scholarly journals Identification, characterization, and quantitative expression analysis of rainbow trout myostatin-1a and myostatin-1b genes

2006 ◽  
Vol 190 (3) ◽  
pp. 879-888 ◽  
Author(s):  
Dilip K Garikipati ◽  
Scott A Gahr ◽  
Buel D Rodgers
Keyword(s):  
Rainbow Trout ◽  
Genomic Organization ◽  
Expression Profiles ◽  
Muscle Growth ◽  
Fish Tissue ◽  
Tissue Expression ◽  
Negative Regulator ◽  
Cdna Clones ◽  
Mrna Levels ◽  
Quantitative Expression

Myostatin is a potent negative regulator of skeletal muscle growth. Although several cDNA clones have been characterized in different vertebrates, the genomic organization and bioactivity of non-mammalian homologs have not. The intron/exon organization and promoter subsequence analysis of two rainbow trout myostatin genes, rtMSTN-1a and rtMSTN-1b (formerly 1 and 2 respectively), as well as a quantitative assessment of their embryonic, larval, and adult tissue expression profiles are reported herein. Each gene was similarly organized into three exons of 490, 368, and 1600 bp for MSTN-1a and 486, 386, and 1419 bp for MSTN-1b. Comparative mapping of coding regions from several vertebrate myostatin genes revealed a common organization between species, including conserved pre-mRNA splice sites; the first among the fishes and the second across all vertebrate species. In silico subsequence analysis of the promoter regions identified E-boxes and other putative myogenic response elements. However, the number and diversity of elements were considerably less than those found in mammalian promoters or in the recently characterized zebrafish MSTN-2 gene. A quantitative analysis of the embryonic expression profile for both genes indicates that rtMSTN-1a expression is consistently greater than that of rtMSTN-1b and neither gene is significantly expressed throughout gastrulation. Expression of both steadily increases fourfold during somitogenesis and subsides as this period ends. After eyeing, however, rtMSTN-1a mRNA levels ultimately rise 20-fold by day 49 and peak before hatching and yolk sac absorption (YSA). Levels of rtMSTN-1b rise similarly, but do not peak before YSA. An analysis of adult (2-year-old fish) tissue expression indicates that both transcripts are present in most tissues although levels are highest in brain, testes, eyes, muscle, and surprisingly spleen. These studies suggest that strong selective pressures have preserved the genomic organization of myostatin genes throughout evolution. However, the different expression profiles and putative promoter elements in fishes versus mammals suggests that limitations in myostatin function may have evolved recently.

scholarly journals Dietary methionine availability affects the main factors involved in muscle protein turnover in rainbow trout (Oncorhynchus mykiss)

2014 ◽  
Vol 112 (4) ◽  
pp. 493-503 ◽  
Author(s):  
Ikram Belghit ◽  
Sandrine Skiba-Cassy ◽  
Inge Geurden ◽  
Karine Dias ◽  
Anne Surget ◽  
...  
Keyword(s):  
Rainbow Trout ◽  
Oncorhynchus Mykiss ◽  
White Muscle ◽  
Muscle Protein ◽  
Muscle Growth ◽  
Mrna Translation ◽  
Fish Feed ◽  
Mrna Levels ◽  
Methionine Deficiency ◽  
Main Factors

Methionine is a limiting essential amino acid in most plant-based ingredients of fish feed. In the present study, we aimed to determine the effect of dietary methionine concentrations on several main factors involved in the regulation of mRNA translation and the two major proteolytic pathways (ubiquitin–proteasome and autophagy-lysosomal) in the white muscle of rainbow trout (Oncorhynchus mykiss). The fish were fed for 6 weeks one of the three isonitrogenous diets providing three different methionine concentrations (deficient (DEF), adequate (ADQ) and excess (EXC)). At the end of the experiment, the fish fed the DEF diet had a significantly lower body weight and feed efficiency compared with those fed the EXC and ADQ diets. This reduction in the growth of fish fed the DEF diet was accompanied by a decrease in the activation of the translation initiation factors ribosomal protein S6 and eIF2α. The levels of the main autophagy-related markers (LC3-II and beclin 1) as well as the expression of several autophagy genes (atg4b, atg12 l, Uvrag, SQSTM1, Mul1 and Bnip3) were higher in the white muscle of fish fed the DEF diet. Similarly, the mRNA levels of several proteasome-related genes (Fbx32, MuRF2, MuRF3, ZNF216 and Trim32) were significantly up-regulated by methionine limitation. Together, these results extend our understanding of mechanisms regulating the reduction of muscle growth induced by dietary methionine deficiency, providing valuable information on the biomarkers of the effects of low-fishmeal diets.

