Comparative study of weaning pigs' muscle proteins using two-dimensional electrophoresis

Authors

  • Anastasia Akhremko . M. Gorbatov Federal Research Center for Food Systems of RAS, Experimental-clinical research laboratory of bioactive substances of animal origin, Talalikhina st., 26, 109316, Moscow, Russia, Tel.: +79152379497 https://orcid.org/0000-0002-0211-8171
  • Liliya Fedulova V. M. Gorbatov Federal Research Center for Food Systems of RAS, Experimental-clinical research laboratory of bioactive substances of animal origin, Talalikhina st., 26, 109316, Moscow, Russia, Tel.: +74956769211 https://orcid.org/0000-0003-3573-930X

DOI:

https://doi.org/10.5219/1449

Keywords:

2-DE, muscle, protein, two-dimensional electrophoresis, pig, piglet

Abstract

The proteostasis system of animals, including various types of protein modification during the growth stage, leads to an almost incomprehensible number of possible forms of protein, and each can regulate numerous functions. In the presented work, the composition of muscle tissue protein from different portions of piglets was studied to understand the main muscle protein formation. Comparative analysis of weaned piglets' main muscle protein from l. dorsi, biceps femoris, and brachiocephalicus were analyzed using two-dimensional electrophoresis. Changes in the staining intensity of protein fractions inherent in different muscles were revealed. As part of this work, candidate groups of pig muscle proteins have been selected. Eleven protein spots were revealed for the longest muscle of the back, and seven for the biceps; the muscles of the neck are characterized by indicators of low protein fraction volume. Among the proteins found, myosin light chains, phosphoglycerate mutase, troponins, and adenylate kinase is most likely present. The obtained results of protein identification in muscle tissues, obtained during the intensive growth period, will allow a more detailed understanding of protein regulation, function, and interactions in complex biological systems, which will subsequently be significantly important for biomonitoring health and predicting farm animals productivity.

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References

Benešová, L., Golian, J., Martišová, P., Semjon, B., Zajác, P., Čapla, J., Vlčko, T. 2019. Authentication and preference mapping of ham. Potravinarstvo Slovak Journal of Food Sciences, vol. 13, no. 1, p. 1051-1056. https://doi.org/10.5219/1263 DOI: https://doi.org/10.5219/1263

Bermúdez, R., Franco, D., Carballo, J., Sentandreu, M. Á., Lorenzo, J. M. 2014. Influence of muscle type on the evolution of free amino acids and sarcoplasmic and myofibrillar proteins through the manufacturing process of Celta dry-cured ham. Food Research International, vol. 56, p. 226-235. https://doi.org/10.1016/j.foodres.2013.12.023 DOI: https://doi.org/10.1016/j.foodres.2013.12.023

Fedulova, L., Elkina, A., Vasilevskaya, E., Barysheva, E. 2018. Identification of tissue-specific proteins of immunocompetent organs of Sus scrofa isolated in deuterium depleted medium. Medical Science, vol. 22, no. 94, p. 509-513.

Gorlov, I., Slozhenkina, M., Mosolov, A., Baranikov, V., Nikolaev, D., Chernyak, A., Sherstyuk, B., Krotova, O. 2020. Nutritional and biological value of pork obtained from animals fed with lysine and methionine. Potravinarstvo Slovak Journal of Food Sciences, vol. 14, p. 112-117. https://doi.org/10.5219/1192 DOI: https://doi.org/10.5219/1192

Grove, H., Hollung, K., Uhlen, A. K., Martens, H., Faergestad, E. M. 2006. Challenges related to analysis of protein spot volumes from two-dimensional gel electrophoresis as revealed by replicate gels. Journal of Proteome Research, vol. 5, no. 12, p. 3399-3410. https://doi.org/10.1021/pr0603250 DOI: https://doi.org/10.1021/pr0603250

Grujić, R., Savanović, D. 2018. Analysis of myofibrillar and sarcoplasmic proteins in pork meat by capillary gel electrophoresis. Foods and Raw Materials, vol. 6 no. 2, p. 421-428. https://doi.org/10.21603/2308-4057-2018-2-421-4281 DOI: https://doi.org/10.21603/2308-4057-2018-2-421-428

