Human cathelicidin LL-37 inhibits platelet aggregation and thrombosis via Src/PI3K/Akt signaling.
Su. Wen W; Chen. Yahui Y; Wang. Caihui C; Ding. Xue X; Rwibasira. Gamariel G; Kong. Yi Y
Key Findings
- LL-37 reduced human platelet aggregation in vitro.
- LL-37 lowered thrombus (clot) formation in live animal experiments.
- The peptide decreased activation markers like Src phosphorylation, Akt (Ser473) phosphorylation, platelet spreading on fibrinogen, and P‑selectin expression.
Practical Outcomes
- LL-37 shows promise as a natural anti‑clotting agent, which could be relevant for longevity or cardiovascular health strategies. However, the study provides no dosage, delivery method, or safety data for human use, so it isn’t ready for self‑experimentation. Enthusiasts should view this as a mechanistic insight that may guide future research rather than an immediate protocol.
Summary
The human peptide LL-37, known for fighting infections, also blocks platelets from clumping together and forming clots in lab tests and animal models. It does this by turning down key signaling proteins (Src and Akt) that tell platelets to stick and activate.
Abstract
Biological functions of human cathelicidin LL-37 have been widely reported, including antibacterial, immune and anti-tumor effects. However, the antiplatelet activity of LL-37 has not been addressed. The purpose of our study was to investigate the antiplatelet and antithrombotic actions of LL-37. We found that this peptide inhibited human platelet aggregation in vitro and attenuated thrombus formation in vivo. Furthermore, LL-37 reduced phosphorylation of Src kinase and Akt(Ser473), decreased platelet spreading on immobilized fibrinogen and inhibited P-selectin expression on platelets. These results demonstrate that LL-37 has antiplatelet and antithrombotic actions.
Study Information
pubmed
2016
2016-03-21T00:00:00.000Z
10.1016/j.bbrc.2016.03.095
22
39