CDB25:0003279 CD24 — L1CAM
Experimentally validated in Mouse; Orthology-inferred in Human, Rat, Chicken, Macaque, Pig, Dog, Cow, Chimp, Horse, Marmoset, Sheep
Title
Journal:; Year Published:
Abstract
The neural recognition molecule L1 is a sialic acid-binding lectin for CD24, which induces promotion and inhibition of neurite outgrowth.
The Journal of biological chemistry, 2001; PubMed, Mus Musculus Cd24a — Mus Musculus L1cam
ABSTRACT: Among the recognition molecules that determine a neuron's interaction with other cells, L1 and CD24 have been suggested to cooperate with each other in neurite outgrowth and signal transduction. Here we report that binding of CD24 to L1 depends on alpha2,3-sialic acid on CD24, which determines the CD24 induced and cell type-specific promotion or inhibition of neurite outgrowth. Using knockout mutants, we could show that the CD24-induced effects on neurite outgrowth are mediated via L1, and not GPI-linked CD24, by trans-interaction of L1 with sialylated CD24. This glycoform is excluded together with L1 from raft microdomains, suggesting that molecular compartmentation in the surface membrane could play a role in signal transduction.
Heat-stable antigen (mouse CD24) in the brain: dual but distinct interaction with P-selectin and L1.
Biochimica et biophysica acta, 1997; PubMed, Mus Musculus Cd24a — Mus Musculus L1cam
ABSTRACT: Heat-stable antigen (HSA/mouse CD24) is expressed in both haematopoietic and neural cells. The small core protein of the molecule is extensively glycosylated and anchored to the membrane via glycosylphosphatidylinositol. The role of HSA in the developing brain as well as its functional properties are poorly understood. Here we show that the brain HSA is associated with N- and O-linked oligosaccharide moieties and decorated with the HNK-1 sulfated carbohydrate epitope. It can bind P-selectin but not E-selectin and this interaction requires divalent cations and is sensitive to high salt. Brain derived HSA is also capable of binding to the L1 adhesion molecule. This interaction is distinct from the P-selectin binding as it is resistant to high salt and does not require bivalent cations. Treatment of HSA with OSGE significantly reduced binding of both P-selectin and I.1. Our data suggest that HSA can bind P-selectin and I.1 by distinct mechanism and that the binding epitopes on HSA are in close proximity.