FREE SHIPPING over $40
OVER 9000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Home / Equine Research Bank / Animals (Basel) / Transcriptomic Profiling Reveals Lysine-Mediated Proliferati...
Animals : an open access journal from MDPI2025; 15(12); doi: 10.3390/ani15121711

Transcriptomic Profiling Reveals Lysine-Mediated Proliferative Mechanisms in Mongolian Horse Myogenic Satellite Cells.

Abstract: Skeletal muscle satellite cells are muscle stem cells that play an important role in the growth, development, and repair of skeletal muscle as well as in the locomotor performance of the animal body. Lysine is the first limiting amino acid and is involved in multiple metabolic pathways in the organism to maintain overall physiological requirements. In this study, Mongolian horse satellite cells were cultured using lysine culture solution at different concentrations, and the proliferative capacity of satellite cells was detected by the cck-8 assay, and the optimal culture concentration was selected. Then, whole transcriptome sequencing technology was used to determine the differential gene expression and regulatory pathways during the proliferation of lysine-cultured satellite cells after 48 h of culture. Our findings revealed that 0.5 mmol/L lysine is the optimal concentration to increase satellite cell activity in equine muscle. The differential genes involved in satellite cell proliferation were mainly enriched in the cAMPsignaling pathway, calcium signaling pathway, and PPAR signaling pathway. Furthermore, upregulation of PLIN5, ACADL, and FADS2 and downregulation of LOC100052888 regulated the expression of the PPAR signaling pathway. 0.5 mmol/L lysine was the optimal concentration to increase satellite cell activity. Lysine can regulate mitochondrial function and lipid metabolism through the PPAR signaling pathway, and promote the proliferation of equine myosatellite cells.
Get Full Text
Publication Date: 2025-06-09 PubMed ID: 40564262PubMed Central: PMC12189514DOI: 10.3390/ani15121711Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
LinkedInCopy
  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research investigates how lysine affects the growth of muscle satellite cells in Mongolian horses, using diverse lysine concentrations and gene sequencing technology.

Context

  • This study centers on skeletal muscle satellite cells, which are fundamental for the growth, development, repair, and overall locomotor functions of skeletal muscles.
  • Lysine, a limiting amino acid, features in numerous metabolic pathways to fulfill the organism‘s physiological requirements.
  • The researchers chose to focus on Mongolian horse satellite cells due to their direct relevance to the study of muscle growth and repair in animals.

Methodology

  • The investigators cultured Mongolian horse satellite cells in various lysine concentration solutions.
  • Their growth was tested through a cck-8 assay, which is a well-known method for measuring cell proliferation.
  • Sequencing technology was employed to identify any changes in gene expression and regulation pathways during the proliferation of these lysine-cultured cells.

Findings

  • Results revealed that a lysine concentration of 0.5 mmol/L was optimal for enhancing satellite cell activity in equine muscle.
  • Genes involved in cell proliferation were primarily linked to the cAMP signaling pathway, calcium signaling pathway, and the PPAR signaling pathway.
  • The researchers found an increase in the expression of certain genes, as well as a decrease in others, all related to the PPAR signaling pathway.

Conclusion

  • The study concluded that the optimal concentration of lysine to increase satellite cell activity was 0.5 mmol/L.
  • Lysine was discovered to influence mitochondrial function and lipid metabolism through the PPAR signaling pathway and encourage the growth of equine myosatellite cells.

Cite This Article

APA
Liu Y, Liu Y, Bai D, Dugarjaviin M, Zhang X. (2025). Transcriptomic Profiling Reveals Lysine-Mediated Proliferative Mechanisms in Mongolian Horse Myogenic Satellite Cells. Animals (Basel), 15(12). https://doi.org/10.3390/ani15121711

Publication

Animals : an open access journal from MDPI
ISSN: 2076-2615
NlmUniqueID: 101635614
Country: Switzerland
Language: English
Volume: 15
Issue: 12

