scholarly journals The developmental pattern of homologous and heterologous tRNA methylation in rat brain differential effect of spermidine

1976 ◽  
Vol 1 (4) ◽  
pp. 369-384 ◽  
Author(s):  
C. E. Salas ◽  
C. J. Cummins ◽  
O. Z. Sellinger
1977 ◽  
Vol 166 (3) ◽  
pp. 421-428 ◽  
Author(s):  
Joanne Pieringer ◽  
G. Subba Rao ◽  
Paul Mandel ◽  
Ronald A. Pieringer

The sulphogalactosylglycerolipid of rat brain is closely associated with the process of myelination, as demonstrated by the following observations. 1. The lipid is barely detectable in rat brain before 10 days of age, accumulates rapidly between age 10 and 25 days, and remains relatively constant in amount (between 0.3 and 0.4μmol per brain) thereafter into adult life. 2. The activity of adenosine 3′-phosphate 5′-sulphatophosphate–galactosyldiacylglycerol sulphotransferase is almost absent before 10 days of age, attains a maximum at age 20 days, and slowly decreases thereafter with increasing age. This developmental pattern correlates well with that of other myelin-specific metabolites. 3. Both the concentration of the sulphogalactosylglycerolipid and the activity of sulphotransferase are greatly decreased in the non-myelinating jimpy mouse. 4. The myelin fraction of rat brain contains most of the sulphogalactosylglycerolipid. The lipid occurs in a diacyl and an alkylacyl form. Determinations of the relative amount of each type in brain showed about a 1:1 mixture in both 21-day-old and adult rats. Rats injected with H235SO4 at 20 days of age lost35S from the diacyl form at a higher rate than from the alkylacyl compound over a 21-day period. These data suggest that the diacyl form has a higher turnover than the alkylacyl derivative. The percentage of the total sulpholipid content of brain contributed by the sulphogalactosylglycerolipid is 16% in 21-day-old rats and 8.4% in adult rats.


Pharmacology ◽  
1997 ◽  
Vol 54 (2) ◽  
pp. 92-97 ◽  
Author(s):  
Leonidas C. Goudas ◽  
Daniel B. Carr ◽  
Iwona Maszczynska ◽  
James E. Marchand ◽  
Heinrich Wurm ◽  
...  

1980 ◽  
Vol 30 ◽  
pp. 188
Author(s):  
Yasuhiro Nishibe ◽  
Yoshikazu Matsuo ◽  
Toshio Yoshizaki ◽  
Masami Eigyo ◽  
Teruo Shloini ◽  
...  

1977 ◽  
Vol 164 (2) ◽  
pp. 339-348 ◽  
Author(s):  
John M. Land ◽  
Robert F. G. Booth ◽  
Ruud Berger ◽  
John B. Clark

1. The development of pyruvate dehydrogenase and citrate synthase activity in rat brain mitochondria was studied. Whereas the citrate synthase activity starts to increase at about 8 days after birth, that of pyruvate dehydrogenase starts to increase at about 15 days. Measurements of the active proportion of pyruvate dehydrogenase during development were also made. 2. The ability of rat brain mitochondria to oxidize pyruvate follows a similar developmental pattern to that of the pyruvate dehydrogenase. However, the ability to oxidize 3-hydroxybutyrate shows a different developmental pattern (maximal at 20 days and declining by half in the adult), which is compatible with the developmental pattern of the ketone-body-utilizing enzymes. 3. The developmental pattern of both the soluble and the mitochondrially bound hexokinase of rat brain was studied. The total brain hexokinase activity increases markedly at about 15 days, which is mainly due to an increase in activity of the mitochondrially bound form, and reaches the adult situation (approx. 70% being mitochondrial) at about 30 days after birth. 4. The release of the mitochondrially bound hexokinase under different conditions by glucose 6-phosphate was studied. There was insignificant release of the bound hexokinase in media containing high KCl concentrations by glucose 6-phosphate, but in sucrose media half-maximal release of hexokinase was achieved by 70μm-glucose 6-phosphate 5. The production of glucose 6-phosphate by brain mitochondria in the presence of Mg2++glucose was demonstrated, together with the inhibition of this by atractyloside. 6. The results are discussed with respect to the possible biological significance of the similar developmental patterns of pyruvate dehydrogenase and the mitochondrially bound kinases, particularly hexokinase, in the brain. It is suggested that this association may be a mechanism for maintaining an efficient and active aerobic glycolysis which is necessary for full neural expression.


Endocrinology ◽  
1994 ◽  
Vol 135 (2) ◽  
pp. 583-588 ◽  
Author(s):  
B Mellström ◽  
C Pipaón ◽  
J R Naranjo ◽  
A Perez-Castillo ◽  
A Santos

1999 ◽  
Vol 35 (4) ◽  
pp. 337-343 ◽  
Author(s):  
M.N Subhash ◽  
K.Y Vinod ◽  
B.N Srinivas

1986 ◽  
Vol 46 (4) ◽  
pp. 1200-1206 ◽  
Author(s):  
Frances V. White ◽  
Arrel D. Toews ◽  
Pierre Morell

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