Age-related muscle dysfunction

doi:10.1016/j.exger.2008.05.003

Experimental Gerontology

Volume 44, Issues 1–2, January–February 2009, Pages 106-111

https://doi.org/10.1016/j.exger.2008.05.003 Get rights and content

Abstract

Aging is associated with a progressive decline of muscle mass, strength, and quality, a condition described as sarcopenia of aging. Despite the significance of skeletal muscle atrophy, the mechanisms responsible for the deterioration of muscle performance are only partially understood. The purpose of this review is to highlight cellular, molecular, and biochemical changes that contribute to age-related muscle dysfunction.

Section snippets

Sarcopenia

Aging is associated with a progressive decline of muscle mass, strength, and quality, a condition described as sarcopenia. These age-related changes are observed in healthy, active adults who are 50 years and older (Hughes et al., 2002). The prevalence of sarcopenia in older adults under the age of 70 years is about 25% and increases to 40% in adults 80 years or older (Baumgartner et al., 1998). Sarcopenia represents a risk factor for frailty, loss of independence, and physical disability (

Muscle physiology – short review

For skeletal muscle, the control of force has to be accurate and precise with the contractile machinery being switched on and off rapidly to allow for complex coordinated movements. Action potentials initiated at the neuromuscular junction propagate along the length of the fiber and the transverse tubules. As the wave of depolarization passes down the transverse tubules there is an interaction with the sarcoplasmic reticulum that results in the release of calcium, initiating the interaction of

Age-related changes in muscle contractility

Despite the significance of skeletal muscle atrophy and weakness as inevitable concomitants of old age, the underlying molecular mechanisms responsible for these impairments are only partially understood. Age-associated muscle atrophy is the result of a combination of individual-fiber atrophy, along with a decrease in the total number of fibers, with a preferential loss of type II (fast-twitch, glycolytic, fibers with myosin heavy chain type II isoforms) muscle fibers (Thompson, 1994). In

Age-related post-translational modifications of skeletal muscle proteins

The ‘free radical theory’ of aging, formulated 50 years ago, proposes that aging and associated degenerative diseases can be attributed to deleterious effects of reactive oxygen species (Harman, 1956). A current version of this theory is the ‘oxidative stress theory’ of aging. The ‘oxidative stress theory’ states that “A chronic state of oxidative stress exists in cells of aerobic organisms even under normal physiological conditions because of an imbalance of proxidants and antioxidants. This

Summary

Clearly, physiological studies detect age-related deterioration of contractility of single fibers. Structural analysis, using EPR, shows structural changes in myosin which are correlated with the age-related decline in force. Biochemical studies reveal age-related molecular changes in myosin and actin, which are most likely due to oxidative modifications. Studies evaluating post-translational modifications of key skeletal muscle proteins reveal modification-specific, protein-specific and

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Age-related muscle dysfunction

Abstract

Section snippets

Sarcopenia

Muscle physiology – short review

Age-related changes in muscle contractility

Age-related post-translational modifications of skeletal muscle proteins

Summary

Journal of Biological Chemistry

Journal of Biological Chemistry

Journal of Biological Chemistry

American Journal of Clinical Nutrition

Archives of Biochemistry and Biophysics

Free Radical Biology and Medicine

Journal of Biological Chemistry

Mechanisms of Ageing and Development

Free Radical Biology and Medicine

Biosens Bioelectron

Journal of Biological Chemistry

Peroxynitrite reactivity with amino acids and proteins

Amino Acids

Muscle fiber type composition of the rat hindlimb

American Journal of Anatomy

Reaction of rabbit skeletal myosin with d-glucose 6-phosphate

Biochemistry and Molecular Biology International

Effects of aging on in vivo synthesis of skeletal muscle myosin heavy-chain and sarcoplasmic protein in humans

American Journal of Physiology. Endocrinology and Metabolism

Epidemiology of sarcopenia among the elderly in New Mexico

American Journal of Epidemiology

Skeletal-muscle weakness in old-age – underlying mechanisms

Medicine and Science in Sports and Exercise

Tissue-specific variation in glycation of proteins in diabetes – evidence for a functional role of amadoriase enzymes

Annals of the New York Academy of Sciences

Superoxide, hydroxyl radical, and hydrogen peroxide effects on single-diaphragm fiber contractile apparatus

Journal of Applied Physiology

Proteomic identification of oxidatively modified proteins in Alzheimer’s disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71

Journal of Neurochemistry

The effect of aging and immobilization on structure and function of human skeletal muscle fibres

Journal of Physiology

Radical-mediated Protein Oxidation

Age-dependent accumulation of N-ε-(carboxymethyl)lysine and N-ε-(carboxymethyl)hydroxylysine in human skin collagen

Biochemistry

Oxidation of glycated proteins-age-dependent accumulation of N-ε-(carboxymethyl)lysine in lens proteins

Biochemistry

Age and sex influence on oxidative damage and functional status in human skeletal muscle

Journal of Muscle Research and Cell Motility

Altered proteasome structure, function, and oxidation in aged muscle

FASEB Journal

Disability in older adults: Evidence regarding significance, etiology, and risk

Journal of the American Geriatrics Society

Protein nitration with aging in the rat semimembranosus and soleus muscles

The Journals of Gerontology. Series A, Biological Sciences and Medical Sciences

Yeast protein glycation in vivo by methylglyoxal

FEBS

Aging: a theory based on free radical and radiation chemistry

Journal of Gerontology

Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase, Reaction of lipoic acid with 4-hydroxy-2-nonenal

Biochemistry