The Effects of Aging on Local Rates of Cerebral Protein Synthesis in Rats

Author(s):  
Malin C. Ingvar ◽  
P. Maeder ◽  
L. Sokoloff ◽  
C. B. Smith
Brain ◽  
1985 ◽  
Vol 108 (1) ◽  
pp. 155-170 ◽  
Author(s):  
M.C. INGVAR ◽  
P. MAEDER ◽  
L. SOKOLOFF ◽  
C. B. SMITH

1986 ◽  
pp. 463-467
Author(s):  
K. Takahashi ◽  
W. Bodsch ◽  
T. Shibata ◽  
K.-A. Hossmann

2001 ◽  
Vol 11 (s1) ◽  
pp. S150-S163 ◽  
Author(s):  
Peter A. Farrell

Skeletal muscle proteins are constantly being synthesized and degraded, and the net balance between synthesis and degradation determines the resultant muscle mass. Biochemical pathways that control protein synthesis are complex, and the following must be considered: gene transcription, mRNA splicing, and transport to the cytoplasm; specific amino acyl-tRNA, messenger (mRNA), ribosomal (rRNA) availability; amino acid availability within the cell; the hormonal milieu; rates of mRNA translation; packaging in vesicles for some types of proteins; and post-translational processing such as glycation and phosphorylation/dephosphorylation. Each of these processes is responsive to the need for greater or lesser production of new proteins, and many states such as sepsis, uncontrolled diabetes, prolonged bed-rest, aging, chronic alcohol treatment, and starvation cause marked reductions in rates of skeletal muscle protein synthesis. In contrast, acute and chronic resistance exercise cause elevations in rates of muscle protein synthesis above rates found in nondiseased rested organisms, which are normally fed. Resistance exercise may be unique in this capacity. This chapter focuses on studies that have used exercise to elucidate mechanisms that explain elevations in rates of protein synthesis. Very few studies have investigated the effects of aging on these mechanisms; however, the literature that is available is reviewed.


1997 ◽  
Vol 9 (2) ◽  
pp. 271-279 ◽  
Author(s):  
Hajime Nakanishi ◽  
Yun Sun ◽  
Richard K. Nakamura ◽  
Kentaro Mori ◽  
Masanori Ito ◽  
...  

1991 ◽  
Vol 11 (5) ◽  
pp. 753-761 ◽  
Author(s):  
G. Mies ◽  
S. Ishimaru ◽  
Y. Xie ◽  
K. Seo ◽  
K.-A. Hossmann

The ischemic threshold of protein synthesis and energy state was determined 1, 6, and 12 h after middle cerebral artery (MCA) occlusion in rats. Local blood flow and amino acid incorporation were measured by double tracer autoradiography, and local ATP content by substrate-induced bioluminescence. The various images were evaluated at the striatal level in cerebral cortex by scanning with a microdensitometer with 75 μm resolution. Each 75 × 75 μm digitized image pixel was then converted into the appropriate units of either protein synthesis, ATP content, or blood flow. The ischemic threshold was defined as the flow rate at which 50% of pixels exhibited complete metabolic suppression. One hour after MCA occlusion, the threshold of protein synthesis was 55.3 ± 12.0 ml 100 g−1 min−1 and that of energy failure was 18.5 ± 9.8 ml 100 g−1 min−1. After 6 and 12 h of MCA occlusion, the threshold of protein synthesis did not change (52.0 ± 9.6 and 56.0 ± 6.5 ml 100 g−1 min−1, respectively) but the threshold of energy failure increased significantly at 12 h following MCA occlusion to 31.9 ± 9.7 ml 100 g−1 min−1 ( p < 0.05 compared to 1 h ATP threshold value; all values are mean ± SD). In focal cerebral ischemia, therefore, the threshold of energy failure gradually approached that of protein synthesis. Our results suggest that with increasing duration of ischemia, survival of brain tissue is determined by the high threshold of persisting inhibition of protein synthesis and not by the much lower one of acute energy failure. If the ischemic penumbra is considered to comprise the region in which cerebral protein synthesis is suppressed and energy state is preserved, it follows that the size of the penumbra decreases with the duration of ischemia.


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