Overview
- Le, Y. et al. (1999) J. Immunol. 163, 6777.
- Christophe, T. et al. (2001) J. Biol. Chem. 276, 21585.
Alomone Labs WKYMVm activates Ca2+ transients in HL-60 cells.Non-differentiated HL-60 cells were loaded with Fluo-3 AM. Changes in intracellular Ca2+ were detected via changes in Fluo-3 emission following application of WKYMVm (#GPW-105) at different concentrations. Normalized fluorescence before and after application (indicated by arrow) of 1 nM, 10 nM and 100 nM WKYMVm are shown compared to control (black).
Chemotactic factors from both Gram-positive and Gram-negative bacteria are short peptides with N-formyl methionine at the N-terminus (extensively reviewed in reference 1). These peptides are released from bacteria during infection and activate formyl peptide receptors (FPR), members of the G-protein coupled receptor (GPCR) superfamily. In humans, the FPR family consists mainly of three receptors, FPR1, FPR2/ALX (formerly FPRL1), and FPR3 (formerly FPRL2) which all couple to the Gi subtype of G-proteins and ultimately lead to the activation of phospholipase C and intracellular Ca2+ increase1,2.
WKYMVm is a selective agonist of the Formyl peptide receptors (FPR2 and FPR3) and was discovered by screening peptide libraries for their ability to stimulate inositol phosphates in lymphocyte cell lines3,4. It is also an agonist of FPR11. FPR2 is expressed in the promyelocytic leukemia cell line HL-60 as well as in the chronic myelogenous leukemia cell line K5625.
WKYMVm inhibited the infection of human peripheral monocyte–derived macrophages and CD41 T lymphocytes by strains of HIV-1, via sensitization of chemokine receptors (CXCR4 and CCR5), following FPR2 activation6.
FPR2, FPR3 receptors
