FREE SHIPPING over $40
OVER 9000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Home / Equine Research Bank / Am J Vet Res / Effect of gluteus medius muscle sample collection depth on p...
American journal of veterinary research2013; 74(6); 910-917; doi: 10.2460/ajvr.74.6.910

Effect of gluteus medius muscle sample collection depth on postprandial mammalian target of rapamycin signaling in mature Thoroughbred mares.

Abstract: To determine the effect of biopsy collection depth on the postprandial activation of mammalian target of rapamycin (mTOR) signaling factors, particularly protein kinase B, ribosomal protein S6 kinase, ribosomal protein S6, and eukaryotic initiation factor 4E binding protein 1 in middle-aged horses. Methods: 6 healthy Thoroughbred mares (mean ± SD age, 13.4 ± 3.4 years). Methods: Horses were fed a high-protein feed at 3 g/kg. Sixty minutes after horses were fed, the percutaneous needle biopsy technique was used to collect biopsy specimens from the gluteus medius muscle at 6, 8, and 10 cm below the surface of the skin. Muscle specimens were analyzed for the activation of upstream and downstream mTOR signaling factors, myosin heavy chain (MHC) isoform composition, and amino acid concentrations. Results: A 21% increase in MHC IIA isoform expression and a 21% decrease in MHC IIX isoform expression were identified as biopsy depth increased from 8 to 10 cm below the surface of the skin; however, no significant change was evident in the degree of MHC I expression with muscle depth. Biopsy depth had no significant effect on the phosphorylation of any of the mTOR signaling factors evaluated. Conclusions: Postprandial mTOR signaling could be compared between middle-aged horses when biopsy specimens were collected between 6 and 10 cm below the surface of the skin. Optimization of muscle biopsy techniques for evaluating mTOR signaling in horses will facilitate the design of future investigations into the factors that regulate muscle mass in horses.
Get Full Text
Publication Date: 2013-05-31 PubMed ID: 23718660PubMed Central: PMC4104021DOI: 10.2460/ajvr.74.6.910Google 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
  • Research Support
  • Non-U.S. Gov't

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.

This research investigates how the depth of muscle sample collection affects the analysis of nutrient processing signals in the muscles of middle-aged thoroughbred horses, specifically after feeding, and finds that depth does not significantly affect these signals.

Research Goals and Methods

  • The researchers wanted to understand if the depth from which a muscle sample (biopsy) was taken would affect how the muscle’s nutrient-processing signals are activated after the horse eats.
  • These signals include protein kinase B, ribosomal protein S6 kinase, ribosomal protein S6, and eukaryotic initiation factor 4E binding protein 1, which are controlled by the mammalian target of rapamycin (mTOR), a central regulator of cell growth, proliferation, survival, and metabolism.
  • The study used six healthy, middle-aged Thoroughbred mares, who were fed a high-protein diet.
  • Muscle samples were taken from the gluteus medius muscle (part of the buttocks) at depths of 6, 8, and 10cm below the skin surface, an hour after the horses had been fed.

Data Analysis

  • The muscle samples were analyzed for the activation of the mTOR signaling factors, the composition of myosin heavy chain (MHC) isoforms which are vital for muscle contraction, and amino acid concentrations.

Research Findings

  • The research found that as biopsy depth increased from 8 to 10 cm below the skin surface, there was a 21% increase in MHC IIA isoform expression and a 21% decrease in MHC IIX isoform expression.
  • No significant difference was observed in MHC I expression with different muscle depths.
  • The depth at which the muscle sample was taken had no noticeable effect on the activation of any of the mTOR signaling factors.

Conclusions

  • Findings from this study suggest that the depth of muscle biopsy does not significantly affect the postprandial (after eating) activation of mTOR signaling. This will assist in optimizing muscle biopsy techniques in horses and inform the design of future studies into muscle mass regulation in horses.

Cite This Article

APA
Wagner AL, Urschel KL, Lefta M, Esser KA. (2013). Effect of gluteus medius muscle sample collection depth on postprandial mammalian target of rapamycin signaling in mature Thoroughbred mares. Am J Vet Res, 74(6), 910-917. https://doi.org/10.2460/ajvr.74.6.910

Publication

American journal of veterinary research
ISSN: 1943-5681
NlmUniqueID: 0375011
Country: United States
Language: English
Volume: 74
Issue: 6
Pages: 910-917

Researcher Affiliations

Wagner, Ashley L
  • Department of Animal and Food Sciences, College of Veterinary Medicine, University of Kentucky, Lexington, KY 40546, USA.
Urschel, Kristine L
    Lefta, Mellani
      Esser, Karyn A

        MeSH Terms

        • Animals
        • Biopsy, Needle
        • Female
        • Gene Expression Regulation / physiology
        • Muscle, Skeletal / metabolism
        • Muscle, Skeletal / pathology
        • Postprandial Period / physiology
        • Specimen Handling
        • TOR Serine-Threonine Kinases / genetics
        • TOR Serine-Threonine Kinases / metabolism