He, J., Yang, H., Wei, W., Chu, W., Yu, S., Tian, Y., Peng, F., Liu, H., Zhang, Z., Chen, J. 2016. The c.–360 T> C mutation affects PGAM2 transcription activity and is linked with the water holding capacity of the longissimus lumborum muscle in pigs. Meat Science, vol. 122, p. 139-144. https://doi.org/10.1016/j.meatsci.2016.07.023 DOI: https://doi.org/10.1016/j.meatsci.2016.07.023

Chen, J., Su, W., Kang, B., Jiang, Q., Zhao, Y., Fu, C., Yao, K. 2018. Supplementation with α-ketoglutarate to a low-protein diet enhances amino acid synthesis in tissues and improves protein metabolism in the skeletal muscle of growing pigs. Amino Acids, vol. 50, no. 11, p. 1525-1537. https://doi.org/10.1007/s00726-018-2618-3 DOI: https://doi.org/10.1007/s00726-018-2618-3

Chernukha, I., Fedulova, L., Kotenkova, E., Akhremko, A. 2018. Hypolipidemic action of the meat product: in vivo study. Potravinarstvo Slovak Journal of Food Sciences, vol. 12, no. 1, p. 566-569. https://doi.org/10.5219/959 DOI: https://doi.org/10.5219/959

Kim, G.-D., Seo, J.-K., Yum, H.-W., Jeong, J.-Y., Yang, H.-S. 2017. Protein markers for discrimination of meat species in raw beef, pork and poultry and their mixtures. Food Chemistry, vol. 217, p. 163-170. https://doi.org/10.1016/j.foodchem.2016.08.100 DOI: https://doi.org/10.1016/j.foodchem.2016.08.100

Kim, J. H., Seong, P. N., Cho, S. H., Park, B. Y., Hah, K. H., Yu, L. H., Lim, D. G., Hwang, I. H., Kim, D. H., Lee, J. M., Ahn, C. N. 2008. Characterization of nutritional value for twenty-one pork muscles. Asian-Australasian Journal of Animal Sciences, vol. 21, no. 1, p. 138-143. https://doi.org/10.5713/ajas.2008.70208 DOI: https://doi.org/10.5713/ajas.2008.70208

Kovaleva, M., Kovalev, L., Lisitskaya K. V., Eremina, L. S., Ivanov, A., Krakhmaleva, I., Sadykhov E., Shishkin, S. 2013. Muscle organs proteomics multi-level database. FEBS Journal, vol. 280, no. 1, p. 488.

Lee, H. Y., Kim, J. M., Byun, M. J., Kang, K. S., Kim, T. H., Hong, K. C., Lee, K. T. 2011. Structure and polymorphisms of the 5′ regulatory region of porcine adenylate kinase 3-like 1 gene and effect on trait of meat quality. Genes & Genomics, vol. 33, no. 2, p. 147. https://doi.org/10.1007/s13258-010-0091-9 DOI: https://doi.org/10.1007/s13258-010-0091-9

Lepczynski, A., Herosimczyk, A., Ozgo, M., Barszcz, M., Taciak, M., Skomial, J. 2019. Modification of ileal proteome in growing pigs by dietary supplementation with inulin or dried chicory root. Journal of Animal and Feed Sciences, vol. 28, p. 177-186. https://doi.org/10.22358/jafs/109518/2019 DOI: https://doi.org/10.22358/jafs/109518/2019

Li, X., Xie, S., Qian, L., Cai, C., Bi, H., Cui, W. 2020. Identification of genes related to skeletal muscle growth and development by integrated analysis of transcriptome and proteome in myostatin-edited Meishan pigs. Journal of Proteomics, vol. 213, p. 103628. https://doi.org/10.1016/j.jprot.2019.103628 DOI: https://doi.org/10.1016/j.jprot.2019.103628

Liu, J., He, J., Yu, J., Mao, X., Zheng, P., Huang, Z., Yu, B., Chen, D. 2014. Birth weight alters the response to postnatal high-fat diet-induced changes in meat quality traits and skeletal muscle proteome of pigs. British Journal of Nutrition, vol. 111, no. 10, p. 1738-1747. https://doi.org/10.1017/S0007114513004431 DOI: https://doi.org/10.1017/S0007114513004431

