title: Spermine specifically inhibits the phosphorylation of an 11,000-dalton nuclear protein in various cultured mammalian cell lines.
abstract: The effect of polyamines (putrescine, spermidine and spermine) on endogenous protein phosphorylation in mouse neuroblastoma cells was investigated by using techniques of sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. The results indicated that spermine at 1mM completely inhibited the phosphorylation of the 11,000-dalton and 120,000-dalton proteins in nuclear fractions. The inhibition of the phosphorylation of the 11,000-dalton but not the 120,000-dalton protein by spermine was also observed in five other cell lines examined and appeared to be a general phenomenon. The inhibitory effect of spermine on the phosphorylation of the 11,000-dalton protein was specific, other cations such as ammonium chloride, arginine, putrescine, cyclen and trien were ineffective at equal molar or much higher concentrations.
mesh_terms: D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000187:drug effects / Q000378:metabolism*; D051379:Mice; D008970:Molecular Weight; D009374:Neoplasms, Experimental / Q000378:metabolism; D009447:Neuroblastoma / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011073:Polyamines / Q000494:pharmacology; D051381:Rats; D013096:Spermine / Q000494:pharmacology*
chemical_list: D010750:Phosphoproteins; D011073:Polyamines; D013096:Spermine