        Grant Funding

        • R01 AR061939 / NIAMS NIH HHS

        References

        This article includes 40 references
        1. Lindholm A, Piehl K. Fibre composition, enzyme activity and concentrations of metabolites and electrolytes in muscles of Standardbred horses.. Acta Vet Scand 1974;15:287–309.
          pmc: PMC8407315pubmed: 4137664
        2. Kline KH, Bechtel PJ. Changes in the metabolic profile of the equine gluteus medius as a function of sampling depth.. Comp Biochem Physiol A Comp Physiol 1988;91:815–819.
          pubmed: 2907449
        3. Sewell DA, Harris RC, Marlin DJ. Skeletal muscle characteristics in 2 year-old race-trained Thoroughbred horses.. Comp Biochem Physiol Comp Physiol 1994;108:87–96.
          pubmed: 7915652
        4. Wagner AL, Urschel KL. Developmental regulation of the activation of translation initiation factors in response to feeding in the skeletal muscle of horses.. Am J Vet Res 2012;73:1241–1251.
          pubmed: 22849685
        5. Urschel KL, Escobar J, McCutcheon LJ. Effect of feeding a high-protein diet following an 18-hour period of feed withholding on mammalian target of rapamycin-dependent signaling in skeletal muscle of mature horses.. Am J Vet Res 2011;72:248–255.
          pubmed: 21281201
        6. Tiley HA, Geor RJ, McCutcheon LJ. Effects of dexamethasone administration on insulin resistance and components of insulin signaling and glucose metabolism in equine skeletal muscle.. Am J Vet Res 2008;69:51–58.
          pubmed: 18167087
        7. Rivero JL, Ruz A, Marti-Korff S. Effects of intensity and duration of exercise on muscular responses to training of Thoroughbred racehorses.. J Appl Physiol 2007;102:1871–1882.
          pubmed: 17255370
        8. Annandale EJ, Valberg SJ, Mickelson JR. Insulin sensitivity and skeletal muscle glucose transport in horses with equine polysaccharide storage myopathy.. Neuromuscul Disord 2004;14:666–674.
          pubmed: 15351424
        9. Waller AP, Geor RJ, Spriet LL. Oral acetate supplementation after prolonged moderate intensity exercise enhances early muscle glycogen resynthesis in horses.. Exp Physiol 2009;94:888–898.
          pubmed: 19429643
        10. Liburt NR, Adams AA, Betancourt A. Exercise-induced increases in inflammatory cytokines in muscle and blood of horses.. Equine Vet J Suppl 2010;(38):280–288.
          pubmed: 21059019
        11. Serrano AL, Petrie JL, Rivero JL. Myosin isoforms and muscle fiber characteristics in equine gluteus medius muscle.. Anat Rec 1996;244:444–451.
          pubmed: 8694280
        12. López-Rivero JL, Serrano AL, Diz AM. Variability of muscle fibre composition and fibre size in the horse gluteus medius: an enzyme-histochemical and morphometric study.. J Anat 1992;181:1–10.
          pmc: PMC1259747pubmed: 1284127
        13. Snow DH, Guy PS. Muscle fibre type composition of a number of limb muscles in different types of horse.. Res Vet Sci 1980;28:137–144.
          pubmed: 6447905
        14. Schiaffino S, Reggiani C. Molecular diversity of myofibrillar proteins: gene regulation and functional significance.. Physiol Rev 1996;76:371–423.
          pubmed: 8618961
        15. Badiani A, Nanni N, Gatta PP. Nutrient profile of horsemeat.. J Food Compost Anal 1997;10:254–269.
        16. Tipton KD, Ferrando AA. Improving muscle mass: response of muscle metabolism to exercise, nutrition and anabolic agents.. Essays Biochem 2008;44:85–98.
          pubmed: 18384284
        17. Miyazaki M, Esser KA. Cellular mechanisms regulating protein synthesis and skeletal muscle hypertrophy in animals.. J Appl Physiol 2009;106:1367–1373.
          pmc: PMC2698644pubmed: 19036895
        18. Kimball SR. The role of nutrition in stimulating muscle protein accretion at the molecular level.. Biochem Soc Trans 2007;35:1298–1301.
          pubmed: 17956335
        19. Liu Z, Jahn LA, Wei L. Amino acids stimulate translation initiation and protein synthesis through an Akt-independent pathway in human skeletal muscle.. J Clin Endocrinol Metab 2002;87:5553–5558.
          pubmed: 12466352
        20. Escobar J, Frank JW, Suryawan A. Physiological rise in plasma leucine stimulates muscle protein synthesis in neonatal pigs by enhancing translation initiation factor activation.. Am J Physiol Endocrinol Metab 2005;288:E914–E921.
          pubmed: 15644455
        21. Escobar J, Frank JW, Suryawan A. Amino acid availability and age affect the leucine stimulation of protein synthesis and eIF4F formation in muscle.. Am J Physiol Endocrinol Metab 2007;293:E1615–E1621.
