Lactosylceramide-associated receptor complex (LacCer-Lyn complex)

Lactosylceramide (LacCer) is a glycosphingolipid that organizes into specialized membrane microdomains or lipid rafts on the surface of various cells, most notably human neutrophils (Iwabuchi K, et al., 2015, PMID: 25852701). These Lactosylceramide-associated receptor complexes typically involve the physical and functional coupling of LacCer with Src-family kinases, particularly Lyn, and alpha-subunits of heterotrimeric G proteins (Nakayama H, et al., 2018, PMID: 30146245). These complexes function as pattern recognition receptors (PRRs) that detect microbial components such as beta-glucans and lipopolysaccharides, triggering essential innate immune responses including chemotaxis, phagocytosis, and the respiratory burst (Iwabuchi K, et al., 1998, PMID: 9707581). Beyond immunology, LacCer-enriched microdomains play roles in cell proliferation, adhesion, and angiogenesis, making them relevant in the study of atherosclerosis and cancer progression (Kolmakova A, et al., 2009, PMID: 19406603). Therapeutic strategies targeting these complexes often focus on disrupting the assembly of the microdomain or inhibiting the downstream signaling kinases to manage inflammatory and infectious diseases. The complex is also involved in the pathogenesis of certain metabolic disorders where glycosphingolipid accumulation occurs. Research into these complexes highlights the importance of lipid-protein interactions in membrane-mediated signaling events.

Other names

Lactosylceramide-enriched membrane microdomainLacCer-Lyn signaling moduleCDw17-associated signaling complexLactosylceramide-G-protein complex

Inhibition of glycosphingolipid biosynthesis or direct antibody-mediated neutralization of the Lactosylceramide-enriched microdomain to prevent ligand binding and downstream kinase activation.