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Number of Brahman and Angus cattle by gender, HGP-status, and genotype (number of favorable alleles) for calpain-system gene markers in the New South Wales (NSW) and Western Australian (WA) experiments

Number of Brahman and Angus cattle by gender, HGP-status, and genotype (number of favorable alleles) for calpain-system gene markers in the New South Wales (NSW) and Western Australian (WA) experiments

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The objective of this study was to investigate whether single nucleotide polymorphisms (SNP) in the calpain 1 (CAPN1), calpain 3 (CAPN3) and calpastatin (CAST) genes, which have been shown to be associated with shear force and tenderness differences in the skeletal muscle of cattle, contribute to phenotypic variation in muscle tenderness by modulat...

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Context 1
... design for the Angus controls in NSW included contrasts of HGP status and gender, and was also chosen to maximize the accuracy of estimating the effect of CAPN1-316 marker status (Robinson et al., 2007). The number of Brahman and Angus animals within each allelic status for the 4 calpain system gene markers and within gender and HGP category in the NSW experiment are also presented in Table 1. ...
Context 2
... design for Angus cattle in- cluded a contrast of HGP status and was also chosen to maximize the accuracy of estimating CAPN1-316 mark- er effect. The number of Brahman and Angus animals within each allelic status for the 4 calpain system gene markers and within HGP category in the WA experiment are also shown in Table 1. Brahman cattle were sourced at weaning (6 to 8 mo of age) from 4 producers in the Northern Agricultural region of WA, and the Angus cattle from a commercial herd in the south-west of WA. ...
Context 3
... 5% higher of "total" CAST mRNA were detected in the LLM of HGP-implanted cattle than in non-implanted cattle (P = 0.01; Table 4 and 7). Table 4. Significance (P-values) of the terms fitted in the linear models 1 Dependent variable 2 Terms fitted (P-values) 2 Abbreviated mRNA transcript identifiers for CALP1 = calpain 1; CALP3 = calpain 3; CAST = 'total' calpastatin; RPLP0 = Ribosomal Protein, Large, P0; CASTII = type II calpastatin splice variant; CASTIII (ex3) = type III calpastatin splice variant containing exon 3; CASTIII (ex2-ex4) = type III calpastatin splice variant lacking exon 3; CASTpA1 = calpastatin proximal polyadenylation variant; and CASTpA2 = calpastatin distal polyadenylation variant. 3 The initial phase of the experiment screened 152 cattle from NSW and 191 cattle from WA. ...

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... The association between reduced levels of calpastatin protein in Longissimus lumborum from Brahman and the occurrence of the favorable allele (CAST:c.2832 A > G polymorphism) also points to its association with regulatory sequences which have a role in the post-transcriptional regulation of CAST mRNA transcripts (Nattrass et al., 2014). One available and promising tool is the use of calpastatin gene marker to assisted selection, which has no negative impact on other production or carcass characteristics (Cafe et al., 2010). ...
... The inhibitory effect of calpastatin is used to predict beef quality by the calpastatin activity (Geesink et al., 2006;Grant et al., 2005); however, it is necessary to consider the significant heterogeneity between calpastatin variants generated by alternative splicing (Raynaud et al., 2005). This variability is associated to the calpastatin inhibitory activity (Nattrass et al., 2014) and can be identified by their mRNAs and by the transcriptional activity of calpastatin (CAST) gene promoters. Different responses to stimuli among species may be partly responsible for variations in CAST expression (species, breeds, and individuals). ...
... Proteins in the calpain system, including calpastatin, have long half-lives (Zhang, Lane, & Mellgren, 1996); therefore, this condition is compatible with greater protein degradation, lower WBSF, and greater MFI associated to lower CAPN1 and greater CAST II mRNA abundances. The difference in calpastatin between biological types that reduces tenderness is associated to CAST gene allele modification (Curi et al., 2010) and, although genetic associations have not been addressed in our study, polymorphism in the CAST gene seems to be related to alterations of mRNA levels, mainly CAST II, as reported by Nattrass et al. (2014). These authors verified that animals with one or two favorable alleles to tenderness showed low mRNA levels to the CAST II variant in comparison to animals without favorable alleles, which in turn presented a 14% increase in mRNA levels and reduced tenderness. ...
