Mobasheri, Ali

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Ali Mobasheri

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Proteomic Profiling and Its Applications to Muscle Aging and Sarcopenia

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Frontiers in Physiology

General Commentary
published: 03 January 2012
doi: 10.3389/fphys.2011.00117
Proteomic profiling and its applications to muscle aging 
and sarcopenia
Ali Mobasheri*
Musculoskeletal Research Group, Division of Veterinary Medicine, Faculty of Medicine and Health Sciences, School of Veterinary Medicine and Science, University of 
Nottingham, Nottingham, UK
*Correspondence: ali.mobasheri@nottingham.ac.uk
drial enzymes and concomitant decrease in 
glycolytic enzymes during the fast-to-slow 
transformation process in aging skeletal 
muscle. This timely mini-review also dis-
cusses alterations in metabolic and contrac-
tile elements that can be used to define a 
“sarcopenia-specific” biomarker signature.
The preservation of skeletal muscle mass 
is central to maintaining mobility and qual-
ity of life with aging and also impacts on our 
capacity to recover from illness and injury 
(Murton and Greenhaff, 2010). Muscle 
mass loss accompanies periods of bedrest 
and limb immobilization in humans 
(Marimuthu et al., 2011). This is something 
that elderly human patients may frequently 
experience especially if they undergo major 
operations and are hospitalized for other 
age-related diseases. Studies investigating 
processes underlying disuse-induced mus-
cle atrophy provide us with an opportunity 
to study temporal changes in cellular and 
molecular processes in muscle (Murton 
and Greenhaff, 2010). Proteomic profiling 
has many potential applications in this area. 
This area of research raises some important 
questions and paves the way forward for 
future areas of investigation. A substantial 
body of evidence has accumulated over the 
past 35 years in support of a role for reac-
tive oxygen species (ROS) oxidative dam-
age to the mitochondrial respiratory chain 
and mitochondrial DNA in aging (Jang and 
Remmen, 2009). More studies are clearly 
required to fully understand the role of 
mitochondria in age related disease and 
aging. These mitochondrial changes are 
thought to contribute to sarcopenia and 
muscle aging (Fulle et al., 2004). This arti-
cle gives hope to muscle researchers who 
have adopted (or are planning to employ) 
proteomic profiling as tool for exploring 
the bioenergetic changes that occur in 
aging muscle and the determining poten-
tial relevance of the mitochondrial theory 
of aging to sarcopenia. This approach may 
also be useful for studies aimed at unrave-
tion) and lipids in muscle affects function 
and there a change in relative muscle fiber 
composition with age where muscle fib-
ers effectively shrink (Grimby et al., 1984). 
These changes in muscle, combined with 
normal aging changes in the nervous sys-
tem, reduce muscular tone and contraction. 
Muscles become rigid like joints and do not 
recover their tone, even with regular physi-
cal exercise. Aging is therefore a complex 
process but in muscle it is usually associated 
with a decrease in mass, strength, and effi-
ciency of contraction. However, in essence, 
there is a generalized decline in muscle pro-
tein synthesis (Grimby and Saltin, 1983). 
The underlying mechanism of functional 
changes in aging muscle has yet to be fully 
understood.
“Physiology and Pathophysiology of 
Musculoskeletal Aging” is a Frontiers 
Research Topic aimed at increasing our 
understanding of musculoskeletal aging, 
placing special emphasis on healthy aging 
as a key research priority. Proteomics and 
mass spectrometry have been successfully 
applied to crude extracts and subcellu-
lar fractions of skeletal muscle to identify 
novel aging marker proteins in animal 
models of aging and human muscle tis-
sues from elderly subjects. In this Research 
Topic Kay Ohlendieck reviews the applica-
tions of proteomic profiling to aging muscle 
and the “fast-to-slow” muscle transitions 
that are thought to occur during aging. 
The author discusses proteomic profiling 
approaches that have helped to established 
an age-related shift to slower protein iso-
forms of myosin heavy chain, myosin light 
chain, actin, and tropomyosin (TM), as 
well as subunits of troponin (Ohlendieck, 
2011). His mini-review also discusses the 
“glycolytic-to-oxidative” shift that occurs 
in slower-twitching senescent muscles and 
the newly identified proteins that are altered 
in aging muscle using proteomic profiling 
(Ohlendieck, 2011). Proteomic profiling 
has also revealed an increase in mitochon-
A commentary on
Proteomic profiling of fast-to-slow muscle 
transitions during aging
by Ohlendieck, K. (2011). Front. Physio. 
2:105. doi: 10.3389/fphys.2011.00105
Aging causes dramatic changes in the 
musculoskeletal system. Muscle, bone, 
cartilage, and tendon are all affected. For 
example, bone mass is reduced as people 
age, especially in women after menopause. 
The bones become lighter and less dense 
