A melanoma cell surface laminin binding protein with apparent Mr 90,000.
Laminin promotes adhesion of various cell types via multiple interactions with cell surface components. We have used a laminin domain involved in adhesion of melanoma cells, peptide F9 (Charonis et al., J. Cell Biol. 107:1253 [( 1988]), to examine its specific interaction with cell surface components. Cells were surface labeled, solubilized, and the cell surface associated macromolecules were purified via laminin and F9 affinity columns. We have observed that a macromolecule with apparent molecular weight 90,000 interacts with laminin and peptide F9. This macromolecule does not change electrophoretic mobility upon reduction, cannot be removed from the cell surface by high salt treatment and partitions in the detergent phase of Triton X-114. These results suggest that this macromolecule is associated with melanoma cell surfaces and may be involved in their interaction with laminin.
Koliakos
G G
GG
Department of Laboratory Medicine and Pathology, UMHC, Minneapolis 55455.
Tsilibary
E C
EC
Charonis
A S
AS
D000818:Animals; D004586:Electrophoresis; D007797:Laminin / Q000302:isolation & purification / Q000378:metabolism; D008545:Melanoma / Q000378:metabolism* / Q000473:pathology; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism; D011971:Receptors, Immunologic / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D017474:Receptors, Laminin
D007797:Laminin; D010446:Peptide Fragments; D011971:Receptors, Immunologic; D017474:Receptors, Laminin; C066529:laminin F9