Degradation of troponin-T associated with calpain/ calpastatin genes expression in native Thai beef cattle fed different levels of energy
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Abstract
The influence of dietary energy level on the degradation of troponin-T protein and expression of calpain and calpastatin genes in native Thai cattle was determined. Eighteen steers (at 200 days old and average body weight of 100 ± 20 kg) were randomly assigned to 3 dietary treatment groups of different metabolizable energy: Treatment 1 [(8.9 MJ/ kg DM; n=6), Treatment 2 (9.7 MJ/kg DM; n=6) and Treatment 3 (10.5 MJ/kg DM; n=6)]. The diets were in the form of fermented total mixed ration (FTMR). At the end of 520 days of feeding, the steers attained 300 ± 10 kg BW at slaughter. The Longissimus dorsi m. samples collected within 2 d postmortem were further aged for 14 d for the troponin-T degradation immunoblot analysis while, the CAPN1, CAPN2, and CAST genes expression analyses only used samples at 2 d postmortem. The relative bands intensities of intact (37 kDa) and degraded troponin-T (30 kDa) were unaffected by the dietary treatments (p>0.05). Higher 37 kDa (p<0.01) and 30 kDa (p<0.001) troponin-T proteins expression were noted at 2 d and 14 d post-mortem, respectively. The CAPN1, CAPN2, and CAST genes expression remained unaffected (p>0.05) by the dietary treatment. Nonetheless, significant associations were observed between CAPN2 and CAST genes expression (r=0.93; p<0.0001), and between CAPN1 gene expression and 30 kDa troponin-T proteins expression at 14 d postmortem (r=0.58; p<0.05). This study concluded that neither troponin-T proteins nor calpain/ calpastatin genes expression were influenced by dietary energy levels in fattened native Thai cattle. The associations between CAPN2 and CAST genes expression, and between CAPN1 gene expression and 30 kDa troponin-T proteins expression at 14 d postmortem suggest the involvement of CAPN1 in myofibrillar proteolysis during the 14 d postmortem ageing of Longissimus dorsi m. in native Thai cattle.
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References
Chaosap, C., Parr, T. and Wiseman, J. (2011). Effect of compensatory growth on forms of glycogen, post-mortem proteolysis, and meat quality in pigs. Journal of Animal Science. 89:2231-2242.
Harris, S. E., Huff-Lonergan, E., Lonergan, S. M., Jones, W. R. and Rankins, D. (2001). Antioxidant status affects color stability and tenderness of calcium chlorideinjected beef. Journal of Animal Science. 79:666-677.
Herd, R. M. and Bisho, S. C. (2000). Genetic variation in residual feed intake and its association with other production traits in british hereford cattle. Livestock Production Science. 63:111-119.
Ho, C. Y., Stromer, M. H. and Robson, R. M. (1994). Identification of 30 kDa polypeptide in postmortem skeletal muscle as a degradation product of troponin–T. Biochimie. 76:369-375.
Huffman, K. L., Miller, M. F., Hoover, L. C., Wu, C. K., Brittin, H. C. and Ramsey, C. B. (1996). Effect of beef tenderness on consumer satisfaction with steaks consumed in the home and restaurant. Journal of Animal Scicence. 74:91-97.
Huff-Lonergan, E., Mitsuhashi, T., Beekman, D. D., Parrish F. C. Jr., Olson, D. G. and Robson, R. M. (1996). Proteolysis of specific muscle structural proteins by mu-calpain at low ph and temperature is similar to degradation in postmortem bovine muscle. Journal of Animal Scicence. 74:993-1008.
Koohmaraie, M. (1992). The role of Ca2+-dependent proteasesin(calpain)postmortem proteolysis and meat tenderness. Biochimie. 74:239-245.
Koohmaraie, M. and Geesink, G. H. (2006). Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain syste. Meat Science. 74: 34-43.
Lomiwes, D., Reis, M. M., Wiklund, E., Young, O. A. and North, M. (2010). Near infrared spectroscopy as an on-line method to quantitatively determine glycogen and predict ultimate ph in pre rigor bovine M. longissimus dorsi. Meat Science. 86:999-1004.
Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J. (1951). Protein measurement with the folin fhenol reagent. Journal of Biological Chemistry. 193:265-275.
Rivero-Gutierrez, B., Anzola, A., Martinez-Augustin, O. and Sanchez de Medina, F. (2014). Stain-free detection as loading control alternative to Ponceau and housekeeping protein immunodetection in Western blotting. Analytical Biochemistry. 467:1-3.
SAS Institute Inc. 2003. SAS/STAT User’s Guide: Version 9.1.SAS Institute Inc,. Cary, NC, USA.
Steen, D., Claeys, E., Uytterhaegen, L., De Smetb, S. and Demeyer, D. (1997). Early post-mortem conditions and the calpain/calpastatin system in relation to tenderness of double-muscled beef. Meat Science. 45:307-319.
Sun, X., Chen, K. J., Berg, E. P., Newman, D. J., Schwartz, C. A., Keller, W. L. and Maddock Carlin, K. R. (2014). Prediction of troponin-t degradation using color image texture features in 10 d aged beef longissimus steaks. Meat Science. 96:837-842.
Xiong, Y. L., Moody, W. G., Blanchard, S.P., Liu, G. and Burris, W.R. (1996). Postmortem proteolytic and organoleptic changes in hot-boned muscle from grass and grain-fed zeranol-implanted cattle. Food Research International. 29:27-34.
