A cyclic adenosine 3':5'-monophosphate-mediated effect of cholera toxin on high-molecular-weight glycoprotein species of malignant cells.
A comparison of the Pronase-sensitive glycosylated species detectable under permissive and nonpermissive conditions by normal rat kidney cells transformed by a temperature-sensitive derivative of Rous sarcoma virus reveals relative decreased labeling of high-molecular-weight glycosylated species under conditions that allow the expression of transformation, in medium supplemented either with 0.5% calf serum or with human alpha2-macroglobulin, 100 mug/ml. Exposure of the cultures to cholera toxin or dibutyryl cyclic adenosine 3':5'-monophosphate leads to a relative increase in the glycosylation of the high-molecular weight species in both wild-type transformed and temperature-sensitive cells exposed to conditions that allow the expression of transformation.
D000818:Animals; D003994:Bucladesine / Q000494:pharmacology*; D002460:Cell Line; D002471:Cell Transformation, Neoplastic; D006023:Glycoproteins / Q000096:biosynthesis*; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000096:biosynthesis*; D001357:Sarcoma, Avian / Q000378:metabolism*; D013696:Temperature; D014118:Toxins, Biological / Q000494:pharmacology*; D014734:Vibrio cholerae / Q000276:immunology*
D006023:Glycoproteins; D009363:Neoplasm Proteins; D014118:Toxins, Biological; D003994:Bucladesine