Proteomic identification of age-dependent protein nitration in rat skeletal muscle

Kański, Jarosław; Alterman, Michail A.; Schöneich, Christian

doi:10.1016/s0891-5849(03)00500-8

Cited by 112 publications

(117 citation statements)

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“…This includes increased oxidative stress, mitochondrial abnormalities, disturbed microcirculation, hormonal imbalance, incomplete ion homeostasis, denervation, and impaired excitation-contraction coupling (Larsson, 1998;Degens, 1998;Squier and Bigelow, 2000;Bua et al, 2002;Delbono, 2002), as well as a decreased regenerative potential (Renault et al, 2002;Lorenzon et al, 2004;Beccafico et al, 2007). In addition, altered posttranslational modifications, such as tyrosine nitration, were recently described as occuring in an age-related manner on numerous skeletal muscle proteins (Kanski et al, 2003(Kanski et al, , 2005. In analogy, we have investigated here potential changes in another frequent post-translational modification, i.e., N-glycosylation, by analyzing the glycoproteome of aged muscle fibers.…”

Section: Discussionmentioning

confidence: 99%

“…Altered post-translational modifications were shown to play a key role in biological aging (Schoneich et al, 1999). For example, altered tyrosine nitration was found in key muscle proteins, such as the sarcoplasmic reticulum Ca 2+ -ATPase, enolase, aldolase, creatine kinase, tropomyosin, glyceraldehyde-3-phosphate dehydrogenase, myosin light chain, pyruvate kinase, actinin, actin, and the ryanodine receptor (Kanski et al, 2003(Kanski et al, , 2005.…”

Section: Introductionmentioning

confidence: 99%

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Lectin-based proteomic profiling of aged skeletal muscle: Decreased pyruvate kinase isozyme M1 exhibits drastically increased levels of N-glycosylation

O’Connell

Doran

Gannon

et al. 2008

European Journal of Cell Biology

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Since various neuromuscular diseases are associated with abnormal glycosylation, it was of interest to determine whether this key post-translational modification is also altered in aged skeletal muscle. Lectins represent highly versatile carbohydrate-binding proteins that are routinely employed for the characterization of glycoproteins. Here, we used the lectin wheat germ agglutinin (WGA) for the proteomic profiling of senescent fibers. WGA labeling of the soluble proteome from 3-month-versus 30-month-old rat gastrocnemius muscle, following two-dimensional gel electrophoretic separation, resulted in the identification of 13 distinct protein species. Analysis of WGA binding levels, in conjunction with mass spectrometric fingerprinting, revealed that one isoform of a major metabolic muscle protein exhibited a drastic alteration in the content of sialic acid and N-acetylglucosaminyl sugar residues. Pyruvate kinase isoform M1 with protein accession number gi|16757994|, exhibiting a pI of 6.6 and an apparent molecular mass of 57.8 kDa, showed a six fold increase in N-glycosylation and a three fold decrease in protein expression. In contrast to comparable levels of N-glycosylated proteins in young adult versus senescent muscle, as judged by fluoresceinconjugated WGA labeling of transverse muscle cryosections, staining with antibodies to the M1 isoform of pyruvate kinase showed reduced expression of this cytosolic element. Furthermore, activity assays demonstrated a reduced activity of this glycolytic enzyme in senescent muscle. This agrees with the idea that abnormal post-translational modifications in key metabolic enzymes may be involved in the conversion of aged muscle to slower twitch patterns and a drastic shift to more aerobic-oxidative metabolism.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Lectin-based proteomic profiling of aged skeletal muscle: Decreased pyruvate kinase isozyme M1 exhibits drastically increased levels of N-glycosylation

O’Connell

Doran

Gannon

et al. 2008

European Journal of Cell Biology

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“…In addition, previous studies demonstrated oxidative modifications of carbonic andydrase III in vivo with a concomitant decrease in catalytic activities in liver tissue (Cabiscol and Levine, 1995). There is increasing evidence that links β-enolase and TPI as targets for nitration in Alzheimer's disease, and in aging cardiac and skeletal muscle, providing a possible rationale for the observed disturbance in energy metabolism of aging tissue (Castegna et al, 2002;Kanski et al, 2003;Kanski et al, 2005b) Viner and colleagues demonstrated a progressive age-related accumulation of nitrotyrosine that was selectively limited to the SERCA2a isoform in preparations from both fast-and slow-twitch rat muscle (Viner et al, 1999). Mass spectrometry analysis of tryptic peptides from aged rats identified the sites of nitration at tyrosine residues 294, 295, and 753.…”

Section: Nitration and Aging Skeletal Musclementioning

confidence: 95%

Age-related muscle dysfunction

Thompson

2009

Experimental Gerontology

200

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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“…Most studies of tyrosine nitration [118] rely on immunological detection thanks to commercially available antinitrotyrosine mAb, whether in the ELISA format [119], in which case it is difficult to distinguish between free circulating 3-nitrotyrosine and protein-bound nitrotyrosine, or in Western blot format after 1-D or 2-DE [120][121][122]. Immunoprecipitation with antinitrotyrosine antibodies allowed Nikov et al [123] to map nitration sites of HSA by MS.…”

Section: Nitrotyrosinementioning

confidence: 99%

Oxidation of proteins: Basic principles and perspectives for blood proteomics

Barelli

Canellini

Thadikkaran

et al. 2008

Proteomics Clinical Apps

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Protein oxidation mechanisms result in a wide array of modifications, from backbone cleavage or protein crosslinking to more subtle modifications such as side chain oxidations. Protein oxidation occurs as part of normal regulatory processes, as a defence mechanism against oxidative stress, or as a deleterious processes when antioxidant defences are overcome. Because blood is continually exposed to reactive oxygen and nitrogen species, blood proteomics should inherently adopt redox proteomic strategies. In this review, we recall the biochemical basis of protein oxidation, review the proteomic methodologies applied to analyse redox modifications, and highlight some physiological and in vitro responses to oxidative stress of various blood components.

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Proteomic identification of age-dependent protein nitration in rat skeletal muscle

Cited by 112 publications

References 39 publications

Lectin-based proteomic profiling of aged skeletal muscle: Decreased pyruvate kinase isozyme M1 exhibits drastically increased levels of N-glycosylation

Lectin-based proteomic profiling of aged skeletal muscle: Decreased pyruvate kinase isozyme M1 exhibits drastically increased levels of N-glycosylation

Age-related muscle dysfunction

Oxidation of proteins: Basic principles and perspectives for blood proteomics

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