L-selectin: mechanisms and physiological significance of ectodomain cleavage.

D. M. Smalley, K. Ley

Research output: Contribution to journalReview articlepeer-review

186 Scopus citations

Abstract

L-selectin is a cell adhesion molecule consisting of a large, highly glycosylated, extracellular domain, a single spanning transmembrane domain and a small cytoplasmic tail. It is expressed on most leukocytes and is involved in their rolling on inflamed vascular endothelium prior to firm adhesion and transmigration. It is also required for the constitutive trafficking of lymphocytes through secondary lymphoid organs. Like most adhesion molecules, L-selectin function is regulated by a variety of mechanisms including gene transcription, post-translational modifications, association with the actin cytoskeleton, and topographic distribution. In addition, it is rapidly downregulated by proteolytic cleavage near the cell surface by ADAM-17 (TACE) and at least one other "sheddase". This process of "ectodomain shedding" results in the release of most of the extracellular portion of L-selectin from the cell surface while retaining the cytoplasmic, transmembrane, and eleven amino acids of the extracellular domain on the cell. This review will examine the mechanism(s) of L-selectin ectodomain shedding and discuss the physiological implications.

Original languageEnglish (US)
Pages (from-to)255-266
Number of pages12
JournalJournal of Cellular and Molecular Medicine
Volume9
Issue number2
DOIs
StatePublished - 2005
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Medicine
  • Cell Biology

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