Matsumoto, H., Haniu, H., Kurien, B. T., Komori, N. 2019. Two-Dimensional Gel Electrophoresis by Glass Tube-Based IEF and SDS-PAGE. In Kurien B., Scofield R. Electrophoretic Separation of Proteins. New York, USA : Humana Press, vol 1855, p. 107-113. ISBN 978-1-4939-8793-1. https://doi.org/10.1007/978-1-4939-8793-1_11 DOI: https://doi.org/10.1007/978-1-4939-8793-1_11

Mitra, B., Lametsch, R., Akcan, T., Ruiz-Carrascal, J. 2018. Pork proteins oxidative modifications under the influence of varied time-temperature thermal treatments: A chemical and redox proteomics assessment. Meat Science, vol. 140, p. 134-144. https://doi.org/10.1016/j.meatsci.2018.03.011 DOI: https://doi.org/10.1016/j.meatsci.2018.03.011

Montowska, M., Pospiech, E. 2012. Myosin light chain isoforms retain their species‐specific electrophoretic mobility after processing, which enables differentiation between six species: 2DE analysis of minced meat and meat products made from beef, pork and poultry. Proteomics, vol. 12, no. 18, p. 2879-2889. https://doi.org/10.1002/pmic.201200043 DOI: https://doi.org/10.1002/pmic.201200043

Mora, L., Calvo, L., Escudero, E., Toldrá, F. 2016. Differences in pig genotypes influence the generation of peptides in dry-cured ham processing. Food Research International, vol. 86, p. 74-82. https://doi.org/10.1016/j.foodres.2016.04.023 DOI: https://doi.org/10.1016/j.foodres.2016.04.023

Mora, L., Gallego, M., Toldrá, F. 2018. New approaches based on comparative proteomics for the assessment of food quality. Current Opinion in Food Science, vol 22, p. 22-27. https://doi.org/10.1016/j.cofs.2018.01.005 DOI: https://doi.org/10.1016/j.cofs.2018.01.005

Murgiano, L., D’Alessandro, A., Egidi, M. G., Crisa, A., Prosperini, G., Timperio, A. M., Valentini, A., Zolla, L. 2010. Proteomics and transcriptomics investigation on longissimus muscles in Large White and Casertana pig breeds. Journal of Proteome Research, vol. 9, no. 12, p. 6450-6466. https://doi.org/10.1021/pr100693h DOI: https://doi.org/10.1021/pr100693h

O'Donovan, C., Martin, M. J., Gattiker, A., Gasteiger, E., Bairoch, A., Apweiler, R. 2002. High-quality protein knowledge resource: SWISS-PROT and TrEMBL. Briefings in bioinformatics, vol. 3, no. 3, p. 275-284. https://doi.org/10.1093/bib/3.3.275 DOI: https://doi.org/10.1093/bib/3.3.275

Oliván, M., Fernández-Suárez, V., Díaz-Martínez, F., Sierra, V., Coto-Montes, A., de Luxán-Delgado, B., Peña, R., Bassols, A., Fàbrega, E., Dalmau, A., Velarde, A. 2015. Identification of biomarkers of stress in meat of pigs managed under different mixing treatments. Biotechnology Journal International, vol. 11, no. 1, p. 1-13. https://doi.org/10.9734/BBJ/2016/22402 DOI: https://doi.org/10.9734/BBJ/2016/22402

Paredi, G., Mori, F., de Marino, M. G., Raboni, S., Marchi, L., Galati, S., Buschini, A., Fiego, D. P., Mozzarelli, A. 2019. Is the protein profile of pig Longissimus dorsi affected by gender and diet? Journal of Proteomics, vol. 206, p. 103437. https://doi.org/10.1016/j.jprot.2019.103437 DOI: https://doi.org/10.1016/j.jprot.2019.103437

Purslow, P. P. 2017. The structure and growth of muscle. In Toldra, F. Lawrie´s Meat Science. Cambridge, UK : Woodhead Publishing, p. 49-97. ISBN-13 978-0-08-100697-9. https://doi.org/10.1016/B978-0-08-100694-8.00003-0 DOI: https://doi.org/10.1016/B978-0-08-100694-8.00003-0

Scheffler, T. L., Park, S., Gerrard, D. E. 2011. Lessons to learn about postmortem metabolism using the AMPKγ3R200Q mutation in the pig. Meat Science, vol. 89, no. 3, p. 244-250. https://doi.org/10.1016/j.meatsci.2011.04.030 DOI: https://doi.org/10.1016/j.meatsci.2011.04.030

