Gene expression profiling of muscle tissue in Brahman steers during nutritional restriction1

Byrne, Keren; Wang, Y. H.; Lehnert, S. A.; Harper, Gregory S.; McWilliam, Sean; Bruce, Heather L.; Reverter, Antônio

doi:10.2527/2005.8311

Cited by 86 publications

(57 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Effects of dietary P levels on electron transport chain gene expression Nutrigenomics approaches have been used to provide a molecular understanding of how common dietary components and nutritional strategies effect animal growth and tissue development by altering the gene expression (Costa et al, 2004;Byrne et al, 2005). Nutrigenomics studies in pigs are still rare, but they are become important as we develop an understanding about the relationship between nutrition, tissue growth and performance.…”

Section: Discussionmentioning

confidence: 99%

Effect of heat stress and feeding phosphorus levels on pig electron transport chain gene expression

Weller

Alebrante

Campos

et al. 2013

Animal

View full text Add to dashboard Cite

The purpose of this study was to evaluate the effect of temperature and different levels of available phosphorus (aP) on the expression of nine genes encoding electron transport chain proteins in the Longissimus dorsi (LD) muscle of pigs. Two trials were carried out using 48 high-lean growth pigs from two different growth phases: from 15 to 30 kg (phase 1) and from 30 to 60 kg (phase 2). Pigs from growth phase 1 were fed with three different levels of dietary aP (0.107%, 0.321% or 0.535%) and submitted either to a thermoneutral (24°C and RH at 76%) or to a heat stress (34°C and RH at 70%) environment. Pigs from growth phase 2 were fed with three different levels of dietary aP (0.116%, 0.306% or 0.496%) and submitted either to a thermoneutral (22ºC and RH at 77%) or to a heat stress (32ºC and RH at 73%) environment. Heat stress decreased (P < 0.001) average daily feed i ntake at both growth phases. At 24°C, pigs in phase 1 fed the 0.321% aP diet had greater average daily gain and feed conversion (P < 0.05) than those fed the 0.107% or 0.535% while, at 34°C pigs fed the 0.535% aP had the best performance (P < 0.05). Pigs from phase 2 fed the 0.306% aP had best performance in both thermal environments. Gene expression profile was analyzed by quantitative real-time polymerase chain reaction. Irrespective of growing phase, the expression of six genes was lower (P < 0.05) at high temperature than at thermoneutrality. The lower expression of these genes under high temperatures evidences the effects of heat stress by decreasing oxidative metabolism, through adaptive physiological mechanisms in order to reduce heat production. In pigs from phase 1, six genes were differentially expressed across aP levels (P < 0.05) in the thermoneutral and one gene in the heat stress. In pigs from phase 2, two genes were differentially expressed across aP levels (P < 0.05) in both thermal environments. These data revealed strong evidence that phosphorus and thermal environments are key factors to regulate oxidative phosphorylation with direct implications on animal performance.Keywords: nutrigenomics, oxidative phosphorylation, pig production, heat stress and animal production, phosphorous levels for pig nutrition ImplicationsData from this study are the first to reveal the effects of different available phosphorus (P) levels in Longissimus dorsi gene expression related to oxidative phosphorylation and its implications on pig performance. Moreover, this study showed the effects of high temperatures on the expression of these genes and how this may alter the physiological response to P. This information will contribute to better understand the role of P in energy metabolism and will bring new insights into the comprehension of the effects of high temperatures on nutritional requirements and mitochondrial function.

show abstract

Section: Discussionmentioning

confidence: 99%

Effect of heat stress and feeding phosphorus levels on pig electron transport chain gene expression

Weller

Alebrante

Campos

et al. 2013

Animal

View full text Add to dashboard Cite

show abstract

“…Physiol Genomics • VOL 28 • www.physiolgenomics.org septic muscle (55); 9) muscle-specific RING finger protein 3 (MuRF3); and 10) ␥-aminobutyric acid receptor associated protein, which is upregulated in mammalian muscle wastage (7,41). On the other hand, RBT degenerating muscle downregulated the expression of many genes (Table 6) involved in several signal transduction cascades that regulate cell cycle progression, including: 1) the anaphase-promoting subunit 1, ubiquitin-protein ligase, and 2) thyroid hormone receptor interactor 3.…”

