Biomaterial Database

LL-37 Triggers Antimicrobial Activity in Human Platelets. 2023

Francisco Javier Sánchez-Peña, and María de Los Ángeles Romero-Tlalolini, and Honorio Torres-Aguilar, and Diego Sait Cruz-Hernández, and Rafael Baltiérrez-Hoyos, and Saraí Remedios Sánchez-Aparicio, and Alba Soledad Aquino-Domínguez, and Sergio Roberto Aguilar-Ruiz

Departamento de Biomedicina Experimental, Facultad de Medicina y Cirugía de la Universidad Autónoma "Benito Juárez" de Oaxaca, Oaxaca 68120, México.

Platelets play a crucial role in hemostasis and the immune response, mainly by recognizing signals associated with vascular damage. However, it has recently been discovered that the antimicrobial peptide LL-37 activates platelets in functions related to thrombus formation and inflammation. Therefore, this work aims to evaluate the effect of LL-37 on the activation of antimicrobial functions of human platelets. Our results show that platelets treated with LL-37 increase the surface expression of receptors (Toll-like receptors (TLRs) 2 and -4, CD32, CD206, Dectin-1, CD35, LOX-1, CD41, CD62P, and αIIbβ3 integrins) for the recognition of microorganisms, and molecules related to antigen presentation to T lymphocytes (CD80, CD86, and HLA-ABC) secrete the antimicrobial molecules: bactericidal/permeability-increasing protein (BPI), azurocidin, human neutrophil peptide (HNP) -1, and myeloperoxidase. They also translate azurocidin, and have enhanced binding to Escherichia coli, Staphylococcus aureus, and Candida albicans. Furthermore, the supernatant of LL-37-treated platelets can inhibit E. coli growth, or platelets can employ their LL-37 to inhibit microbial growth. In conclusion, these findings demonstrate that LL-37 participates in the antimicrobial function of human platelets.

UI	MeSH Term	Description	Entries
D001792	Blood Platelets	Non-nucleated disk-shaped cells formed in the megakaryocyte and found in the blood of all mammals. They are mainly involved in blood coagulation.	Platelets,Thrombocytes,Blood Platelet,Platelet,Platelet, Blood,Platelets, Blood,Thrombocyte
D002352	Carrier Proteins	Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes.	Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D004926	Escherichia coli	A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.	Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000890	Anti-Infective Agents	Substances that prevent infectious agents or organisms from spreading or kill infectious agents in order to prevent the spread of infection.	Anti-Infective Agent,Anti-Microbial Agent,Antimicrobial Agent,Microbicide,Microbicides,Anti-Microbial Agents,Antiinfective Agents,Antimicrobial Agents,Agent, Anti-Infective,Agent, Anti-Microbial,Agent, Antimicrobial,Agents, Anti-Infective,Agents, Anti-Microbial,Agents, Antiinfective,Agents, Antimicrobial,Anti Infective Agent,Anti Infective Agents,Anti Microbial Agent,Anti Microbial Agents
D054804	Cathelicidins	Antimicrobial cationic peptides with a highly conserved amino terminal cathelin-like domain and a more variable carboxy terminal domain. They are initially synthesized as preproproteins and then cleaved. They are expressed in many tissues of humans and localized to EPITHELIAL CELLS. They kill nonviral pathogens by forming pores in membranes.	ALL-38 Peptide,Antibacterial Peptide LL-37,Antimicrobial Peptide LL-37,Bac4 Protein, Bos taurus,CAP18 Lipopolysaccharide-Binding Protein,CATH-1 Protein,Cathelicidin,Cathelicidin 1,Cathelicidin Antimicrobial Peptide,Cathelicidin LL-37,Cathelicidin-1,Cathelin-Like Protein,Cathelin-Related Antimicrobial Peptide,LL-37 Antibacterial Peptide,LL-37 Peptide,Myeloid Cathelicidin 1 Protein, Equus caballus,Ropocamptide,eCATH-1,hCAP-18,CAP-18,CAP18,FA-LL-37,K9CATH,eCATH-1 protein, Equus caballus,ALL 38 Peptide,Antibacterial Peptide LL 37,Antibacterial Peptide, LL-37,Antimicrobial Peptide LL 37,Antimicrobial Peptide, Cathelin-Related,CAP 18,CAP18 Lipopolysaccharide Binding Protein,CATH 1 Protein,Cathelicidin LL 37,FA LL 37,LL 37 Antibacterial Peptide,LL 37 Peptide,LL-37, Antibacterial Peptide,LL-37, Antimicrobial Peptide,LL-37, Cathelicidin,Lipopolysaccharide-Binding Protein, CAP18,Peptide LL-37, Antibacterial,Peptide LL-37, Antimicrobial,Peptide, ALL-38,Peptide, Cathelin-Related Antimicrobial,Peptide, LL-37,Peptide, LL-37 Antibacterial,Protein, CAP18 Lipopolysaccharide-Binding,Protein, CATH-1,Protein, Cathelin-Like,eCATH 1,eCATH 1 protein, Equus caballus,hCAP 18