Spoel, S. H. 2018. Orchestrating the proteome with post-translational modifications. Journal of Experimental Botany, vol. 69, no. 19, p. 4499-4503. https://doi.org/10.1093/jxb/ery295 DOI: https://doi.org/10.1093/jxb/ery295

Welzenbach, J., Neuhoff, C., Heidt, H., Cinar, M. U., Looft, C., Schellander, K., Tholen, E., Große-Brinkhaus, C. 2016. Integrative analysis of metabolomic, proteomic and genomic data to reveal functional pathways and candidate genes for drip loss in pigs. International Journal of Molecular Sciences, vol. 17, no. 9, p. 1426. https://doi.org/10.3390/ijms17091426 DOI: https://doi.org/10.3390/ijms17091426

Yang, H., Xu, X. L., Ma, H. M., Jiang, J. 2016. Integrative analysis of transcriptomics and proteomics of skeletal muscles of the Chinese indigenous Shaziling pig compared with the Yorkshire breed. BMC genetics, vol. 17, no. 1, p. 80. https://doi.org/10.1186/s12863-016-0389-y DOI: https://doi.org/10.1186/s12863-016-0389-y

Zhou, C. Y., Tang, C. B., Wang, C., Dai, C., Bai, Y., Yu, X. B., Li, C-B., Xu, X-L., Zhou, G-H., Cao, J. X. 2020. Insights into the evolution of myosin light chain isoforms and its effect on sensory defects of dry-cured ham. Food Chemistry, vol. 315, p. 126318. https://doi.org/10.1016/j.foodchem.2020.126318 DOI: https://doi.org/10.1016/j.foodchem.2020.126318

Zia, Q., Alawami, M., Mokhtar, N. F. K., Nhari, R. M. H. R., Hanish, I. 2020. Current Analytical Methods for Porcine Identification in Meat and Meat Products. Food Chemistry, vol. 324, p. 126664. https://doi.org/10.1016/j.foodchem.2020.126664 DOI: https://doi.org/10.1016/j.foodchem.2020.126664

Zou, C., Li, J., Luo, W., Li, L., Hu, A., Fu, Y., Hou, Y., Li, C. 2017. Transcriptome analysis reveals long intergenic non-coding RNAs involved in skeletal muscle growth and development in pig. Scientific Reports, vol. 7, no. 1, p. 1-11. https://doi.org/10.1038/s41598-017-07998-9 DOI: https://doi.org/10.1038/s41598-017-07998-9

Zou, X., Zhou, G., Yu, X., Bai, Y., Wang, C., Xu, X., Dai, C., Li, C. 2018. In vitro protein digestion of pork cuts differ with muscle type. Food Research International, vol. 106, p. 344-353. https://doi.org/10.1016/j.foodres.2017.12.070 DOI: https://doi.org/10.1016/j.foodres.2017.12.070

Zuber, E., Outhouse, A. C., Dekkers, J. C. M., Gabler, N. K., Huff-Lonergan, E., Lonergan, S. M. 2019. Rate and extent of troponin-T degradation in loins from pigs selected for low and high residual feed intake. Meat and Muscle Biology, vol. 1, no. 3. https://doi.org/10.221751/rmc2017.154 DOI: https://doi.org/10.22175/rmc2017.154

Zvereva, E. A., Kovalev, L. I., Ivanov, A. V., Kovaleva, M. A., Zherdev, A. V., Shishkin, S. S., Lisitsyn, A. B., Chernukha, I. M., Dzantiev, B. B. 2015. Enzyme immunoassay and proteomic characterization of troponin I as a marker of mammalian muscle compounds in raw meat and some meat products. Meat Science, vol. 105, p. 46-52. https://doi.org/10.1016/j.meatsci.2015.03.001 DOI: https://doi.org/10.1016/j.meatsci.2015.03.001

Published

2021-01-28

How to Cite

Akhremko, A., & Fedulova, L. (2021). Comparative study of weaning pigs’ muscle proteins using two-dimensional electrophoresis. Potravinarstvo Slovak Journal of Food Sciences, 15, 52–57. https://doi.org/10.5219/1449