Section: Microarray Analysis Of Atrophying Trout Musclementioning

confidence: 99%

Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model

Salem

Kenney

Rexroad

et al. 2006

Physiological Genomics

115

View full text Add to dashboard Cite

Salem M, Kenney PB, Rexroad CE 3rd, Yao J. Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model. Physiol Genomics 28: 33-45, 2006. First published August 1, 2006; doi:10.1152/physiolgenomics.00114.2006.-Muscle atrophy is a physiological response to diverse physiological and pathological conditions that trigger muscle deterioration through specific cellular mechanisms. Despite different signals, the biochemical changes in atrophying muscle share many common cascades. Muscle deterioration as a physiological response to the energetic demands of fish vitellogenesis represents a unique model for studying the mechanisms of muscle degradation in non-mammalian animals. A salmonid microarray, containing 16,006 cDNAs, was used to study the transcriptome response to atrophy of fast-switch muscles from gravid rainbow trout compared with sterile fish. Eighty-two unique transcripts were upregulated and 120 transcripts were downregulated in atrophying muscles. Transcripts having gene ontology identifiers were grouped according to their functions. Muscle deterioration was associated with elevated expression of genes involved in the catheptic and collagenase proteolytic pathways; the aerobic production, buffering, and utilization of ATP; and growth arrest; whereas atrophying muscle showed downregulation of genes encoding a serine proteinase inhibitor, enzymes of anaerobic respiration, muscle proteins as well as genes required for RNA and protein biosynthesis/processing. Therefore, gene transcription of the trout muscle atrophy changed in a manner similar to mammalian muscle atrophy. These changes result in an arrest of normal cell growth, protein degradation, and decreased glycolytic cellular respiration that is characteristic of the fast-switch muscle. For the first time, other changes/mechanisms unique to fish were discussed including genes associated with muscle atrophy. atrophy; Oncorhynchus mykiss SEVERAL PHYSIOLOGICAL and pathological conditions can cause muscle atrophy by triggering unique responses through distinct cellular stimuli. Transcriptional mechanisms of muscle wastage are well characterized at the transcriptome level in mammalian models as a response to nutritional restriction (7), fasting, severe diseases, including cancer, renal failure, diabetes (41, 42), and sepsis (42), as well as muscle disuse or denervation (4, 57). Some studies have dealt with fish muscle atrophy at the level of individual genes/mechanisms (46, 51, 58, 60 -62). The molecular basis of mammalian muscle atrophy has received considerable attention in the literature (25,30). Losing muscle mass results from elevated rate of proteolysis and decreased rate of protein synthesis. Despite the significant amount of literature (30,32,42), the specific roles of the proteolytic systems in degrading mammalian muscle still are unclear. Moreover, we recently showed that fish use different muscle degrading proteolytic strategies compared with mammals (58). The ubiquitin-proteasome pathway,...

show abstract

“…In agriculture and veterinary medicine, muscle atrophy caused by malnutrition is the culprit of inefficiently growing animals and alters meat quality. Atrophy, along with caloric restriction, induces cytoskeletal remodeling of muscle fibers which may contribute to lower quality less tender meat product [42]. Aging also proves to be a factor for muscle atrophy.…”

Section: Mapks and Muscle Atrophymentioning

confidence: 99%

MAPK Pathway in Skeletal Muscle Diseases

Geisler¹,

Shi

Gerrard³

2013

Journal of Veterinary Science and Animal Husbandry

View full text Add to dashboard Cite

Mitogen-Activated Protein Kinase (MAPK) pathway is a signal transduction pathway that functions in a wide range of physiological and pathophysiological cellular events including cell proliferation, differentiation, apoptosis, migration, inflammation, metabolic disorders and diseases. In skeletal muscle, it plays an essential role in muscle fiber specialization, muscle mass maintenance, damage induced muscle regeneration and muscle diseases. This review provides an overview of MAPK pathway and its pathophysiological role in skeletal muscle diseases with a primary focus on muscular dystrophy and atrophy.MAPK pathway consists of at least 4 subfamilies that include extracellular signal-regulated kinase 1 and 2 (ERK 1/2), p38α/β/γ/δ MAPK, c-Jun NH2-terminal kinases 1, 2, and 3 (JNK 1/2/3), and ERK5 [1][2][3][4]. MAPKs are a family of protein phosphorylating enzymes [5] that regulate diverse aspects of cellular responses in physiology, immunology, neurobiology, and energy metabolism [6]. Cellular activities regulated by MAPKs include proliferation, differentiation, apoptosis, motility [7,8], stress responses, inflammation, and innate immunity [9][10][11]. MAPK functions through transcriptional activation and posttranslational modification on the downstream substrates. Specifically, MAPKs are involved in the production of antimicrobial factors, cytokines, chemokines, and other inflammatory mediatory factors [12]. In the central nervous system, MAPKs are required for proper neuronal axonal development [13]. MAPKs also play a critical part in energy metabolism through modulating lipid metabolism [14][15][16] and skeletal muscle growth and fiber type [6]. Given the fact that MAPKs play such a fundamental and integral role in a broad range of biological processes, interference of this pathway and their downstream effector proteins may have detrimental consequences leading to either metabolic disorder or diseases. This review mainly focuses on the functional role of MAPK pathway in skeletal muscle diseases. [18,19]. Given the fact that each tier of phosphorylation consists of multiple kinases, one may question how an extracellular signal is decoded and transduced into a specific cellular response in a temporal and spatial manner. The complexity of regulation of the MAPKs provides a platform on which diverse signals converge and are precisely deciphered to generate a specific signal that fine-tunes the signaling network within a cell. On the other hand, an activated MAPK signal has to be curtailed in a timely manner so that cell will not overreact to a stimulus so to maintain metabolic homeostasis. One mechanism involves the dephosphorylation and thus inactivation of MAPKs by the MAPK phosphatases (MKPs) [5]. MKPs, also known as dual-specificity protein phosphatases (DUSPs), are a group of 10 catalytically active protein tyrosine phosphatases [9,20,21]. MKPs inactivate MAPKs through dephosphorylation of MAPKs on regulatory threonine and tyrosine residues. Though the substrates of the MKPs are to some extent overlapp...

show abstract

Gene expression profiling of muscle tissue in Brahman steers during nutritional restriction1

Cited by 86 publications

References 39 publications

Effect of heat stress and feeding phosphorus levels on pig electron transport chain gene expression

Effect of heat stress and feeding phosphorus levels on pig electron transport chain gene expression

Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model

MAPK Pathway in Skeletal Muscle Diseases

Contact Info

Product

Resources

About