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... Twenty-one isoforms of the human CAST gene are included in RefSeq (https ://www.ncbi.nlm. nih.gov/gene/831#), and similarly, several isoforms of bovine CAST [65] are found in RefSeq (https ://www. ncbi.nlm.nih.gov/gene/28103 ...
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... Four alternative promoters direct the expression of four different transcripts isolated from different tissues, named Type I, II, III, and IV, which differ in their 5´ ends (Raynaud et al., 2005a). Moreover, differences in transcript length can also be originated by alternative polyadenylation sites and alternative exon splicing (Cong et al., 1998;Raynaud et al., 2005b;Nattrass et al., 2014). ...
... There is still little information about the expression of CAST isoforms with different polyadenylation sites in different muscles or breeds, and its potential effects on beef quality traits. Nattrass et al. (2014) quantified two polyadenylation variants of CAST (those designated here as short and long, respectively) in the longissimus lumborum muscle of Angus and Brahman steers. The steers had been genotyped for the CAST:c.2832 ...
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Calpastatin activity has a key role in the tenderization process that occurs during post-mortem storage of meat under refrigerated conditioning. The regulation of calpastatin (CAST) expression is highly complex, the gene has four putative promoters and at least three different polyadenylation sites, and it is also alternatively spliced. We investigated the presence of alternative polyadenylation (APA) isoforms of CAST transcripts in three muscles (infraspinatus, triceps brachii and semitendinosus) of two bovine breeds (Angus and Brahman). The 3´ RACE-PCR was used to specifically amplify the different APA sites. The amplified fragments were cloned and sequenced. Sequencing confirmed the existence of three expected polyadenylation sites corresponding to short, medium and long polyadenylated transcripts. Also, transcripts with a novel APA site were found in the three muscles of both breeds. Because the same APAs isoforms were found between muscles and breeds, we could hypothesize a possible contribution to the relative abundance of different isoforms, probably in coordination with promoter preference and alternative splicing. This knowledge would be useful in the design of future experiments to analyze differential expression of CAST isoforms and their contribution to the definition of beef tenderness.
... Four alternative promoters direct the expression of four different transcripts isolated from different tissues, named Type I, II, III, and IV, which differ in their 5´ ends (Raynaud et al., 2005a). Moreover, differences in transcript length can also be originated by alternative polyadenylation sites and alternative exon splicing (Cong et al., 1998;Raynaud et al., 2005b;Nattrass et al., 2014). ...
... There is still little information about the expression of CAST isoforms with different polyadenylation sites in different muscles or breeds, and its potential effects on beef quality traits. Nattrass et al. (2014) quantified two polyadenylation variants of CAST (those designated here as short and long, respectively) in the longissimus lumborum muscle of Angus and Brahman steers. The steers had been genotyped for the CAST:c.2832 ...
... The favorable A allele has been shown to produce a more energetically unstable mRNA (Leal-Gutiérrez, et al., 2018). This is substantiated by reports of Brahman animals with the AA genotype having approximately 14% lower mRNA expression than the GG genotype (Nattrass et al. 2014), suggesting less calpastatin protein being produced and therefore less postmortem µ-calpain inhibition. ...
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Beef palatability is a complex concept and could be described through an array of features such as tenderness, juiciness and flavor traits. Improving the eating experience when consuming beef and the ability to accurately inform the consumers of the expected eating quality when the product is purchased are critical challenges. In this review, we discuss the current knowledge of quantitative and molecular genetic aspects of palatability and discuss implications of genetic manipulation for the cattle industry.
... Niciura et al (48) encontraron que la expresión del gen CAST fue dos veces mayor en el músculo de los animales homocigotos para el genotipo GG con respecto a los animales con genotipo AG en el marcador CAST T1. Natrass et al (49) determinaron esta relación en ganado Bos indicus y Bos taurus y encontraron diferencias en la expresión de los genes de la CAPN1 y la CAST entre las variantes favorables y desfavorables de estos marcadores (marcadores CAPN1 4751 y CAST T1), sugiriendo un efecto polimórfico en la expresión génica. Estos hallazgos sugieren que las diferencias en la terneza de la carne explicadas por los marcadores genéticos podrían ser una consecuencia de la alteración en los niveles de ARNm, actividad, velocidad y (o) extensión de la proteólisis post mortem en el músculo esquelético. ...
