Results 31 to 40 of about 1,333,743 (274)

The human cathelicidin peptide LL-37 inhibits pancreatic cancer growth by suppressing autophagy and reprogramming of the tumor immune microenvironment

open access: yesFrontiers in Pharmacology, 2022
Pancreatic cancer is amongst the most lethal malignancies, while its poor prognosis could be associated with promotion of autophagy and the tumor immune microenvironment.
Zhu Zhang   +14 more
doaj   +1 more source

The Antimicrobial Peptide, LL-37, Inhibits in vitro Osteoclastogenesis [PDF]

open access: yesJournal of Dental Research, 2012
Uncoupled bone resorption leads to net alveolar bone loss in periodontitis. The deficiency of LL-37, the only human antimicrobial peptide in the cathelicidin family, in patients with aggressive periodontitis suggests that LL-37 may play a pivotal role in the inhibition of alveolar bone destruction in periodontitis.
Supanchart, C.   +6 more
openaire   +5 more sources

Cathelicidin LL-37: LPS-neutralizing, pleiotropic peptide. [PDF]

open access: yesAnnals of agricultural and environmental medicine : AAEM, 2007
Human organism, constantly exposed to a large variety of pathogenic microorganisms and their products, such as lipopolysaccharide (LPS), developed innate immunity as a first line of defence. One of the compartments of our organism well equipped with these defence mechanisms is the respiratory system. The cells lining the airways respond to the presence
Golec, Marcin, Golec, M
openaire   +3 more sources

The antimicrobial peptide LL-37 triggers release of apoptosis-inducing factor and shows direct effects on mitochondria

open access: yesBiochemistry and Biophysics Reports, 2022
The human antimicrobial peptide LL-37 permeabilizes the plasma membrane of host cells, but LL-37-induced direct effects on mitochondrial membrane permeability and function has not been reported.
Elisabeth Bankell   +6 more
doaj   +1 more source

Identifying the Critical Domain of LL-37 Involved in Mediating Neutrophil Activation in the Presence of Influenza Virus: Functional and Structural Analysis. [PDF]

open access: yesPLoS ONE, 2015
The human cathelicidin LL-37 has been shown to play a role in host defense against influenza A viruses (IAV) through direct antiviral effects and through modulating inflammatory responses to infection.
Shweta Tripathi   +5 more
doaj   +1 more source

The potentials of short fragments of human anti-microbial peptide LL-37 as a novel therapeutic modality for diseases

open access: yesFrontiers in Bioscience-Landmark, 2021
Human cathelicidin antimicrobial peptide LL-37 (LL-37) is an antimicrobial peptide derived from its precursor protein hCAP18, which is an only cathelicidin in human.
Keqiang Chen   +4 more
doaj   +1 more source

Roles and Mechanisms of Human Cathelicidin LL-37 in Cancer [PDF]

open access: yesCellular Physiology and Biochemistry, 2018
LL-37, the C-terminal peptide of human cathelicidin antimicrobial peptide (CAMP, hCAP18), reportedly increases resistance to microbial invasion and exerts important physiological functions in chemotaxis, promotion of wound closure, and angiogenesis. Accumulating evidence indicates that LL-37 also plays a significant role in human cancer.
Xi Chen   +6 more
openaire   +3 more sources

Involvement of the Antimicrobial Peptide LL-37 in Human Atherosclerosis [PDF]

open access: yesArteriosclerosis, Thrombosis, and Vascular Biology, 2006
Objective— Antimicrobial peptides are effector molecules of the innate immune system. To understand the function of vascular innate immunity in atherosclerosis, we investigated the role of LL-37, a cathelicidin antimicrobial peptide, in the disease process.
Kristina, Edfeldt   +7 more
openaire   +2 more sources

Evaluation of the ability of LL-37 to neutralise LPS in vitro and ex vivo. [PDF]

open access: yesPLoS ONE, 2011
BackgroundHuman cathelicidin LL-37 is a cationic antimicrobial peptide (AMP) which possesses a variety of activities including the ability to neutralise endotoxin. In this study, we investigated the role of LPS neutralisation in mediating LL-37's ability
Aaron Scott   +9 more
doaj   +1 more source

Characterizing the role of cell-wall β-1,3-exoglucanase Xog1p in Candida albicans adhesion by the human antimicrobial peptide LL-37. [PDF]

open access: yesPLoS ONE, 2011
Candida albicans is the major fungal pathogen of humans. Its adhesion to host-cell surfaces is the first critical step during mucosal infection. Antimicrobial peptides play important roles in the first line of mucosal immunity against C.
Pei-Wen Tsai   +3 more
doaj   +1 more source

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