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Part of the book series: Results and Problems in Cell Differentiation ((RESULTS,volume 33))

Abstract

The selectins encompass a family of three type I transmembrane glycoproteins exclusively expressed on blood cells and vascular cells. All known functions of the selectins require the N-terminal C-type lectin domain. The lectin domains show the highest degree of homology among different species (about 72% identity) and considerable homology among the three selectins within the same species (about 52% for human selectins; Kansas 1996). All three selectins strictly require the presence of free calcium ions for ligand binding, and incubation with a chelator eliminates all selectin binding. One EGF domain follows the lectin domain, and two or more short consensus repeats are between the EGF domain and the transmembrane domain. Each domain is encoded by a separate exon, except the cytoplasmic domain, which is encoded by two exons. Complementary DNAs for all three selectins were cloned in 1989 (Bevilacqua et al. 1989; Camerini et al. 1989; Johnston et al. 1989; Siegelman et al. 1989; Tedder et al. 1989), and no new selectins have been found in the past 10 years, suggesting that this protein family consists of only three members.

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Ley, K. (2001). Functions of Selectins. In: Crocker, P.R. (eds) Mammalian Carbohydrate Recognition Systems. Results and Problems in Cell Differentiation, vol 33. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-46410-5_10

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