As we age we lose 30% of our muscle

As we age we lose 30% of our muscle (Faulkner JA, Brooks SV, Zerba E 1995; Rogers A, Evans WJ 1993 ).
This 30% includes your vital organs: liver, kidneys, brain and pancreas (Rattan 1992 ; Parrado 1999 ; Blazejowski 1983 ).

Extract

Institute of Gerontology, University of Michigan, Ann Arbor, USA.

In old compared with young animals, muscle mass is decreased by 30% to 40%, and maximum force and power are decreased to an even greater extent. The age-related declines in muscle mass and muscle function are similar to those that occur with decreased physical activity. Despite the similarities, we conclude that the losses in muscle mass, force, and power are not due solely to old animals being less active, but rather accrue from intrinsic age-related changes in muscles and in muscle fibers that appear to be immutable and irreversible.

The intrinsic changes are associated with denervation of fast fatigable fibers and motor units and motor unit remodeling, which may be initiated by contraction-induced injury. The mechanisms remain unresolved for the weakness, the fatigability, the high susceptibility to contraction-induced injury, and the impaired recovery from injury demonstrated by the skeletal muscles of old animals.

Synthesis, modifications, and turnover of proteins during aging.

Rattan SI.

Department of Chemistry, Aarhus University, Denmark.

Slowing down of bulk protein synthesis is one of the most commonly observed biochemical changes during aging. The implications and consequences of slower rates of protein synthesis are manifold, including a decrease in the availability of enzymes for the maintenance, repair, and normal metabolic functioning of the cell, an inefficient removal of inactive, abnormal, and damaged macromolecules in the cell, the inefficiency of the intracellular and intercellular signalling pathways, and a decrease in the production and secretion of hormones, antibodies, neurotransmitters, and the components of the extracellular matrix. Age-related changes in the activity, specificity, and stability of a large number of proteins have been reported. However, the molecular mechanisms responsible for such alterations are still poorly understood. Studies on various components of the protein synthetic machinery have revealed a decline in the efficiency and accuracy of ribosomes, an increase in the levels of rRNA and tRNA, and a decrease in the amounts and activities of elongation factors. Because posttranslational modifications of proteins determine their activity and stability, alterations in the extent and level of various modifications such as phosphorylation, methylation, ADP-ribosylation, oxidation, glycation, and conformational changes during aging are being studied. Changes in the regulation of protein synthesis, posttranslational modifications, and protein turnover are crucial determinants of age-related decline in the maintenance, repair, and survival of the organism.

Effects of aging on the various steps of protein synthesis: fragmentation of elongation factor 2.

Parrado J, Bougria M, Ayala A, Castano A, Machado A.

Departamento de Bioquimica, Bromatologia y Toxicologia, Facultad de Farmacia, Universidad de Sevilla, Spain.

The possible mechanism responsible for the in vivo protein synthesis decline during aging was studied. In order to determine the effect of aging on the various steps of protein synthesis, we determined the ribosomal state of aggregation and the time of assembly and release of polypeptide chains in the process of protein synthesis in rat liver. The results suggest that elongation is the most sensitive step to aging. A molecular study of the Elongation Factor 2 (EF-2), the main protein involved in the elongation step, shows that this protein has a higher content of carbonyl groups and is less active in old rats. In addition, the molecular mass analysis of EF-2 shows that this protein becomes fragmented in old rats. A similar pattern of fragmentation is found in 3-month-old rats suffering oxidative stress, in that the decline in protein synthesis is similar to that found in old rats. These data suggest that: i) oxidative stress seems to be involved in the modifications of EF-2 observed during aging, and ii) the observed modifications (oxidation and fragmentation) of EF-2 could account for the decline in protein synthesis in old animals.

Decreased rates of protein synthesis by cell-free preparations from different organs of aging mice.

Blazejowski CA, Webster GC.

Protein synthetic activity was determined in postmitochondrial preparations from heart, brain, kidney, liver and skeletal muscle of 5-26-month-old female C57B1/6J mice. An age-dependent decrease in the rate of protein synthesis was exhibited by all preparations except heart muscle. A 65% decrease in translational rate was found in liver, with the greatest decrease appearing after 21 months. Translation in the brain preparation declined little during the first 20 months, but dropped 33% between 20 and 26 months. The kidney preparation decreased 30% during the first 16 months and 70% by the end of 26 months of age. Skeletal muscle showed an overall decrease of 85% in translation rate. In contrast, heart muscle decreased no more than 10% over the life-span of the mice. From these results, it appears that aging has a differential effect on protein synthesis in different kinds of cells.