Researcher Affiliations

Liu, Yumeng
  • Key Laboratory of Equus Germplasm Innovation, Ministry of Agriculture and Rural Affairs, Hohhot 010018, China.
  • Inner Mongolia Key Laboratory of Equine Science Research and Technology Innovation, Inner Mongolia Agricultural University, Hohhot 010018, China.
  • College of Animal Science, Inner Mongolia Agricultural University, Hohhot 010018, China.
Liu, Yuanyi
  • Key Laboratory of Equus Germplasm Innovation, Ministry of Agriculture and Rural Affairs, Hohhot 010018, China.
  • Inner Mongolia Key Laboratory of Equine Science Research and Technology Innovation, Inner Mongolia Agricultural University, Hohhot 010018, China.
  • College of Animal Science, Inner Mongolia Agricultural University, Hohhot 010018, China.
Bai, Dongyi
  • Key Laboratory of Equus Germplasm Innovation, Ministry of Agriculture and Rural Affairs, Hohhot 010018, China.
  • Inner Mongolia Key Laboratory of Equine Science Research and Technology Innovation, Inner Mongolia Agricultural University, Hohhot 010018, China.
  • College of Animal Science, Inner Mongolia Agricultural University, Hohhot 010018, China.
Dugarjaviin, Manglai
  • Key Laboratory of Equus Germplasm Innovation, Ministry of Agriculture and Rural Affairs, Hohhot 010018, China.
  • Inner Mongolia Key Laboratory of Equine Science Research and Technology Innovation, Inner Mongolia Agricultural University, Hohhot 010018, China.
  • College of Animal Science, Inner Mongolia Agricultural University, Hohhot 010018, China.
Zhang, Xinzhuang
  • Key Laboratory of Equus Germplasm Innovation, Ministry of Agriculture and Rural Affairs, Hohhot 010018, China.
  • Inner Mongolia Key Laboratory of Equine Science Research and Technology Innovation, Inner Mongolia Agricultural University, Hohhot 010018, China.
  • College of Animal Science, Inner Mongolia Agricultural University, Hohhot 010018, China.

Grant Funding

  • BR230405 / Outstanding Youth Science Fund Training Project of Inner Mongolia Agricultural University
  • 2023YFDZ0002 / Key R&D Project of Inner Mongolia
  • 2021MS03016 / Natural Science Foundation of Inner Mongolia
  • 31902188 / The National Natural Science Foundation of China
  • BR221018, BR251007 / Fundamental scientific research funds for universities directly under the Inner Mongolia Autonomous Region

Conflict of Interest Statement

The authors declare no conflicts of interest.