scholarly journals Expression profiles of myostatin and calpastatin genes and analysis of shear force and intramuscular fat content of yak longissimus muscle

2011 ◽  
Vol 56 (No. 12) ◽  
pp. 545-550 ◽  
Author(s):  
Y.C. Zheng ◽  
Y.Q. Lin ◽  
Y. Yue ◽  
Y.O. Xu ◽  
S.Y. Jin
Keyword(s):  
Expression Profiles ◽  
Muscle Growth ◽  
Intramuscular Fat ◽  
Mrna Levels ◽  
Longissimus Muscle ◽  
Rt Pcr ◽  
Yellow Cattle ◽  
Significant Difference ◽  
Different Ages ◽  
Imf Content

The main objective of this study was to reveal the expression profiles of two negative regulators, myostatin (MSTN) and calpastatin (CAST)genes, of skeletal muscle growth in highland yaks (Bos grunniens). mRNA levels of both genes were quantified in different yak tissues by semi-quantitative RT-PCR to reveal the tissue expression pattern, and real-time quantitative RT-PCR was employed to compare the mRNA levels of MSTN and CAST in longissimus muscles of yaks at different ages and adult Yellow cattle. Intramuscular fat (IMF) content, tenderness and pH of longissimus muscle of yaks at different ages and of adult Yellow cattle were also measured. The results showed that MSTN and CAST expressions have tissue specificity and both exhibited a high level in longissimus muscle and a low level in adipose tissue. Yak calves had lower mRNA levels of both MSTN and CAST in longissimus muscle compared with adult yaks. The analysis of meat quality traits of longissimus muscle showed that the shear forces of raw longissimus muscle of yak calves were significantly lower than those of adult yaks and Yellow cattle, no significant difference was found between adult yaks and Yellow cattle of similar age. IMF content in longissimus muscle was lower in yaks than in Yellow cattle. Although yaks were smaller in body size than Yellow cattle, adult yaks showed lower levels of MSTN and similar level of CAST mRNA in longissimus muscle compared to Yellow cattle. These data indicate that the expression of both MSTN and CAST in longissimus muscle differs between adult yaks and yak calves, and the yak longissimus muscle shows a lower IMF content compared to cattle.  

scholarly journals Identification and tissue distribution of mRNAs encoding salmon-type calcitonins-IV and -V in the rainbow trout

2004 ◽  
Vol 32 (3) ◽  
pp. 963-974 ◽  
Author(s):  
Y Hidaka ◽  
M Suzuki
Keyword(s):  
Rainbow Trout ◽  
Amino Acid ◽  
Tissue Distribution ◽  
Restriction Enzymes ◽  
Tissue Expression ◽  
Pcr Analysis ◽  
Cdna Clones ◽  
Rt Pcr ◽  
Parenchymal Cells ◽  
Ultimobranchial Gland

