Proteomic analysis of the mitochondria-enriched fraction from diabetic rat skeletal muscle

Mullen, Edel; Ohlendieck, Kay

doi:10.5584/jiomics.v1i1.42

Cited by 3 publications

(3 citation statements)

References 35 publications

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“…We also detected reduced expression of NADH dehydrogenase subunit 1(ND) in diabetic rats of both genders, with greater reduction in females compared to healthy controls, similar to that observed in T2DM subjects [30,31]. Impaired expression of ND1 represents mitochondrial metabolic derangement during the development of diabetes [30].…”

Section: Discussionmentioning

confidence: 78%

Gender-Dimorphic Regulation of Skeletal Muscle Proteins in Streptozotocin-Induced Diabetic Rats

Choi

Choi²,

Chaudhari³

et al. 2013

Cell Physiol Biochem

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Background: Despite the fact that sexual differences increase diabetic risk and contribute to the need for gender-specific care, there remain contradictory results as to whether or not sexual dimorphism increases susceptibility to the development of type 1 diabetes mellitus. Methods: To examine gender-dimorphic regulation of skeletal muscle proteins between healthy control and STZ-induced diabetic rats of both genders, we performed differential proteome analysis using two-dimensional electrophoresis combined with mass spectrometry. Results: Animal experiments revealed that STZ treatment rendered female rats more susceptible to induction of diabetes than their male littermates with significantly lower plasma insulin levels due to hormonal regulation. Proteomic analysis of skeletal muscle identified a total of 21 proteins showing gender-dimorphic differential expression patterns between healthy controls and diabetic rats. Most interestingly, gender-specific proteome comparison showed that male and female rats displayed differential regulation of proteins involved in muscle contraction, carbohydrate, and lipid metabolism, as well as oxidative phosphorylation and cellular stress. Conclusion: The current proteomic study revealed that impaired protein regulation was more prominent in the muscle tissue of female diabetic rats, which were more susceptible to STZ-induced diabetes. We expect that the present proteomic data can provide valuable information for evidence-based gender-specific treatment of diabetes.

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Section: Discussionmentioning

confidence: 78%

Gender-Dimorphic Regulation of Skeletal Muscle Proteins in Streptozotocin-Induced Diabetic Rats

Choi

Choi²,

Chaudhari³

et al. 2013

Cell Physiol Biochem

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“…Sample Technique Isfort, et al 2000 [3] Rat soleus denervation 2DGE, MALDI-TOF Sanchez, et al 2001 [4] Mouse skeletal muscle 2DGE, MALDI-TOF Yan, et al 2001 [11] Rat skeletal muscle 2DGE, MALDI-TOF Le Bihan, et al 2004 [12] Mouse skeletal muscle SELDI-TOF Donoghue, et al 2005 [13] Rabbit skeletal muscle electro-stimulation 2DGE, MALDI-TOF Piec, et al 2005 [14] Rat skeletal muscle ageing 2DGE, MALDI-TOF Okumura, et al 2005 [15] Rat skeletal muscle SDS-PAGE, 2DGE, MALDI-TOF Gelfi, et al 2006 [6] Rat soleus & gastrocnemius ageing 2-DGE, LC-ESI-MS/MS Guelfi, et al 2006 [16] Rat skeletal muscle acute exercise 2DGE, LC-ESI-MS/MS O'Connell, et al 2007 [17] Rat skeletal muscle ageing 2DGE, MALDI-TOF De Palma, et al 2007 [18] Rat skeletal muscle hypoxia 2D DIGE, LC-ESI-MS/MS Donoghue, et al 2007 [19] Rabbit tibialis anterior electro-stimulation 2DGE, MALDI-TOF Burniston 2008 [20] Rat Plantaris exercise 2DGE, MALDI-TOF/TOF Doran, et al 2008 [21] Rat skeletal muscle ageing 2D DIGE, MALDI-TOF O'Connell, et al 2008 [22] Rat gastrocnemius ageing 2DGE, MALDI-TOF Moriggi, et al 2008 [23] Rat skeletal muscle dytrophy 2D DIGE, MALDI-TOF Gannon, et al 2008 [24] Rat gastrocnemius ageing 2DGE, MALDI-TOF Gannon, et al 2009 [25] Rat gastrocnemius ageing 2DGE, MALDI-TOF Donoghue, et al (2010) [26] Rat skeletal muscle ageing 2DGE, MALDI-TOF, LC-ESI-MS/MS Lewis & Ohlendieck 2010 [27] Mouse skeletal muscle dystrophy 2DGE , LC-ESI-MS/MS Mullen & Ohlendieck 2010 [28] Rats gastrocnemius diabetes 2DGE, LC-ESI-MS/MS Mullen & Ohlendieck 2011 [29] Rat gastrocnemius diabetes 2DGE, LC-ESI-MS/MS Macedo, et al 2012 [30] Mouse skeletal muscle MALDI-TOF/TOF…”