as they lose calcium and other minerals. 
Intervertebral disks lose fluid and become 
thinner, compromising their gel-like prop-
erties and their ability to withstand load. 
Synovial joints become stiff and lose their 
flexibility. Articular cartilage becomes drier, 
thinner, and much more fragile and syno-
vial fluid loses some of its lubricating prop-
erties. This eventually results in the erosion 
of cartilage, formation of osteophytes, and 
changes in subchondral bone.
Sarcopenia is the degenerative loss of 
skeletal muscle structure and function 
associated with the aging process. Age-
related changes in muscle mass, structure, 
and function can be particularly dramatic. 
The gradual loss of muscle tissue (atrophy) 
reduces total body mass. The age-related 
alterations in muscle involve age-related 
muscle fiber transitions and metabolic 
shifts in aging muscle. These alterations col-
lectively affect posture and gait and these 
changes are particularly evident in our sev-
enties, eighties, and nineties. These changes 
involve anatomical, morphological, and 
enzymatic alterations in muscle (Grimby 
et al., 1982). In older individuals the nor-
mal physiological turnover of muscle is 
compromised and older muscle is replaced 
much more slowly, and the lost muscle may 
be replaced with adipose tissue or a tough 
fibrous connective tissue. The deposition 
of lipofuscin (also known as the aging pig-
ment and by-product of lysosomal degrada-
www.frontiersin.org January 2012 | Volume 2 | Article 117 | 1
Marimuthu, K., Murton, A. J., and Greenhaff, P. L. (2011). 
Mechanisms regulating muscle mass during disuse 
atrophy and rehabilitation in humans. J. Appl. Physiol. 
110, 555–560.
Murton, A. J., and Greenhaff, P. L. (2010). Physiological 
control of muscle mass in humans during resistance 
exercise, disuse and rehabilitation. Curr. Opin. Clin. 
Nutr. Metab. Care 13, 249–254.
Ohlendieck, K. (2011). Proteomic profiling of fast-to-
slow muscle transitions during aging. Front. Physiol. 
2:105. doi: 10.3389/fphys.2011.00105
Received: 04 December 2011; accepted: 15 December 2011; 
published online: 03 January 2012.
Citation: Mobasheri A (2012) Proteomic profiling and its 
applications to muscle aging and sarcopenia. Front. Physio. 
2:117. doi: 10.3389/fphys.2011.00117
This article was submitted to Frontiers in Striated Muscle 
Physiology, a specialty of Frontiers in Physiology.
Copyright © 2012 Mobasheri. This is an open-access arti-
cle distributed under the terms of the Creative Commons 
Attribution Non Commercial License, which permits non-
commercial use, distribution, and reproduction in other 
forums, provided the original authors and source are credited.
Celegato, B., Capitanio, D., Pescatori, M., Romualdi, C., 
Pacchioni, B., Cagnin, S., Vigano, A., Colantoni, L., 
Begum, S., Ricci, E., Wait, R., Lanfranchi, G., and Gelfi, 
C. (2006). Parallel protein and transcript profiles of 
FSHD patient muscles correlate to the D4Z4 arrange-
ment and reveal a common impairment of slow to 
fast fibre differentiation and a general deregulation 
of MyoD-dependent genes. Proteomics 6, 5303–5321.
Fulle, S., Protasi, F., Di Tano, G., Pietrangelo, T., Beltramin, 
A., Boncompagni, S., Vecchiet, L., and Fano, G. (2004). 
The contribution of reactive oxygen species to sarco-
penia and muscle ageing. Exp. Gerontol. 39, 17–24.
Grimby, G., Aniansson, A., Zetterberg, C., and Saltin, B. 
(1984). Is there a change in relative muscle fibre com-
position with age? Clin. Physiol. 4, 189–194.
Grimby, G., Danneskiold-Samsoe, B., Hvid, K., and Saltin, 
B. (1982). Morphology and enzymatic capacity in arm 
and leg muscles in 78-81 year old men and women. 
Acta Physiol. Scand. 115, 125–134.
Grimby, G., and Saltin, B. (1983). The ageing muscle. 
Clin. Physiol. 3, 209–218.
Jang, Y. C., and Remmen, V. H. (2009). The mitochondrial 
theory of aging: insight from transgenic and knockout 
mouse models. Exp. Gerontol. 44, 256–260.
ling the role of satellite cells and innerva-
tion in skeletal repair and adaptation and 
the potential for reversing skeletal muscle 
atrophy (Carlson, 1995), especially in the 
context of ROS imbalance induced by an 
increased oxidative metabolism (Celegato 
et al., 2006). Clearly there is a need for more 
dialog and discussion between researchers 
in closely related fields (e.g., endocrinology, 
skeletal muscle, physiology, exercise physi-
ology, gerontology) and for multidiscipli-
nary approaches in order to gain greater 
insight into sarcopenia. This is one of the 
overarching objectives of this Frontiers 
Research Topic.
RefeRences
Carlson, B. M. (1995). Factors influencing the repair and 
adaptation of muscles in aged individuals: satellite 
cells and innervation. J. Gerontol. A Biol. Sci. Med. 
Sci. 50, 96–100.
Mobasheri Proteomic profiling of muscle aging
Frontiers in Physiology | Striated Muscle Physiology  January 2012 | Volume 2 | Article 117 | 2


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Proteomic Profiling and Its Applications to Muscle Aging and Sarcopenia

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