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Langerin, a novel C-type lectin specific to Langerhans cells, is an endocytic receptor that induces the formation of Birbeck granules.
Langerin is a potent inducer of membrane superimposition and zippering leading to BG formation and the data suggest that induction of BG is a consequence of the antigen-capture function of Langerin, allowing routing into these organelles and providing access to a nonclassical antigen-processing pathway. Expand
P-selectin glycoprotein ligand-1 mediates rolling of human neutrophils on P-selectin
Data indicate thatPSGL-1 accounts for the high affinity binding sites for P-selectin on leukocytes, and PSGL- 1 must interact with P- Selectin in order for neutrophils to roll on P- selectin at physiological shear stresses. Expand
Activated platelets signal chemokine synthesis by human monocytes.
Thrombin-activated platelets induce the expression and secretion of monocyte chemotactic protein-1 and IL-8 by monocytes and provide a model for the study of gene regulation in cell-cell interactions, suggesting that activated platelets regulate chemokine secretion by monocyte in inflammatory lesions in vivo. Expand
Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells
The preferential interaction of the ligand with P-selectin suggests that it may play a role in adhesion of myeloid cells to activated platelets and endothelial cells. Expand
GMP-140, a platelet alpha-granule membrane protein, is also synthesized by vascular endothelial cells and is localized in Weibel-Palade bodies.
The restricted expression of GMP-140 in secretory granules of platelets and endothelium suggests that it has a specific function in the vascular system rather than a general role related to inducible secretion. Expand
Neutrophils use both shared and distinct mechanisms to adhere to selectins under static and flow conditions.
It is suggested that PSGL-1 functions cooperatively with L-selectin to mediate optimal attachment of flowing neutrophils to E- selectin but not to P-selecting, perhaps because of the higher affinity of P- Selectin for the PL1-defined site on PS GL-1. Expand
Neutrophil-neutrophil interactions under hydrodynamic shear stress involve L-selectin and PSGL-1. A mechanism that amplifies initial leukocyte accumulation of P-selectin in vitro.
It is shown that purified neutrophil PSGL-1, a sialomucin glycoprotein that serves as a ligand for both P- and E-selectin, can also support the attachment and rolling of free flowing neutrophils in vitro and may play an important role in amplifying the rate of initial leukocyte recruitment at sites of inflammation. Expand
The Biology and Enzymology of Protein Tyrosine O-Sulfation*
  • K. Moore
  • Biology, Medicine
  • Journal of Biological Chemistry
  • 4 July 2003
The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine.
It is demonstrated that the polypeptide component of this ligand is identical to that of P-selectin glycoprotein ligand-1 (PSGL-1), a molecule recently identified by expression cloning from a human myeloid cell cDNA library. Expand
L-selectin binds to P-selectin glycoprotein ligand-1 on leukocytes: interactions between the lectin, epidermal growth factor, and consensus repeat domains of the selectins determine ligand binding
L-selectin was shown to bind leukocytes through the P- selectin ligand, PSGL-1, although at lower levels than P-select in this study, and may mediate neutrophil rolling on stationary leukocyte bound to cytokine-induced endothelial cells, which was previously reported to be a L- Selectin-dependent process. Expand