Results 91 to 100 of about 52,950,106 (199)

Cathelicidin (LL-37) protects hamsters from lethal Leptospira infection.

open access: yes, 2016
(A) Survival in hamsters pre-treated with 1 mg/kg of cathelicidin (LL-37) (n = 7) was significantly greater than LL-37 scrambled peptide (Scrambled) (n = 7) (P = 0.016) or ddH2O-treated controls (ddH2O) (n = 7) (P = 0.008) following lethal challenge with
Ruth R. Montgomery (139579)   +18 more
core   +1 more source

A Novel Pathway of Platelet Activation in ACS Mediated by LL-37 Immunoglobulin G Autoantibody Immune Complexes

open access: yesJACC: Basic to Translational Science
Summary: The cathelicidin antimicrobial peptide LL-37 is a self-antigen in neutrophil extracellular traps that provokes autoantibody responses in autoimmune/autoinflammatory conditions.
Paul C. Dimayuga, PhD   +8 more
doaj   +1 more source

Antimicrobial peptide LL-37 ameliorates a murine sepsis model via the induction of microvesicle release from neutrophils

open access: yesInnate Immunity, 2020
Sepsis is a life-threatening disease caused by systemic dys-regulated inflammatory response to infection. We previously revealed that LL-37, a human cathelicidin antimicrobial peptide, improves the survival of cecal ligation and puncture septic mice ...
Yumi Kumagai   +5 more
doaj   +1 more source

Evaluation of Anti-microbial Peptide (Cathelicidin/Ll-37) Levels in Ethanol-Induced Pulmonary Vitamin D Dysmetabolism

open access: yes, 2015
Introduction: Vitamin D has been recognized to play an important role in human immune system and function. In the pulmonary system, vitamin D regulates the function of anti-microbial peptides such as Cathelicidin/LL-37.
Ogunsakin, Olalekan Akintunde
core  

LL-37, the only human member of the cathelicidin family of antimicrobial peptides

open access: yesBiochimica et Biophysica Acta (BBA) - Biomembranes, 2006
Antimicrobial peptides and their precursor molecules form a central part of human and mammalian innate immunity. The underlying genes have been thoroughly investigated and compared for a considerable number of species, allowing for phylogenetic characterization.
Dürr, Ulrich H.N.   +2 more
openaire   +2 more sources

Group A Streptococcal M1 protein sequesters cathelicidin to evade innate immune killing [PDF]

open access: yes, 2015
SummaryThe antimicrobial peptide LL-37 is generated upon proteolytic cleavage of cathelicidin and limits invading pathogens by directly targeting microbial membranes as well as stimulating innate immune cell function.
Todd, Jordan   +19 more
core   +1 more source

Examining the Use of Ceftaroline in the Treatment of Streptococcus pneumoniae Meningitis with Reference to Human Cathelicidin LL-37 [PDF]

open access: yes
Five cases of bacterial meningitis treated with ceftaroline (4 Streptococcus pneumoniae and 1 Staphylococcus aureus) are summarized here. The pharmacodynamics of human cathelicidin LL-37 and ceftaroline were evaluated against S. pneumoniae.
Rybak, Michael J.   +5 more
core   +2 more sources

The di-leucine motif in the host defense peptide LL-37 is essential for initiation of autophagy in human macrophages

open access: yesCell Reports
Summary: The human cathelicidin peptide LL-37 induces autophagy in human macrophages. Different post-translational modifications (PTMs) such as citrullination, acetylation, and formylation impact LL-37, yet their effect on autophagy remains unknown. Thus,
Rokeya Sultana Rekha   +8 more
doaj   +1 more source

Stability of the Cathelicidin Peptide LL-37 in a Non-healing Wound Environment

open access: yesActa Dermato Venereologica, 2011
The endogenous cathelicidin peptide LL-37 is strongly expressed at the wound edge early in the process of acute wound healing, but only weakly expressed in chronic wounds. Excessive proteolysis may limit the therapeutic usefulness of exogenous LL-37, especially in ulcers colonized with Pseudomonas aeruginosa that produce elastase, which degrades LL-37.
Alvar, Grönberg   +2 more
openaire   +3 more sources

Human cathelicidin peptide LL-37 induces endothelial-to-mesenchymal transition

open access: yesBioscience, Biotechnology, and Biochemistry
Abstract Endothelial-to-mesenchymal transition (EndMT) is a process that causes endothelial cells (ECs) to lose their EC characteristics and transform into mesenchymal cells. Accumulating studies suggest that EndMT is induced in atherosclerotic plaques and contributes to the pathogenesis of atherosclerosis.
Kaori Suzuki, Mari Ohkuma, Isao Nagaoka
openaire   +2 more sources

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