Four types of calcitonin are produced in salmonid fish, although their functional diversity is almost unknown. To explore the significance of these isoforms, we have characterized salmon-type calcitonin (sCT) mRNAs in the rainbow trout (Oncorhynchus mykiss), and examined their tissue distribution. In addition to the previously isolated sCT-I cDNAs, two new forms of sCT cDNA were cloned from the ultimobranchial gland, and one of them (sCT-IV cDNA) was predicted to encode an N-terminal peptide of 80 amino acid residues, a putative cleavage site Lys-Arg, sCT-IV, a cleavage and amidation sequence Gly-Lys-Lys-Arg, and a C-terminal peptide of 18 amino acids. The sCT-IV precursor was 78% identical with the rainbow trout sCT-I precursors. The other cloned cDNA encoded a precursor for a novel CT, sCT-V. The sCT-V peptide was different from sCT-IV by only one amino acid residue: Val at position 8 in the latter was replaced by Met. The sCT-V precursor had 80 and 90% identity with the sCT-I and -IV precursors respectively. No cDNA clones were obtained for sCTs-II or -III.Tissue distribution of sCT-I, -IV and -V mRNAs was examined by RT-PCR and specific cleavage with restriction enzymes. An amplified fragment from sCT-I mRNA was detected not only in the ultimobranchial gland, but also in the gills, testis and ovary. RT-PCR analysis coupled to restriction digestion further revealed that sCT-IV mRNA was expressed in both the testis and the ultimobranchial gland. The expression sites of sCT-IV mRNA were localized to the Leydig cells of the testis and to the parenchymal cells of the ultimobranchial gland, by in situ hybridization histochemistry. Although the amino acid sequence of sCT-V peptide was nearly the same as that of sCT-IV, the sCT-V gene showed a much wider pattern of expression: the band amplified by RT-PCR was detected in all the tissues examined except the kidney, gills and blood cells. The sCT-V mRNA was shown to be localized in the parenchymal cells of the ultimobranchial gland, but not in other tissues at the cellular level, suggesting very low expression of sCT-V mRNA in those tissues. Our results show different patterns of tissue expression of three types of sCT genes in the rainbow trout, suggesting that sCTs-I, -IV and -V might differ in their local actions.

scholarly journals Myostatin inhibits myosatellite cell proliferation and consequently activates differentiation: evidence for endocrine-regulated transcript processing

2012 ◽  
Vol 215 (1) ◽  
pp. 177-187 ◽  
Author(s):  
Dilip K Garikipati ◽  
Buel D Rodgers
Keyword(s):  
Rainbow Trout ◽  
Gene Family ◽  
Muscle Growth ◽  
Cellular Growth ◽  
Negative Regulator ◽  
Differentiation Markers ◽  
Delayed Effects ◽  
Functional Conservation ◽  
Quiescent Cells ◽  
Transcript Processing

Myostatin is a potent negative regulator of muscle growth in mammals. Despite high structural conservation, functional conservation in nonmammalian species is only assumed. This is particularly true for fish due to the presence of several myostatin paralogs: two in most species and four in salmonids (MSTN-1a, -1b, -2a, and -2b). Rainbow trout are a rich source of primary myosatellite cells as hyperplastic muscle growth occurs even in adult fish. These cells were therefore used to determine myostatin's effects on proliferation whereas our earlier studies reported its effects on quiescent cells. As in mammals, recombinant myostatin suppressed proliferation with no changes in cell morphology. Expression of MSTN-1a was several fold higher than the other paralogs and was autoregulated by myostatin, which also upregulated the expression of key differentiation markers: Myf5, MyoD1, myogenin, and myosin light chain. Thus, myostatin-stimulated cellular growth inhibition activates rather than represses differentiation. IGF-1 stimulated proliferation but had minimal and delayed effects on differentiation and its actions were suppressed by myostatin. However, IGF-1 upregulated MSTN-2a expression and the processing of its transcript, which is normally unprocessed. Myostatin therefore appears to partly mediate IGF-stimulated myosatellite differentiation in rainbow trout. This also occurs in mammals, although the IGF-stimulated processing of MSTN-2a transcripts is highly unique and is indicative of subfunctionalization within the gene family. These studies also suggest that the myokine's actions, including its antagonistic relationship with IGF-1, are conserved and that the salmonid gene family is functionally diverging.

scholarly journals Circulating skeletal muscle related microRNAs profile in Piedmontese cattle during different age

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Rupal S. Tewari ◽  
Ugo Ala ◽  
Paolo Accornero ◽  
Mario Baratta ◽  
Silvia Miretti
Keyword(s):  
Skeletal Muscle ◽  
Expression Profiles ◽  
Muscle Growth ◽  
Age Groups ◽  
Negative Regulator ◽  
Small Rna Sequencing ◽  
Muscle Physiology ◽  
Sequencing Data ◽  
Double Muscle ◽  
Mirnas Expression

