Molecular mechanisms of LL-37-induced receptor activation: An overview.
Verjans. Eddy-Tim ET; Zels. Sven S; Luyten. Walter W; Landuyt. Bart B; Schoofs. Liliane L
Key Findings
- LL-37 can activate several unrelated cell‑surface receptors and intracellular targets.
- The exact molecular handshake between LL-37 and its receptors is not well defined, with few classic ligand‑receptor examples.
- The review compiles current evidence of downstream signaling pathways triggered by LL-37.
Practical Outcomes
- For now, the information is mostly scientific background and doesn’t translate into clear dosing or usage tips. It signals that any DIY LL-37 experiments should be done cautiously and that more research is needed before claiming specific health benefits.
Summary
LL-37 is a natural peptide that helps the immune system, but scientists still don’t fully know how it talks to many different cell receptors. This review gathers what we do know about the ways LL-37 can turn on these receptors, showing that the exact binding tricks are still fuzzy and often indirect.
Abstract
The human cathelicidin peptide LL-37 plays a crucial role in the immune system on many levels, from the first line of defense in epithelial cells to restoring the tissue after infection. On host cells, the majority of the LL-37-induced effects are mediated via the direct or indirect activation of several structurally unrelated cell surface receptors or intracellular targets. How LL-37 is able to affect multiple receptors is currently not well understood. So far, the mechanistic details underlying receptor activation are poorly investigated and evidence for a conventional ligand/receptor interaction is scarce. Over the past few decades, a large number of studies have reported on the activation of a receptor and/or components of the downstream signal transduction pathway induced by LL-37. This review summarizes the current knowledge on molecular mechanisms underlying LL-37-induced receptor activation.
Study Information
pubmed
2016
2016-09-05T00:00:00.000Z
10.1016/j.peptides.2016.09.002
74
118