References

This article includes 39 references
  1. Sprayberry K.A., Slovis N.M.. Sales performance and athletic outcome in young Thoroughbreds with pericarditis.. Equine Vet. J. 2017;49:729–733.
    pubmed: 28719028
  2. Valberg S.J.. Muscle Conditions Affecting Sport Horses.. Vet. Clin. N. Am. Equine Pract. 2018;34:253–276.
    pubmed: 29853158
  3. Kamei Y., Hatazawa Y., Uchitomi R., Yoshimura R., Miura S.. Regulation of Skeletal Muscle Function by Amino Acids.. Nutrients 2020;12:261.
    doi: 10.3390/nሁ0261pmc: PMC7019684pubmed: 31963899google scholar: lookup
  4. Liu M., Li C., Tang H., Gong M., Yue Z., Zhao M., Liu L., Li F.. Dietary lysine supplementation improves growth performance and skeletal muscle development in rabbits fed a low protein diet.. J. Anim. Physiol. Anim. Nutr. 2022;106:1118–1129.
    pubmed: 34496098
  5. Wolf P., Pinna W., Boatto G., Pudda F., Cappai M.G., Accioni F.. Variation of Hematochemical Profile and Vitamin E Status in Feral Giara Horses From Free Grazing in the Wild to Hay Feeding During Captivity.. J. Equine Vet. Sci. 2020;94:103220.
    pubmed: 33077079
  6. National Research Council. Nutrient Requirements of Horses.. 6th ed. The National Academies Press; Washington, DC, USA: 2007.
  7. Ott E.A., Asquith R.L., Feaster J.P., Martin F.G.. Influence of Protein Level and Quality on the Growth and Development of Yearling Foals3.. J. Anim. Sci. 1979;49:620–628.
  8. Malesky S., Turner J., Browne-Silva J., Chen L., Löest C.. Nitrogen Retention and Plasma Amino Acid Responses in Mature Geldings Fed Three Dietary Concentrations of Lysine.. J. Equine Vet. Sci. 2013;33:733–738.
  9. Song Z.W., Jin C.L., Ye M., Gao C., Yan H., Wang X.. Lysine inhibits apoptosis in satellite cells to govern skeletal muscle growth via the JAK2-STAT3 pathway.. Food Funct. 2020;11:3941–3951.
    pubmed: 32338270
  10. Wang X., Zong X., Ye M., Jin C., Xu T., Yang J., Gao C., Wang X., Yan H.. Lysine Distinctively Manipulates Myogenic Regulatory Factors and Wnt/Ca2+ Pathway in Slow and Fast Muscles, and Their Satellite Cells of Postnatal Piglets.. Cells 2024;13:650.
    pmc: PMC11011516pubmed: 38607088
  11. Jin C.L., Ye J.L., Yang J., Gao C., Yan H., Li H., Wang X.. mTORC1 Mediates Lysine-Induced Satellite Cell Activation to Promote Skeletal Muscle Growth.. Cells 2019;8:1549.
    pmc: PMC6953079pubmed: 31801253
  12. Wang T., Feugang J.M., Crenshaw M.A., Naresh Regmi N., Blanton J.R., Liao S.F.. A Systems Biology Approach Using Transcriptomic Data Reveals Genes and Pathways in Porcine Skeletal Muscle Affected by Dietary Lysine.. Int. J. Mol. Sci. 2017;18:885.
    pmc: PMC5412465pubmed: 28430144
  13. Sato T., Ito Y., Nagasawa T.. L-Lysine suppresses myofibrillar protein degradation and autophagy in skeletal muscles of senescence-accelerated mouse prone 8.. Biogerontology 2017;18:85–95.
    pubmed: 27752791
  14. Palma-Granados P., Haro A., Seiquer I., Lara L., Aguilera J.F., Nieto R.. Similar effects of lysine deficiency in muscle biochemical characteristics of fatty and lean piglets.. J. Anim. Sci. 2017;95:3025–3036.
    doi: 10.2527/jas2017.1364pubmed: 28727124google scholar: lookup
  15. Shannon P., Markiel A., Ozier O., Baliga N.S., Wang J.T., Ramage D., Amin N., Schwikowski B., Ideker T.. Cytoscape: A software environment for integrated models of biomolecular interaction networks.. Genome Res. 2003;13:2498–2504.
    doi: 10.1101/gr.1239303pmc: PMC403769pubmed: 14597658google scholar: lookup
  16. Pallafacchina G., Blaauw B., Schiaffino S.. Role of satellite cells in muscle growth and maintenance of muscle mass.. Nutr. Metab. Cardiovasc. Dis. 2013;23((Suppl. 1)):S12–S18.
    doi: 10.1016/j.numecd.2012.02.002pubmed: 22621743google scholar: lookup
  17. Venema R.C., Caprara M.G., Hatzoglou M., Majumder M., Wang C., Snider M.D., Gaccioli F., Komar A.A., Yaman I., Zeenko V.V.. The hnRNA-binding proteins hnRNP L and PTB are required for efficient translation of the Cat-1 arginine/lysine transporter mRNA during amino acid starvation.. Mol. Cell Biol. 2009;29:2899–2912.
    pmc: PMC2682027pubmed: 19273590
  18. Morales A., García H., Arce N., Cota M., Zijlstra R.T., Araiza B.A., Cervantes M.. Effect of L-lysine on expression of selected genes, serum concentration of amino acids, muscle growth and performance of growing pigs.. J. Anim. Physiol. Anim. Nutr. 2015;99:701–709.
    pubmed: 25354230
  19. Fogl C., Puckey L., Hinssen U., Zaleska M., El-Mezgueldi M., Croasdale R., Bowman A., Matsukawa A., Samani N.J., Savva R.. A structural and functional dissection of the cardiac stress response factor MS1.. Proteins 2012;80:398–409.
    doi: 10.1002/prot.23201pubmed: 22081479google scholar: lookup
  20. Olson E.N., Bassel-Duby R., Richardson J.A., Frey N., Bezprozvannaya S., Barrientos T., Kuwahara K., Pipes G.C.T., Frank D., Katus H.A.. Two novel members of the ABLIM protein family, ABLIM-2 and -3, associate with STARS and directly bind F-actin.. J. Biol. Chem. 2007;282:8393–8403.
    pubmed: 17194709