AbstractPiedmontese cattle is known for double-muscle phenotype. MicroRNAs (miRNAs) play important role as regulators in skeletal muscle physiological processes, and we hypothesize that plasma miRNAs expression profiles could be affected by skeletal muscle growth status related to age. Plasma samples of cattle were collected during four different ages from first week of life until the time of commercial end of the fattening period before slaughter. Small-RNA sequencing data analysis revealed the presence of 40% of muscle-related miRNAs among the top 25 highly expressed miRNAs and, 19 miRNAs showed differential expression too. Using qRT-PCR, we validated in a larger bovine population, miRNAs involved in skeletal muscle physiology pathways. Comparing new-born with the other age groups, miR-10b, miR-126-5p, miR-143 and miR-146b were significantly up-regulated, whereas miR-21-5p, miR-221, miR-223 and miR-30b-5p were significantly down-regulated. High expression levels of miR-23a in all the groups were found. Myostatin, a negative regulator of skeletal muscle hypertrophy, was predicted as the target gene for miR-23a and miR-126-5p and we demonstrated their direct binding. Correlation analysis revealed association between miRNAs expression profiles and animals’ weights along the age. Circulating miRNAs could be promising for future studies on their biomarker potentialities to beef cattle selection.

scholarly journals Influence of hyperthyroid conditions on gene expression in extraocular muscles of rats

2009 ◽  
Vol 37 (3) ◽  
pp. 231-238 ◽  
Author(s):  
Thomas S. Postler ◽  
Murat T. Budak ◽  
Tejvir S. Khurana ◽  
Neal A. Rubinstein
Keyword(s):  
Gene Expression ◽  
Thyroid Hormone ◽  
Protein Localization ◽  
Muscle Growth ◽  
Extraocular Muscles ◽  
Negative Regulator ◽  
Mrna Levels ◽  
Sprague Dawley ◽  
Wide Range ◽  
Canonical Pathways

Extraocular muscles (EOMs) are a highly specialized type of tissue with a wide range of unique properties, including characteristic innervation, development, and structural proteins. Even though EOMs are frequently and prominently affected by thyroid-associated diseases, little is known about the direct effects of thyroid hormone on these muscles. To create a comprehensive profile of changes in gene expression levels in EOMs induced by thyroid hormone, hyperthyroid conditions were simulated by treating adult Sprague-Dawley rats with intraperitoneal injections of the thyroid hormone 3,3′,5-triiodo-l-thyronine (T3); subsequently, microarray analysis was used to determine changes in mRNA levels in EOMs from T3-treated animals relative to untreated control animals. The expression of 468 transcripts was found to be significantly altered, with 466 of these transcripts downregulated in EOMs from T3-treated animals. The biological processes into which the affected genes could be grouped included cellular metabolism, transport, biosynthesis, protein localization, and cell homeostasis. Moreover, 15 distinct biochemical canonical pathways were represented among the genes with altered transcription levels. Strikingly, myostatin ( Gdf8), a potent negative regulator of muscle growth, was found to be strongly downregulated in EOMs from T3-treated animals. Together, these findings suggest that pathological concentrations of thyroid hormone have a unique effect on gene expression in EOMs, which is likely to play a hitherto neglected role in thyroid-associated ophthalmopathies.

scholarly journals Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate acyltransferases and their regulation by PPARα in murine heart

2005 ◽  
Vol 385 (2) ◽  
pp. 469-477 ◽  
Author(s):  
Biao LU ◽  
Yan J. JIANG ◽  
Yaling ZHOU ◽  
Fred Y. XU ◽  
Grant M. HATCH ◽  
...  
Keyword(s):  
Expression Profiles ◽  
Tissue Expression ◽  
In Vitro Transcription ◽  
Amino Acid Sequences ◽  
Peroxisome Proliferator ◽  
Mrna Levels ◽  
Wild Type ◽  
Peroxisome Proliferator Activated Receptor

