Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

The effect of secretagogues on protein carboxyl methylation in the rat brain

Thesis/Dissertation ·
OSTI ID:5406602
The influence of various substrates which are known to alter free intracellular calcium concentrations on protein carboxyl methyltransferase (PCM) activity was investigated in rat brain synaptosomes. The synaptosomes were labeled with ({sup 3}H)-L-methionine and the {sup 3}H-methyl esters of proteins were formed from the methyl donor ({sup 3}H)-S-adenosyl-L-methionine (({sup 3}H)-AdoMet). The calcium ionophore A23187 and ouabain decreased PCM activity and the decrease produced by A23187 was antagonized by ethylene glycol bis({beta}-aminoethyl ether)-N,N{prime}-tetraacetic acid (EGTA) and MnCl{sub 2}. On the other hand, ruthenium red, an inhibitor of calcium uptake, stimulated PCM activity. These data suggest that PCM activity is inversely related to the free cytoplasmic calcium concentration. Veratridine, A23187 and elevated potassium ions decreased the levels of ATP and ({sup 3}H)-AdoMet. The A23187-mediated decrease in ATP levels and the reduced ({sup 3}H)-AdoMet formation was antagonized by EGTA and MnCl{sub 2}. Inhibition of metabolic activity of the synaptosomes by NaCN led to: (1) decreased ATP levels; (2) inhibition of ({sup 3}H)-AdoMet formation; and (3) inhibition of PCM activity. Four endogenously methylated proteins were isolated from synaptosomes by acidic gel electrophoresis.
Research Organization:
Kansas State Univ., Manhattan, KS (USA)
OSTI ID:
5406602
Country of Publication:
United States
Language:
English