Spermine specifically inhibits the phosphorylation of an 11,000-dalton nuclear protein in various cultured mammalian cell lines |
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Authors: | Kuang Yu Chen Rati Verma |
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Institution: | 1. Department of Chemistry Rutgers - The State University of New Jersey New Brunswick, New Jersey 08903, U.S.A.;2. Department of Biochemistry Rutgers - The State University of New Jersey New Brunswick, New Jersey 08903, U.S.A. |
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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. |
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