LL-37
LL-37 is the only known human cathelicidin, a 37-amino-acid antimicrobial peptide generated by cleavage of the precursor protein hCAP18. In research it plays a central role in innate immune defence and wound healing, yet acts in a context-dependent manner as both anti- and pro-inflammatory and has been linked to autoimmune processes. LL-37 is not an approved drug; the evidence base is predominantly basic and preclinical.
Mechanism of action
LL-37 is a cationic, amphipathic helical peptide and the only member of the cathelicidin family in humans. It is generated by proteolytic cleavage from the C-terminal portion of the precursor protein hCAP18 (CAP-18). Mechanistically it associates with and can permeabilize microbial membranes; in addition it modulates immune cells, influences cytokine release, exerts chemotactic activity, and can bind extracellular self-DNA. Preclinical models have described both anti-inflammatory and pro-inflammatory effects, depending on concentration and tissue context.
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Wat de studies laten zien
Waar studies elkaar tegenspreken
Is LL-37 anti-inflammatory or pro-inflammatory?
Farmacokinetiek
Veiliger gebruik & risico's
Interacties & combinaties
Juridische status per land
Reconstitutie-calculator
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- 3Resultaat = concentratie in mg per mL.
Studieregister
LL-37, the only human member of the cathelicidin family of antimicrobial peptides
The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium
Induction of keratinocyte migration via transactivation of the epidermal growth factor receptor by the antimicrobial peptide LL-37
Cathelicidin LL-37: a defense molecule with a potential role in psoriasis pathogenesis
Bronnen & methode
Ontvang nieuwe studies over LL-37
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