Abstract
Recent understanding of cell adhesion mechanisms has been greatly enhanced by the elucidation of the integrin superfamily of cell adhesion molecules (1). These adhesion receptors include at least 11 different cell-matrix and cell-cell adhesion receptor heterodimers with major structural similarities (Table 2.1). They are subdivided into three families known as (i) VLA proteins (2,3), (ii) cytoadhesins (4), and (iii) LFA-1, Mac-1, p150,95 proteins (5). Among these receptors, the a subunits of a fibro-nectin receptor (VLA-5) (6,7), vitronectin receptor (8), platelet gpIIa (7,9), Mac-1 (10–12), and p150,95 (13) have been sequenced and show 20 to 60% conservation of amino acids, consistent with their structural relatedness.
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Hemler, M.E., Takada, Y., Elices, M., Crouse, C. (1990). Structure and Functions for the Adhesion Receptors VLA-2 and VLA-4: Comparisons to other Members of the Integrin Superfamily. In: Springer, T.A., Anderson, D.C., Rothlein, R., Rosenthal, A.S. (eds) Leukocyte Adhesion Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3234-6_3
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DOI: https://doi.org/10.1007/978-1-4612-3234-6_3
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