Journal
JOURNAL OF CELLULAR AND MOLECULAR MEDICINE
Volume 9, Issue 2, Pages 255-266Publisher
WILEY
DOI: 10.1111/j.1582-4934.2005.tb00354.x
Keywords
L-selectin; ectodomain shedding; cell adhesion molecules; leukocytes; TACE
Categories
Funding
- NIBIB NIH HHS [R01EB002185] Funding Source: Medline
Ask authors/readers for more resources
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 JACE) 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available