... Niciura et al (48) found that CAST was expressed twice as much in muscle of homozygous GG as in heterozygous AG in the CAST T1 marker. Natrass et al (49) investigated this relationship in Bos indicus and Bos taurus cattle and found differences in CAPN1 and CAST gene expression between favourable and unfavourable allelic variants of these genes (CAPN1 4751 and CAST T1 markers), indicating a polymorphic effect on gene expression. These findings suggest that differences in tenderness explained by gene markers could be a consequence of the alteration in their mRNA levels, protein activity and rate and (or) the extent of postmortem proteolysis in skeletal muscle. ...
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a terneza de la carne es considerada como el atributo de mayor importancia en el concepto de calidad de carne. El proceso de tenderización de la carne post mortem es principalmente el resultado de la degradación de proteínas clave de las fibras musculares, mediado por las proteasas del sistema calpaína. Este sistema proteico está compuesto por tres moléculas: dos proteasas calcio-dependientes y su inhibidor específico. Numerosos estudios han demostrado que el sistema calpaína desempeña un papel central en la proteólisis postmortem y en la tenderización de la carne. El objetivo de esta revisión es describir los últimos descubrimientos bioquímicos y moleculares en relación con este sistema proteolítico y su relación con la terneza de la carne bovina. Se describen los hallazgos de polimorfismos de ADN y de expresión de ARNm y proteínas, como herramientas para predecir la terneza de la carne. La comprensión de las bases moleculares de la tenderización de la carne puede ser de utilidad para la industria cárnica, permitiendo la modificación de las prácticas de manipulación antes del sacrificio y los tratamientos post mortem, mejorando la calidad de la carne bovina.
... However, the mRNA expression of genes does not always explain the differences in myofibrillar proteolysis in skeletal muscle of Bos taurus and Bos indicus cattle ( Giusti et al. 2013). Thus, due to inconsistencies regarding mRNA levels of CAPN1 and myofibrillar proteolysis of skeletal muscle in Bos taurus and Bos indicus, a post-transcriptional regulatory mechanism such as a change in the abundance of an alternative polyadenylated variant of the CAST transcript has been proposed ( Nattrass et al. 2014). However, the molecular factors underlying the differences in proteolysis between Bos taurus and Bos indicus animals are still not fully understood. ...
... The next question to be answered is what causes the differences in myofibrillar proteolysis in skeletal muscle of Bos taurus and Bos indicus. To answer that question a great body of evidence has been amassed to evaluate the mRNA abundance and/or the allelic as well as genotype frequencies of CAPN1 and CAST and their polymorphism to assess the possible mechanisms related to myofibrillar proteolysis in the skeletal muscle ( Curi et al. 2009Curi et al. , 2010Giusti et al. 2013;Nattrass et al. 2014). Although most of these studies were developed to investigate beef tenderness, their results may reflect the effects of these genes on proteolysis in a live skeletal muscle tissue. ...
... Although most of these studies were developed to investigate beef tenderness, their results may reflect the effects of these genes on proteolysis in a live skeletal muscle tissue. Nattrass et al. (2014) speculated that the level of gene expression of CAPN1 and CAST would ultimately influence the activity of the proteins encoded by these genes (Calpain and Calpastatin), thus leading to the difference in the extent of skeletal muscle proteolysis. However, a genome scan performed by Tizioto et al. (2013) found a small effect of single nucleotide polymorphisms (SNPs) in CAPN1 and CAST in proteolysis and consequently Warner-Bratzler shear force on beef from Nellore cattle. ...
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... Pleiotropy could be important both to understand genetic architecture of complex traits and also to characterize more completely the underlying biology and phenotypic consequences of associated loci. However, we did not detect any SNP on CAST or CAPN1, which regulates calpastatin expression in bovine skeletal muscle, and were strongly associated with SF as previous report (Nattrass et al. 2014;Tizioto et al. 2014). ...
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