Section: Author Yearmentioning

confidence: 99%

A Short History of Skeletal Muscle Proteomics

AB MALIK

2017

BPOJ

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Proteomics is the study of proteins using high-throughput techniques and relies on a combination of genomics, mass spectrometry and protein biochemistry. The human genome contains of approximately 20,000 genes that are transcribed into mRNA and then can be translated in to proteins Researchers can test hypotheses regarding individual mRNA or proteins using techniques such as Northern blots (for mRNA expression) or Western blots (for protein abundance). This ‘reductionist’ approach, where biology is reduced to individual questions, has been the mainstay of biological research. However, data arising from hypothesis-led studies clearly indicates that biology is not organised or controlled by isolated events Rather, biological systems are organised as complex networks and multiple interactions occur to bring about physiological changes. Therefore, more comprehensive (eg ‘-omic’) analysis techniques are required in order to advance our understanding of biological systems. The proteome is cell-specific and dynamic, responding on a minute-by-minute basis to changes in cell environment. Consequently, the proteome reflects the particular stage of development and current environmental condition the cell finds itself experiencing with regard exercise proteomics, report proteomic studies have mostly focused on striated muscle responses to endurance training, which are associated with health benefits underpinned by improvements in aerobic capacity. Over the past decade, researchers have studied the ability of proteomics analysis on skeletal muscle and the development of techniques. In this review we will point out some of the studies related that contributed to skeletal muscle proteomics

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“…Exercise, bre transitions, disuse atrophy and hypertrophy are clearly related to distinct changes in HSPB molecules. Systematic surveys of changes in HSP chaperones in neu-romuscular pathologies has included dysferlinopathy [111], Duchenne muscular dystrophy [17,70,71,[112][113][114][115][116][117][118][119][120][121][122][123][124][125][126], myobrillar myopathies with abnormalities in HSPB5, desmin, lamin or myotilin [127][128][129][130], myasthenia gravis [131], myotonia-related hyperexcitability [132], motor neuron diseases including amyotrophic lateral sclerosis [133][134][135][136][137], hypokalemic myopathy [138], obesity-related muscular weakness and/or type 2 diabetes-associated insulin resistance [139][140][141][142][143][144], burn sepsis-related stress [145] and post mortem changes in skeletal muscle samples [146].…”

Section: Comparative Proteomic Pro Ling Of Hspb In Skeletal Musclesmentioning

confidence: 99%

Proteomic profiling of the HSPB chaperonome: Mass spectrometric identification of small heat shock proteins in stressed skeletal muscles

Murphy¹,

Ohlendieck

2015

JIOMICS

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e continuing maintenance of protein homeostasis and the protection of proteomic integrity is essential for the survival of complex cellular systems under stressful conditions. Proteostasis is maintained by a complex system of protective pathways that involve several classes of molecular chaperones, now referred to as the chaperonome. e elaborate interplay of these components averts detrimental protein aggregation and supports proteins in resuming their functional fold. In skeletal muscle tissues, molecular chaperones protect contractile functions throughout bre adaptations to changed physiological demands and prevent tissue damage during acute phases of protein misfolding or prolonged periods of harmful protein accumulation. is results in considerable changes in the expression pro le of individual members of the large family of heat shock proteins. Systematic proteomic surveys of skeletal muscle tissues have revealed that the concentration of small heat shock proteins is especially a ected following strenuous exercise, in various neuromuscular disorders and during the natural aging process. Of the 10 identi ed members of the small heat shock protein HSPB family, HSPB1 (Hsp25), HSPB2 (MKBP), HSPB3 (Hsp27), HSPB4 (αA-crystallin), HSPB5 (αB-crystallin), HSPB6 (Hsp20), HSPB7 (cardiovascular cvHsp) and HSPB8 (Hsp22) are clearly present in skeletal muscle tissues. is review outlines the proteomic identi cation of small heat shock proteins and their muscle-speci c expression and induction patterns in health and disease. Since HSPB molecules are of relatively low molecular mass, belong to the markedly soluble type of proteins and represent critical pro-survival proteins that are intrinsically involved in the prevention of stress-induced bre damage, they present ideal muscle-associated biomarker candidates for the establishment of superior diagnostic and therapy-monitoring approaches to assess stress-related skeletal muscle degeneration.

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Proteomic analysis of the mitochondria-enriched fraction from diabetic rat skeletal muscle

Cited by 3 publications

References 35 publications

Gender-Dimorphic Regulation of Skeletal Muscle Proteins in Streptozotocin-Induced Diabetic Rats

Gender-Dimorphic Regulation of Skeletal Muscle Proteins in Streptozotocin-Induced Diabetic Rats

A Short History of Skeletal Muscle Proteomics

Proteomic profiling of the HSPB chaperonome: Mass spectrometric identification of small heat shock proteins in stressed skeletal muscles

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