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- W2885699562 abstract "Abstract Leukocyte-released antimicrobial peptides contribute to pathogen elimination and activation of the immune system. Their role in thrombosis is incompletely understood. Here we show that the cathelicidin LL-37 is abundant in thrombi from patients with acute myocardial infarction. Its mouse homologue, CRAMP, is present in mouse arterial thrombi following vascular injury, and derives mainly from circulating neutrophils. Absence of hematopoietic CRAMP in bone marrow chimeric mice reduces platelet recruitment and thrombus formation. Both LL-37 and CRAMP induce platelet activation in vitro by involving glycoprotein VI receptor with downstream signaling through protein tyrosine kinases Src/Syk and phospholipase C. In addition to acute thrombosis, LL-37/CRAMP-dependent platelet activation fosters platelet–neutrophil interactions in other inflammatory conditions by modulating the recruitment and extravasation of neutrophils into tissues. Absence of CRAMP abrogates acid-induced lung injury, a mouse pneumonia model that is dependent on platelet–neutrophil interactions. We suggest that LL-37/CRAMP represents an important mediator of platelet activation and thrombo-inflammation." @default.
- W2885699562 created "2018-08-22" @default.
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- W2885699562 date "2018-04-18" @default.
- W2885699562 modified "2023-10-03" @default.
- W2885699562 title "Cathelicidins prime platelets to mediate arterial thrombosis and tissue inflammation" @default.
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- W2885699562 doi "https://doi.org/10.1038/s41467-018-03925-2" @default.
- W2885699562 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5906636" @default.
- W2885699562 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29670076" @default.
- W2885699562 hasPublicationYear "2018" @default.
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