Structure, function and biological properties of integrin alpha v beta 3 on human melanoma cells.
Human melanoma represents one of the most metastatic cancers in man. The capacity of melanoma cells to invade a variety of tissues and extracellular matrices is, in part, due to their repertoire of adhesion receptors. To this end, human melanoma cells express multiple integrin cell adhesion receptors among these is the vitronectin receptor, alpha v beta 3. This adhesion receptor enables melanoma cells to attach to a wide variety of extracellular matrix components containing the sequence Arg-Gly-Asp. This review will focus on the biosynthetic, biochemical and biological properties of this receptor expressed on the surface of human melanoma cells.
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Research Institute of Scripps Clinic, Dept. of Immunology, LaJolla, CA 92037.
D000595:Amino Acid Sequence; D002448:Cell Adhesion; D005732:Gangliosides / Q000502:physiology; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D008545:Melanoma / Q000378:metabolism / Q000473:pathology*; D008969:Molecular Sequence Data; D009361:Neoplasm Invasiveness; D011971:Receptors, Immunologic / Q000096:biosynthesis / Q000502:physiology*; D019030:Receptors, Vitronectin
D005732:Gangliosides; D011971:Receptors, Immunologic; D019030:Receptors, Vitronectin; C026226:ganglioside, GD3; C019403:ganglioside, GD2