Differential proteome and transcriptome analysis of porcine skeletal muscle during development

Xu, Yongjie; Qian, Hui; Feng, Xiaoting; Xiong, Yan; Lei, Minggang; Ren, Zhuqing; Zuo, Bo; Xu, Dequan; Ma, Yun; Yuan, Hongyu

doi:10.1016/j.jprot.2012.01.013

Cited by 47 publications

(35 citation statements)

References 88 publications

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“…In recent years, studies by combination of transcriptome and proteome have become more and more popular [17,[27][28][29][30], especially for non-model organisms and those lacking reference genomes. In most studies, proteome analysis was conducted based on the transcriptome analysis as it was thought that transcriptome deduced proteins could cover almost all of the proteins found in iTRAQ [27].…”

Section: Introductionmentioning

confidence: 99%

Transcriptomic and proteomic analyses of splenic immune mechanisms of rainbow trout (Oncorhynchus mykiss) infected by Aeromonas salmonicida subsp. salmonicida

Long

Zhao

et al. 2015

Journal of Proteomics

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Section: Introductionmentioning

confidence: 99%

Transcriptomic and proteomic analyses of splenic immune mechanisms of rainbow trout (Oncorhynchus mykiss) infected by Aeromonas salmonicida subsp. salmonicida

Long

Zhao

et al. 2015

Journal of Proteomics

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“…Large-scale MS studies of developing muscle fibers promise to establish the regulatory hierarchy of myogenesis and skeletal muscle regeneration. 2D gel-based analyses of skeletal muscle development have involved the proteomic profiling of C2C12 muscle cell culture models with a focus on myoblast differentiation and myotube formation [156,157] and postnatal muscle growth [158,159]. In addition, 1D-GE approaches were used to study changes in the skeletal muscle secretome during myogenesis [160,161,162].…”

Section: Comparative Skeletal Muscle Proteomics Using Two-dimensiomentioning

confidence: 99%

“…Proteomics also confirmed complex changes during the early postnatal period. The developing rat tibialis anterior [158] and porcine longissimus dorsi muscle [159] showed a time-dependent increase in contractile proteins and drastic alterations in metabolic enzymes, cytoskeletal proteins, molecular chaperones and signal transduction factors. An interesting negative regulator of muscle growth is myostatin, a secreted differentiation factor that belongs to the TGF-β superfamily [163].…”

Section: Comparative Skeletal Muscle Proteomics Using Two-dimensiomentioning

confidence: 99%

Comparative Skeletal Muscle Proteomics Using Two-Dimensional Gel Electrophoresis

Murphy¹,

Dowling²,

Ohlendieck³

2016

Proteomes

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The pioneering work by Patrick H. O’Farrell established two-dimensional gel electrophoresis as one of the most important high-resolution protein separation techniques of modern biochemistry (Journal of Biological Chemistry 1975, 250, 4007–4021). The application of two-dimensional gel electrophoresis has played a key role in the systematic identification and detailed characterization of the protein constituents of skeletal muscles. Protein changes during myogenesis, muscle maturation, fibre type specification, physiological muscle adaptations and natural muscle aging were studied in depth by the original O’Farrell method or slightly modified gel electrophoretic techniques. Over the last 40 years, the combined usage of isoelectric focusing in the first dimension and sodium dodecyl sulfate polyacrylamide slab gel electrophoresis in the second dimension has been successfully employed in several hundred published studies on gel-based skeletal muscle biochemistry. This review focuses on normal and physiologically challenged skeletal muscle tissues and outlines key findings from mass spectrometry-based muscle proteomics, which was instrumental in the identification of several thousand individual protein isoforms following gel electrophoretic separation. These muscle-associated protein species belong to the diverse group of regulatory and contractile proteins of the acto-myosin apparatus that forms the sarcomere, cytoskeletal proteins, metabolic enzymes and transporters, signaling proteins, ion-handling proteins, molecular chaperones and extracellular matrix proteins.

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“…They were predominantly directed on identification of key factors for meat quality variations (e.g. 123-125), but also compared effects of different muscle fiber type composition 126, compensatory growth 127, genetically determined muscle hypertrophy 128, intrauterine growth retardation 129, and ontogenetic stage 130. All of these studies considered the total proteome without differentiating between structural and functional components of the muscle cell itself on one hand and secreted proteins, on the other hand.…”

Section: Myokines - An Emerging New Class Of Secreted Proteinsmentioning

confidence: 99%

Molecular Heterogeneities of Adipose Depots - Potential Effects on Adipose-Muscle Cross-Talk in Humans, Mice and Farm Animals

Komolka¹,

Albrecht²,

Wimmers³

et al. 2014

J. Genomics

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Adipose tissue is considered as a major endocrine organ that secretes numerous proteins called adipokines. The heterogeneous nature of adipose tissue in different parts of the body suggests respective heterogeneity of proteomes and secretomes. This review consolidates knowledge from recent studies targeting the diversity of different adipose depots affecting the pattern of secreted adipokines and discusses potential consequences for the cross-talk between adipose and skeletal muscle in humans, rodent models and farm animals. Special attention is paid to muscle-associated fat depots like inter- and intramuscular fat that become focus of attention in the context of the rather new notion of skeletal muscle as a major endocrine organ. Understanding the complexity of communication between adipocytes and skeletal muscle cells will allow developing strategies for improvement of human health and for sustainable production of high quality meat.

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Differential proteome and transcriptome analysis of porcine skeletal muscle during development

Cited by 47 publications

References 88 publications

Transcriptomic and proteomic analyses of splenic immune mechanisms of rainbow trout (Oncorhynchus mykiss) infected by Aeromonas salmonicida subsp. salmonicida

Transcriptomic and proteomic analyses of splenic immune mechanisms of rainbow trout (Oncorhynchus mykiss) infected by Aeromonas salmonicida subsp. salmonicida

Comparative Skeletal Muscle Proteomics Using Two-Dimensional Gel Electrophoresis

Molecular Heterogeneities of Adipose Depots - Potential Effects on Adipose-Muscle Cross-Talk in Humans, Mice and Farm Animals

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