CELL ADHESION PROTEIN RECEPTORS
\sˈɛl ɐdhˈiːʒən pɹˈə͡ʊtiːn ɹɪsˈɛptəz], \sˈɛl ɐdhˈiːʒən pɹˈəʊtiːn ɹɪsˈɛptəz], \s_ˈɛ_l ɐ_d_h_ˈiː_ʒ_ə_n p_ɹ_ˈəʊ_t_iː_n ɹ_ɪ_s_ˈɛ_p_t_ə_z]\
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A family of transmembrane glycoproteins consisting of noncovalent heterodimers. They interact with a wide variety of ligands including extracellular matrix glycoproteins, complement, and other cells, while their intracellular domains interact with the cytoskeleton. The integrins consist of at least three identified families: the cytoadhesin receptors, the leukocyte adhesion receptors, and the very-late-antigen receptors. Each family contains a common beta-subunit combined with one or more distinct alpha-subunits. These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development, hemostasis, thrombosis, wound healing, immune and nonimmune defense mechanisms, and oncogenic transformation.
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Proto Oncogene Proteins c erbB 2
- cell surface protein-tyrosine kinase that is found to be overexpressed in significant number adenocarcinomas. It has extensive homology can heterodimerize EGF EPIDERMAL GROWTH FACTOR), 3 receptor (RECEPTOR, 3) and the 4 receptor. Activation of erbB-2 receptor occurs during heterodimer formation with a ligand-bound erbB family members. EC 2.7.11.-.