L-selectin
L-selectin is a type of adhesion molecule that is important in the immune system. It is a type of selectin, which are proteins that bind to carbohydrates on the surfaces of cells. L-selectin is found on the surface of white blood cells and helps them to move to sites of inflammation or injury.
Structure[edit | edit source]
L-selectin is a single-chain glycoprotein that is approximately 74-95 kDa in size. It is composed of a large, extracellular domain, a single transmembrane domain, and a short cytoplasmic tail. The extracellular domain contains a C-type lectin domain, an EGF-like domain, and two complement control protein modules.
Function[edit | edit source]
The primary function of L-selectin is to mediate the adhesion of circulating leukocytes to endothelial cells in the blood vessels. This is a crucial step in the immune response, as it allows the leukocytes to exit the bloodstream and enter the tissues where they can fight infection or repair damage. L-selectin binds to specific carbohydrate structures on the endothelial cells, which triggers a process known as rolling adhesion. This is a type of weak, transient adhesion that allows the leukocytes to roll along the inner surface of the blood vessel until they reach the site of inflammation or injury.
Clinical significance[edit | edit source]
Alterations in L-selectin function or expression can have significant clinical implications. For example, elevated levels of soluble L-selectin have been associated with various inflammatory conditions, including rheumatoid arthritis, systemic lupus erythematosus, and inflammatory bowel disease. In addition, L-selectin has been implicated in the pathogenesis of certain types of cancer, as it may facilitate the metastasis of cancer cells to distant sites in the body.
See also[edit | edit source]
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