Pleiotropic Signaling Functions Of L-Selectin

Signaling functions of L-selectin in neutrophils: alterations in the cytoskeleton and colocalization with CD18.

Ligation and clustering of L-selectin by Ab ("cross-linking") or physiologic ligands results in activation of diverse responses that favor enhanced microvascular sequestration and emigration of neutrophils. The earliest responses include a rise in intracellular calcium, enhanced tyrosine phosphorylation, and activation of extracellular signal-regulated kinases. Additionally, cross-linking of L-...

The Pleiotropic Functions of Interleukin 15

Since its discovery in 1994, IL-15 has been studied in the context of its structural cousin, IL-2 (1). Early biochemical and in vitro lymphocyte studies revealed many similarities between IL-15 and IL-2: (a) IL-2 and IL-15 constitute the only two members of a family of cytokines containing a four a helix bundle; (b) the heterotrimeric receptors for IL-2 and IL-15 share both the IL-2/15R b and I...

The cytoplasmic domain of L-selectin participates in regulating L-selectin endoproteolysis.

Neutrophil recruitment at sites of inflammation is regulated by a series of adhesion and activation events. L-selectin (CD62L) is a leukocyte expressed adhesion protein that is important for neutrophil accumulation and rolling along the vascular endothelium. L-selectin is unique from other adhesion molecules involved in leukocyte transmigration in that its adhesiveness appears to be regulated p...

Homing in on L-selectin.

Activation-Independent L-Selectin Shedding Shedding: Phenylarsine Oxide Promotes Sulfhydryl Regulation of L-Selectin