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Overview
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CD62L (L-selectin), binds a 95 kDa (on neutrophils) or 74 kDa (on lymph ocytes) receptor with lectin-like and Epidermal Growth Factor-like domains. In the mouse, L-selectin is detected on most thymocytes, with the highest levels of expression on an immunocompetent subset and a population of dividing progenitor cells, and on peripheral leukocytes, including subsets of B and T lymph ocytes, neutrophils, monocytes, and eosinophils. This member of the selectin adhesion molecule family appears to be required for lymph ocyte homing to peripheral lymph nodes and to contribute to neutrophil emigration at inflammatory sites. L-selectin is rapidly shed from lymph ocytes and neutrophils upon cellular activation; metalloproteinases may mediate the release of CD62L ectodomains from the cell surface. The level of CD62L expression, along with other markers, distinguishes naive, effector, and memory T cells. L-selectin binds to sialytaed oligosaccharide determinants on high endothelial venules (HEV) in peripheral lymph nodes. In vitro studies have demonstrated that CD34, GlyCAM-1, and MAdCAM-1, all recognized by mAb MECA-79 (anti-mouse PNAd Carbohydrate Epitope, may be ligands for CD62L. MEL-14 mAb blocks in vitro binding of lymph ocytes to peripheral lymph node HEV and inhibits in vivo lymph ocyte extravasation into peripheral lymph nodes and late stages of leukocyte rolling.
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