Lectin—Carbohydrate Binding as a Model for Platelet Contact Interactions
Lectins have been defined as sugar-binding proteins or glycoproteins of nonimmune origin that can agglutinate cells and/or glycoconjugates (Goldstein et al., 1980). Lectins occur in plants and animals, and are devoid of enzymatic activity for the sugars to which they bind and do not require glycosidic hydroxyl groups on these sugars for their binding (Kocoureck and Horejsi, 1981; Barondes, 1981). One of the functions suggested for lectins is that of mediating direct cell—cell interactions (reviewed in Phillips and Gartner, 1980; Barondes, 1981). The first data suggesting this functional activity was published by Rosen et al. (1973), who showed that a lectin expressed by the cellular slime mold Dictyostelium discoideum may mediate the cohesiveness of these cells. Since these initial studies, numerous studies have appeared concerning the role of carbohydrate-binding proteins in aggregation of slime mold cells (reviewed in Bartles et al., 1982; Barondes, 1981). The concept developed from these studies is that lectins, bound to carbohydrate-containing receptors on adjacent cells, mediate cell—cell interaction. This concept has been utilized to explain the interactions of a wide variety of cells, including sea urchin egg-sperm interactions (Glabe et al., 1982), the attachment of Rhizobium trifolii to the roots of clover (Dazzo, 1981), attachment of Escherichia coli to mucosal cells (Ofek et al, 1977), the attachment of the Sendai virus to host cells (Markwellet al., 1981), and phagocytosis by human neutrophils (Doolittle et al, 1983).
KeywordsHuman Platelet Amino Sugar Slime Mold Hemagglutination Activity Lectin Activity
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