sources

Role of antimicrobial peptide cathelicidin in thrombosis and thromboinflammation

open access: yesFrontiers in Immunology, 2023
Thrombosis is a frequent cause of cardiovascular mortality and hospitalization. Current antithrombotic strategies, however, target both thrombosis and physiological hemostasis and thereby increase bleeding risk.
Qing Zhang   +6 more
doaj   +1 more source

The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent

open access: yesAntibiotics, 2021
The rise in antimicrobial resistant bacteria threatens the current methods utilized to treat bacterial infections. The development of novel therapeutic agents is crucial in avoiding a post-antibiotic era and the associated deaths from antibiotic ...
Kylen E. Ridyard, Joerg Overhage
doaj   +1 more source

The collectin SP-A and its trimeric recombinant fragment protect alveolar epithelial cells from the cytotoxic and proinflammatory effects of human cathelicidin in vitro

open access: yesFrontiers in Immunology, 2022
Human cathelicidin (LL-37) is a defense peptide with antimicrobial activity against various pathogens. However, LL-37 can also trigger tissue injury by binding to host cell membranes.
Lidia de Tapia   +4 more
doaj   +1 more source

LL-37 Triggers Antimicrobial Activity in Human Platelets

open access: yesInternational Journal of Molecular Sciences, 2023
Platelets play a crucial role in hemostasis and the immune response, mainly by recognizing signals associated with vascular damage. However, it has recently been discovered that the antimicrobial peptide LL-37 activates platelets in functions related to thrombus formation and inflammation.
Francisco Javier Sánchez-Peña   +7 more
openaire   +2 more sources

Defense of the Skin with LL-37 [PDF]

open access: yesJournal of Investigative Dermatology, 2009
As the first line of defense against invading organisms, the skin uses a multiplicity of processes to ensure host survival, including physical, immunological, and innate systems of defense. The innate immune system, which defends skin in a nonspecific fashion, includes the cathelicidins and the single currently known human cathelicidin, hCAP18.
Bouzari, Navid   +2 more
openaire   +2 more sources

LL-37 induces polymerization and bundling of actin and affects actin structure. [PDF]

open access: yesPLoS ONE, 2012
Actin exists as a monomer (G-actin) which can be polymerized to filaments) F-actin) that under the influence of actin-binding proteins and polycations bundle and contribute to the formation of the cytoskeleton.
Asaf Sol   +3 more
doaj   +1 more source

Endogenous antimicrobial peptide LL-37 induces human vasodilatation [PDF]

open access: yesBritish Journal of Anaesthesia, 2008
Septic shock includes blood vessel dilatation and activation of innate immunity, which in turn causes release of antimicrobial peptides such as LL-37. It has been shown that LL-37 can attract leucocytes via the lipoxin A(4) receptor (ALX, FPRL1). ALX is also present in vascular endothelial cells. To explore possible ways of pharmacological intervention
I, Berkestedt, A, Nelson, M, Bodelsson
openaire   +2 more sources

The ratio of serum LL-37 levels to blood leucocyte count correlates with COVID-19 severity

open access: yesScientific Reports, 2022
Beneficial effects of vitamin D on COVID-19 progression have been discussed in several studies. Vitamin D stimulates the expression of the antimicrobial peptide LL-37, and evidence shows that LL-37 can antagonize SARS-CoV-2.
Matthias Keutmann   +7 more
doaj   +1 more source

Beta-Lactamase Repressor BlaI Modulates Staphylococcus aureus Cathelicidin Antimicrobial Peptide Resistance and Virulence. [PDF]

open access: yes, 2015
BlaI is a repressor of BlaZ, the beta-lactamase responsible for penicillin resistance in Staphylococcus aureus. Through screening a transposon library in S.
Gallo, Richard L   +6 more
core   +10 more sources

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