Advanced Glycation End-Product Accumulation and Associated Protein Modification in Type II Skeletal Muscle With Aging

Snow, LeAnn M.; Fugere, Nicole A.; Thompson, La Dora V.

doi:10.1093/gerona/62.11.1204

Cited by 69 publications

(56 citation statements)

References 38 publications

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“…Age-related AGEs accumulation in skeletal muscle has been previously reported in an animal model [25], but in the present study, AGEs accumulation was unchanged by aging. Even GLO-1 levels were not changed in skeletal muscle.…”

Section: Discussioncontrasting

confidence: 45%

“…Even GLO-1 levels were not changed in skeletal muscle. Other studies have shown an increasing pattern of AGEs accumulation in skeletal muscle by aging used 33-month rats as the old groups [25]. In the present study, we used 22-month mice, which could explain the discrepancy between results, and suggests AGEs accumulation in the skeletal muscle might accelerate after 22 months in mice.…”

Section: Discussionmentioning

confidence: 67%

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Age dependent accumulation patterns of advanced glycation end product receptor (RAGE) ligands and binding intensities between RAGE and its ligands differ in the liver, kidney, and skeletal muscle

Son

Chung

et al. 2017

Immun Ageing

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BackgroundMuch evidence indicates receptor for advanced glycation end products (RAGE) related inflammation play essential roles during aging. However, the majority of studies have focused on advanced glycation end products (AGEs) and not on other RAGE ligands. In the present study, the authors evaluated whether the accumulation of RAGE ligands and binding intensities between RAGE and its ligands differ in kidney, liver, and skeletal muscle during aging.ResultsIn C57BL/6 N mice aged 12 weeks, 12 months, and 22 months, ligands accumulation, binding intensities between RAGE and its ligands, activated macrophage infiltration, M1/M2 macrophage expression, glyoxalase-1expression, and signal pathways related to inflammation were evaluated. The RAGE ligands age-associated accumulation patterns were found to be organ dependent. Binding intensities between RAGE and its ligands in kidney and liver increased with age, but those in skeletal muscle were unchanged. Infiltration of activated macrophages in kidney and liver increased with age, but infiltration in the skeletal muscle was unchanged. M1 expression increased and M2 and glyoxalase-1 expression decreased with age in kidney and liver, but their expressions in skeletal muscle were not changed.ConclusionThese findings indicate patterns of RAGE ligands accumulation, RAGE/ligands binding intensities, or inflammation markers changes during aging are organs dependent.Electronic supplementary materialThe online version of this article (doi:10.1186/s12979-017-0095-2) contains supplementary material, which is available to authorized users.

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Section: Discussioncontrasting

confidence: 45%

Section: Discussionmentioning

confidence: 67%

Age dependent accumulation patterns of advanced glycation end product receptor (RAGE) ligands and binding intensities between RAGE and its ligands differ in the liver, kidney, and skeletal muscle

Son

Chung

et al. 2017

Immun Ageing

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“…24,25 Similarly, progressive accumulation of AGE-modified proteins with aging and modification of critical enzymes in muscle energy production have been reported in experimental animals. 26 The accumulation of AGEs in myocytes is considered a pathogenic mechanism for the myocardial damage observed in diabetes mellitus. 27 Moreover, early glycated products such as glycated albumin are also capable of stimulating the production of reactive oxygen species (ROS) in cardiac myocytes.…”

Section: Discussionmentioning

confidence: 99%

Weight Increase Is Associated with Skeletal Muscle Immunostaining for Advanced Glycation End Products, Receptor for Advanced Glycation End Products, and Oxidation Injury

Maza

Uribarri²,

Olivares³

et al. 2008

Rejuvenation Research

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“…In a study comparing the extensor digitorum longus muscle (fast-twitch muscle) from young and very old rats, the older rats had a significantly greater percentage (10-fold difference) of myofibers that immunolabeled intracellularly for CML compared to the younger group (Snow et al, 2007). The pattern of the AGE immunolabeling had two characteristic appearances at the individual myofiber level.…”

Section: Glycation and Aging Skeletal Musclementioning

confidence: 99%

Age-related muscle dysfunction

Thompson

2009

Experimental Gerontology

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170

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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 weakness. Keywordsactin; myosin; aged muscle; enzymatic activity; oxidative modifications SarcopeniaAging 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 (Roubenoff, 2000). Loss of mobility resulting from muscle loss predicts major physical disability and mortality, and is associated with poor quality of life, social needs, and health care needs (Fried and Guralnik, 1997). The economic impact of sarcopenia and its detrimental correlates are immense (Janssen et al., 2004). Thus, understanding the mechanisms leading to muscle dysfunction (e.g., weakness) at advanced age represents a high public health priority. The purpose of this article is to highlight cellular, molecular, and biochemical changes that contribute to age-related muscle dysfunction. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. NIH Public Access Muscle physiology-short reviewFor 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 actin and myosin and muscle contraction. This process is known as excitation-contraction coupling. Thus, age-related structural changes or chemical modifications in proteins that affect excitation-contraction coupling are likely to influence muscle function.The basic contractile unit of muscle, the myofibril, consists of a linear array of sarcomeres, which contains interdigitating myosin and actin fila...

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Advanced Glycation End-Product Accumulation and Associated Protein Modification in Type II Skeletal Muscle With Aging

Cited by 69 publications

References 38 publications

Age dependent accumulation patterns of advanced glycation end product receptor (RAGE) ligands and binding intensities between RAGE and its ligands differ in the liver, kidney, and skeletal muscle

Age dependent accumulation patterns of advanced glycation end product receptor (RAGE) ligands and binding intensities between RAGE and its ligands differ in the liver, kidney, and skeletal muscle

Weight Increase Is Associated with Skeletal Muscle Immunostaining for Advanced Glycation End Products, Receptor for Advanced Glycation End Products, and Oxidation Injury

Age-related muscle dysfunction

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