Results 211 to 220 of about 44,172 (240)
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The telling tail of L-selectin

Biochemical Society Transactions, 2004
L-selectin is constitutively expressed on the surface of most leucocytes and is important for tethering and subsequent rolling of leucocytes on endothelial cells, facilitating their migration into secondary lymphoid organs (e.g. naive T cells) and sites of inflammation (e.g. neutrophils).
A, Ivetic, A J, Ridley
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Elevated serum L-selectin levels and abnormal regulation of L-selectin expression on leukocytes in atopic dermatitis: Soluble L-selectin levels indicate disease severity

Journal of Allergy and Clinical Immunology, 1999
L-selectin mediates leukocyte rolling on endothelium at sites of inflammation, suggesting that L-selectin may be involved in the development of cutaneous lesions of atopic dermatitis (AD). After leukocyte activation, L-selectin is rapidly shed from the cell surface.The purpose of this study was to assess leukocyte L-selectin expression and quantitate ...
Y, Shimada   +4 more
openaire   +2 more sources

Adrenaline upregulates monocyte L-selectin in vitro

Resuscitation, 1999
Although surface adhesion molecules mediate leucocyte-endothelial interactions at sites of inflammation, relatively little is known of the factors which increase the expression of L-selectin in circulating leucocytes. The expression of leucocyte L-selectin increases during acute stress events such as injury and is temporally related to an early ...
T H, Rainer, N, Lam, R A, Cocks
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The L-selectin adhesion system

Current Opinion in Hematology, 1995
L-selectin is a cell surface glycoprotein expressed on most leukocyte subsets that mediates leukocyte interaction with ligands on lymphoid tissue high endothelial venule cells as well as with ligands on activated endothelium at sites of inflammation in nonlymphoid organs.
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CD45 Engagement Induces L‐Selectin Down‐Regulation

Scandinavian Journal of Immunology, 1996
The CD45 glycoprotein isoforms exhibit a receptor‐like composition and display intracellular protein tyrosine phosphatase (PTPase) activity. The present study links CD45 to the regulation of L‐selectin (CD62L), a leucocyte glycoprotein important for extravasation and homotypic aggregation.
D, Stibenz   +3 more
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L-selectin in health and disease

Resuscitation, 2002
This article reviews recent advances in the knowledge of the role of L-selectin, an adhesion molecule that is expressed on the surface of circulating leucocytes, in animal and human physiology and pathophysiology. After a brief discussion on nomenclature and structure, it progresses through the evidence for expression and regulation of L-selectin, cell
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Cytoskeletal interactions regulate inducible L-selectin clustering

American Journal of Physiology-Cell Physiology, 2005
L-selectin (CD62L) amplifies neutrophil capture within the microvasculature at sites of inflammation. Activation by G protein-coupled stimuli or through ligation of L-selectin promotes clustering of L-selectin and serves to increase its adhesiveness, signaling, and colocalization with β2-integrins.
Polly E, Mattila   +4 more
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L-selectin

Experimental and Toxicologic Pathology, 2005
The leucocyte expressed surface-bound L-selectin belongs to the selectin family of adhesion molecules. It exhibits adhesive as well as signalling functions. Mainly, it is of importance in lymphocyte homing and in the extravasation of leucocytes into the surrounding tissue during inflammation.
Barkhausen, T   +2 more
openaire   +1 more source

Cleaved L-selectin concentrations in meningeal leukaemia

The Lancet, 1995
Involvement of the central nervous system has important therapeutic implications in acute leukaemia. Because the identification of blast cells in cerebrospinal fluid (CSF) is often difficult, there is a need for sensitive markers of leukaemic infiltration.
A, Stucki   +5 more
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Structure and function of L‐selectin

APMIS, 1992
The selectins are a newly described family of carbohydrate‐binding adhesion molecules involved in the regulation of leukocyte traffic. Selectins are composed of an N‐terminal C‐type lectin domain, a single EGF domain, a variable number of short concensus repeat (SCR) domains, a transmembrane region and a cytoplasmic tail.
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