AGPAT (1-acyl-sn-glycerol 3-phosphate acyltransferase) exists in at least five isoforms in humans, termed as AGPAT1, AGPAT2, AGPAT3, AGPAT4 and AGPAT5. Although they catalyse the same biochemical reaction, their relative function, tissue expression and regulation are poorly understood. Linkage studies in humans have revealed that AGPAT2 contributes to glycerolipid synthesis and plays an important role in regulating lipid metabolism. We report the molecular cloning, tissue distribution, and enzyme characterization of mAGPATs (murine AGPATs) and regulation of cardiac mAGPATs by PPARα (peroxisome-proliferator-activated receptor α). mAGPATs demonstrated differential tissue expression profiles: mAGPAT1 and mAGPAT3 were ubiquitously expressed in most tissues, whereas mAGPAT2, mAGPAT4 and mAGPAT5 were expressed in a tissue-specific manner. mAGPAT2 expressed in in vitro transcription and translation reactions and in transfected COS-1 cells exhibited specificity for 1-acyl-sn-glycerol 3-phosphate. When amino acid sequences of five mAGPATs were compared, three highly conserved motifs were identified, including one novel motif/pattern KX2LX6GX12R. Cardiac mAGPAT activities were 25% lower (P<0.05) in PPARα null mice compared with wild-type. In addition, cardiac mAGPAT activities were 50% lower (P<0.05) in PPARα null mice fed clofibrate compared with clofibrate fed wild-type animals. This modulation of AGPAT activity was accompanied by significant enhancement/reduction of the mRNA levels of mAGPAT3/mAGPAT2 respectively. Finally, mRNA expression of cardiac mAGPAT3 appeared to be regulated by PPARα activation. We conclude that cardiac mAGPAT activity may be regulated by both the composition of mAGPAT isoforms and the levels of each isoform.

cDNA sequence and tissue expression of bovine vacuolar H(+)-ATPase M(r) 70,000 subunit

1992 ◽  
Vol 263 (1) ◽  
pp. F171-F174 ◽  
Author(s):  
M. M. Marushack ◽  
B. S. Lee ◽  
K. Masood ◽  
S. Gluck
Keyword(s):  
Protein Sequence ◽  
Adenosine Triphosphatase ◽  
Tissue Expression ◽  
Amino Acid Identity ◽  
Cdna Clones ◽  
Mrna Levels ◽  
Coding Region ◽  
Kidney Medulla ◽  
Relative Molecular Weight ◽  
Low Levels

cDNA clones encoding the 70,000 relative molecular weight (M(r)) subunit of the bovine vacuolar proton-adenosine triphosphatase (H(+)-ATPase) were isolated, and a total length of 3.1 kb in overlapping clones from bovine kidney and brain libraries was sequenced. The cDNA contains a 1.9-kb coding region and yields a deduced protein sequence of 618 amino acids. The subunit sequence has 50% amino acid identity with the corresponding subunit from yeast, carrot, and Neurospora vacuolar H(+)-ATPases. The internal regions of the protein are most highly conserved, whereas the NH2- and COOH-terminals exhibit variability. mRNA levels of the M(r) 70,000 subunit were examined in multiple bovine tissues and were found to be expressed at highest levels in kidney medulla and cortex, at moderate levels in brain and adrenal gland, and at low levels in liver, muscle, and heart.

scholarly journals Function of the Porcine TRPC1 Gene in Myogenesis and Muscle Growth

Cells ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 147
Author(s):  
Yu Fu ◽  
Peng Shang ◽  
Bo Zhang ◽  
Xiaolong Tian ◽  
Ruixue Nie ◽  
...  
Keyword(s):  
Transient Receptor Potential ◽  
Growth Traits ◽  
Expression Profiles ◽  
Muscle Growth ◽  
Receptor Potential ◽  
Transient Receptor Potential Channel ◽  
Nucleotide Polymorphisms ◽  
Pig Breeds ◽  
Muscle Tissues ◽  
Transient Receptor

In animals, muscle growth is a quantitative trait controlled by multiple genes. Previously, we showed that the transient receptor potential channel 1 (TRPC1) gene was differentially expressed in muscle tissues between pig breeds with divergent growth traits base on RNA-seq. Here, we characterized TRPC1 expression profiles in different tissues and pig breeds and showed that TRPC1 was highly expressed in the muscle. We found two single nucleotide polymorphisms (SNPs) (C-1763T and C-1604T) in TRPC1 that could affect the promoter region activity and regulate pig growth rate. Functionally, we used RNAi and overexpression to illustrate that TRPC1 promotes myoblast proliferation, migration, differentiation, fusion, and muscle hypertrophy while inhibiting muscle degradation. These processes may be mediated by the activation of Wnt signaling pathways. Altogether, our results revealed that TRPC1 might promote muscle growth and development and plays a key role in Wnt-mediated myogenesis.

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