Synthetic Glycoprotein Mimics Inhibit L-Selectin-Mediated Rolling and Promote L-Selectin Shedding [PDF]
Chemistry & Biology, 2004 L-selectin is a leukocyte cell-surface protein that facilitates the rolling of leukocytes along the endothelium, a process that leads to leukocyte migration to a site of infection. Preventing L-selectin-mediated rolling minimizes leukocyte adhesion and extravasation; therefore, compounds that inhibit rolling may act as anti-inflammatory agents.
Mowery, Patricia +6 more
openaire +3 more sources
P-selectin glycoprotein ligand-1 forms dimeric interactions with E-selectin but monomeric interactions with L-selectin on cell surfaces. [PDF]
PLoS ONE, 2013 Interactions of selectins with cell surface glycoconjugates mediate the first step of the adhesion and signaling cascade that recruits circulating leukocytes to sites of infection or injury.
Yan Zhang +5 more
doaj +1 more source
Calmodulin adopts an extended conformation when interacting with L-selectin in membranes. [PDF]
PLoS ONE, 2013 Calmodulin, an intracellular calcium-binding protein, is thought to regulate ectodomain shedding of many membrane proteins, but the underlying molecular mechanism has remained unclear.
Wei Deng, John A Putkey, Renhao Li
doaj +1 more source
The Cytoplasmic Domain of L-Selectin Participates in Regulating L-Selectin Endoproteolysis [PDF]
The Journal of Immunology, 2001 Abstract 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.
E, Matala +3 more
openaire +2 more sources
Transcriptional regulation of mouse l-selectin [PDF]
Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 2009 L-selectin mediates the initial tethering and rolling of lymphocytes in high endothelial venules. To study the transcriptional regulation of mouse L-selectin, we cloned 4.5 kb 5'-flanking sequences of the mouse sell. Luciferase analysis of serial 5'-deletion mutants showed that the first 285 bp was sufficient to drive high promoter activity in EL4 ...
Xitong, Dang +2 more
openaire +2 more sources
L-Selectin Shedding Regulates Leukocyte Recruitment [PDF]
The Journal of Experimental Medicine, 2001 The physiologic role of L-selectin shedding is unknown. Here, we investigate the effect of L-selectin shedding on firm adhesion and transmigration. In a tumor necrosis factor α–induced model of inflammation, inhibition of L-selectin shedding significantly increased firm adhesion and transmigration by a lymphocyte function–associated antigen (LFA)-1 and
A, Hafezi-Moghadam +4 more
openaire +2 more sources
Evaluation of L-selectin expression and assessment of protein tyrosine phosphorylation in bovine polymorphonuclear neutrophil leukocytes around parturition. [PDF]
, 2002 Impaired polymorphonuclear neutrophil leukocyte (PMN) function around parturition has been associated with increased clinical mastitis in dairy cows. Rolling and attachment of PMN to the endothelium is the first step in the recruitment process and is ...
Burvenich, Christian +6 more
core +1 more source
Frontiers in Medicine, 2020 Selectins [endothelial (E), platelet (P), and leucocytes (L)] are a class of cell adhesion molecules, stimulated in response to inflammation. Pre-eclampsia is characterized by inflammation, and angiotensin II is pro-inflammatory.
Hiten D. Mistry +5 more
doaj +1 more source
Sulfation-dependent recognition of high endothelial venules (HEV)-ligands by L-selectin and MECA 79, and adhesion-blocking monoclonal antibody. [PDF]
, 1994 L-selectin is a lectin-like receptor that mediates the attachment of lymphocytes to high endothelial venules (HEV) of lymph nodes during the process of lymphocyte recirculation.
Butcher, EC, Hemmerich, S, Rosen, SD
core +2 more sources
Human T cell glycosylation and implications on immune therapy for cancer [PDF]
, 2020 Glycosylation is an important post-translational modification, giving rise to a diverse and abundant repertoire of glycans on the cell surface, collectively known as the glycome.
Callewaert, Nico +3 more
core +1 more source