The apparent inducibility of tumour marker glycoproteins in a melanoma cell line selected for growth in low levels of glucose.
It has been reported previously that malignancy in hybrid cells is associated with changes in two glycoproteins of molecular mass 90,000 and 100,000. In the current paper the characteristics of a clonal derivation of a murine melanoma cell line (PG19G-), selected for growth in low levels of glucose, are described. The cells had considerably reduced amounts of the 90 K and 100 K glycoproteins as judged by lectin affinity-labelling. When the level of glucose in the medium is raised the two glycoproteins become detectable after a few hours. This inducibility is specific for D-glucose and D-mannose at concentrations in excess of 300 mg/l and is inhibited by cytochalasin B but not by cytochalasin A. The 90 K glycoprotein differs from the 100 K in that its level varies with the glucose concentration even in the parent cell line PG19 and in other tumour lines. This is not the case for the 100 K glycoprotein, the synthesis and/or glycosylation of these two glycoproteins are, therefore, governed by separate control mechanisms. The relationship of the glucose-sensitive proteins to the glucose transporter is discussed.
D000818:Animals; D002460:Cell Line; D005947:Glucose / Q000378:metabolism*; D006023:Glycoproteins / Q000096:biosynthesis*; D008545:Melanoma / Q000378:metabolism*; D051379:Mice; D008810:Mice, Inbred C57BL; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000096:biosynthesis*; D009374:Neoplasms, Experimental / Q000378:metabolism; D014212:Tretinoin / Q000494:pharmacology
D006023:Glycoproteins; D009363:Neoplasm Proteins; D014212:Tretinoin; D005947:Glucose