  21. Arai A., Spencer J.A., Olson E.N.. STARS, a striated muscle activator of Rho signaling and serum response factor-dependent transcription.. J. Biol. Chem. 2002;277:24453–24459.
    pubmed: 11983702
  22. Lamon S., Russell A.P., Wallace M.A.. The regulation and function of the striated muscle activator of rho signaling (STARS) protein.. Front. Physiol. 2012;3:469.
    pmc: PMC3520124pubmed: 23248604
  23. Taniguchi K., Tominaga R., Takeya R., Kan-O M., Narusawa M., Shiose A., Sumimoto H., Suetsugu S.. Mammalian Formin Fhod3 Regulates Actin Assembly and Sarcomere Organization in Striated Muscles.. J. Biol. Chem. 2009;284:29873–29881.
    pmc: PMC2785617pubmed: 19706596
  24. Frey N., Olson E.N.. Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins.. J. Biol. Chem. 2002;277:13998–14004.
    pubmed: 11842093
  25. Suila H., Zara I., Belgrano A., Carpen O., Faulkner G., von Nandelstadh P., Valle G., Gardin C., Ismail M.. A class III PDZ binding motif in the myotilin and FATZ families binds enigma family proteins: A common link for Z-disc myopathies.. Mol. Cell. Biol. 2009;29:822–834.
    pmc: PMC2630697pubmed: 19047374
  26. Park J., Moon S.S., Song S., Cheng H., Im C., Du L., Kim G.-D.. Comparative review of muscle fiber characteristics between porcine skeletal muscles.. J. Anim. Sci. Technol. 2024;66:251–265.
    pmc: PMC11016745pubmed: 38628685
  27. Yamano S., Eto D., Hiraga A., Miyata H.. Recruitment pattern of muscle fibre type during high intensity exercise (60–100% VO2max) in thoroughbred horses.. Res. Vet. Sci. 2006;80:109–115.
    pubmed: 15992837
  28. Chan S., Seto J.T., MacArthur D.G., Yang N., North K.N., Head S.I.. A gene for speed: Contractile properties of isolated whole EDL muscle from an alpha-actinin-3 knockout mouse.. Am. J. Physiol. Cell Physiol. 2008;295:C897–C904.
    pubmed: 18650267
  29. Payne R.C., Crook T.C., Cruickshank S.E., Stubbs N., Wilson A.M., McGowan C.M., Hodson-Tole E.. A comparison of the moment arms of pelvic limb muscles in horses bred for acceleration (Quarter Horse) and endurance (Arab). J. Anat. 2010;217:26–37.
    pmc: PMC2913009pubmed: 20492428
  30. Willoughby D.. Organization of cAMP signalling microdomains for optimal regulation by Ca2+ entry.. Biochem. Soc. Trans. 2012;40:246–250.
    pubmed: 22260699
  31. Clarke K., Branco C., Ashmore T., West J.A., Morash A.J., Murfitt S.A., Kotwica A.O., Finnerty J., Griffin J.L., Johnson R.S.. Nitrate enhances skeletal muscle fatty acid oxidation via a nitric oxide-cGMP-PPAR-mediated mechanism.. BMC Biol. 2015;13:110.
    pmc: PMC4688964pubmed: 26694920
  32. Wu J., Luo J., Xia Y., An X., Guo P., He Q., Tian H., Hu Q., Li C., Wang H.. Goat FADS2 controlling fatty acid metabolism is directly regulated by SREBP1 in mammary epithelial cells.. J. Anim. Sci. 2023;101:skad030.
    doi: 10.1093/jas/skad030pmc: PMC9982361pubmed: 36694375google scholar: lookup
  33. Hawkins W., Brown K.M., Baker E., van der Merwe M., Sharma S., Puppa M.J.. Delta-6-desaturase (FADS2) inhibition and omega-3 fatty acids in skeletal muscle protein turnover.. Biochem. Biophys. Rep. 2019;18:100622.
    pmc: PMC6424014pubmed: 30923750
  34. Parkington H.C., Bayliss J., Suturin V.M., Bruce C.R., Montgomery M.K., Mokhtar R., Watt M.J.. Perilipin 5 Deletion Unmasks an Endoplasmic Reticulum Stress-Fibroblast Growth Factor 21 Axis in Skeletal Muscle.. Diabetes 2018;67:594–606.
    pubmed: 29378767
  35. Ni H.Y., Yu L., Zhao X., Wang L., Zhao C., Huang H., Zhu H., Efferth T., Gu C., Fu Y.. Seed oil of Rosa roxburghii Tratt against non-alcoholic fatty liver disease in vivo and in vitro through PPARα/PGC-1α-mediated mitochondrial oxidative metabolism.. Phytomedicine 2022;98:153919.
    pubmed: 35104757
  36. Hesselink M., Sparks L., Jorgensen J., Kersten S., Schrauwen P., Bosma M., Hooiveld G., Houten S.. Overexpression of PLIN5 in skeletal muscle promotes oxidative gene expression and intramyocellular lipid content without compromising insulin sensitivity.. Biochim. Biophys. Acta. 2013;1831:844–852.
    pubmed: 23353597
  37. Wu T., Wang S., Wang L., Zhang W., Chen W., Lv X., Li Y., Hussain Z., Sun W.. Long Noncoding RNA (lncRNA) CTTN-IT1 Elevates Skeletal Muscle Satellite Cell Proliferation and Differentiation by Acting as ceRNA for YAP1 Through Absorbing miR-29a in Hu Sheep.. Front. Genet. 2020;11:843.
    pmc: PMC7427492pubmed: 32849826
  38. Ge M.X., Shao R.G., He H.. Advances in understanding the regulatory mechanism of cholesterol 7α-hydroxylase.. Biochem. Pharmacol. 2019;164:152–164.
    pubmed: 30978324
  39. Patel D.D., Knight B.L., Soutar A.K., Gibbons G.F., Wade D.P.. The effect of peroxisome-proliferator-activated receptor-alpha on the activity of the cholesterol 7 alpha-hydroxylase gene. Pt 3. Biochem. J. 2000;351:747–753.
    doi: 10.1042/bj3510747pmc: PMC1221415pubmed: 11042130google scholar: lookup
Subscribe to our newsletter
Join 99,359 horse owners like you who receive our email updates on horse health and nutrition.