          pmc: PMC2715339pubmed: 17878223
        22. Parkington JD, Siebert AP, LeBrasseur NK. Differential activation of mTOR signaling by contractile activity in skeletal muscle.. Am J Physiol Regul Integr Comp Physiol 2003;285:R1086–R1090.
          pubmed: 12881204
        23. Baar K, Esser K. Phosphorylation of p70(S6k) correlates with increased skeletal muscle mass following resistance exercise.. Am J Physiol 1999;276:C120–C127.
          pubmed: 9886927
        24. Tannerstedt J, Apro W, Blomstrand E. Maximal lengthening contractions induce different signaling responses in the type I and type II fibers of human skeletal muscle.. J Appl Physiol 2009;106:1412–1418.
          pubmed: 19112158
        25. Koopman R, Zorenc AH, Gransier RJ. Increase in S6K1 phosphorylation in human skeletal muscle following resistance exercise occurs mainly in type II muscle fibers.. Am J Physiol Endocrinol Metab 2006;290:E1245–E1252.
          pubmed: 16434552
        26. Gazzaneo MC, Orellana RA, Suryawan A. Differential regulation of protein synthesis and mTOR signaling in skeletal muscle and visceral tissues of neonatal pigs after a meal.. Pediatr Res 2011;70:253–260.
          pmc: PMC3152601pubmed: 21654549
        27. Henneke DR, Potter GD, Kreider JL. Relationship between condition score, physical measurements and body fat percentage in mares.. Equine Vet J 1983;15:371–372.
          pubmed: 6641685
        28. National Research Council. Nutrient requirements of horses.. 6th ed. Washington, DC: National Academies Press; 2007.
        29. Talmadge RJ, Roy RR. Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms.. J Appl Physiol 1993;75:2337–2340.
          pubmed: 8307894
        30. Crook TC, Cruickshank SE, McGowan CM. Comparative anatomy and muscle architecture of selected hind limb muscles in the Quarter Horse and Arab.. J Anat 2008;212:144–152.
          pmc: PMC2408980pubmed: 18194205
        31. Vick MM, Adams AA, Murphy BA. Relationships among inflammatory cytokines, obesity, and insulin sensitivity in the horse.. J Anim Sci 2007;85:1144–1155.
          pubmed: 17264235
        32. Lindner A, Dag S, Marti-Korff S. Effects of repeated biopsying on muscle tissue in horses.. Equine Vet J 2002;34:619–624.
          pubmed: 12358004
        33. Wood CH, Ross TT, Armstrong JB. Homogeneity of muscle fiber composition in the M gluteus medius of the horse.. J Equine Vet Sci 1988;8:294–296.
        34. Valette JP, Barrey E, Jouglin M. Standardisation of muscular biopsy of gluteus medius in French trotters.. Equine Vet J Suppl 1999;(30):342–344.
          pubmed: 10659280
        35. Eizema K, van den Burg MM, de Jonge HW. Myosin heavy chain isoforms in equine gluteus medius muscle: comparison of mRNA and protein expression profiles.. J Histochem Cytochem 2005;53:1383–1390.
          pubmed: 15983121
        36. Suryawan A, Torrazza RM, Gazzaneo MC. Enteral leucine supplementation increases protein synthesis in skeletal and cardiac muscles and visceral tissues of neonatal pigs through mTORC1-dependent pathways.. Pediatr Res 2012;71:324–331.
          pmc: PMC3619200pubmed: 22391631
        37. Zeanandin G, Balage M, Schneider SM. Differential effect of long-term leucine supplementation on skeletal muscle and adipose tissue in old rats: an insulin signaling pathway approach.. Age (Dordr) 2012;34:371–387.
          pmc: PMC3312629pubmed: 21472380
        38. Glynn EL, Fry CS, Drummond MJ. Excess leucine intake enhances muscle anabolic signaling but not net protein anabolism in young men and women.. J Nutr 2010;140:1970–1976.
          pmc: PMC2955876pubmed: 20844186
        39. Mittendorfer B, Andersen JL, Plomgaard P. Protein synthesis rates in human muscles: neither anatomical location nor fibre-type composition are major determinants.. J Physiol 2005;563:203–211.
          pmc: PMC1665563pubmed: 15611031
        40. Timmerman KL, Lee JL, Dreyer HC. Insulin stimulates human skeletal muscle protein synthesis via an indirect mechanism involving endothelial-dependent vasodilation and mammalian target of rapamycin complex 1 signaling.. J Clin Endocrinol Metab 2010;95:3848–3857.
          pmc: PMC2913031pubmed: 20484484

        Citations

        This article has been cited 2 times.
        1. Busse NI, Gonzalez ML, Wagner AL, Johnson SE. Short Communication: Supplementation with calcium butyrate causes an increase in the percentage of oxidative fibers in equine gluteus medius muscle. J Anim Sci 2022 Aug 1;100(8).
          doi: 10.1093/jas/skac108pubmed: 35908781google scholar: lookup
        2. Busse NI, Gonzalez ML, Krason ML, Johnson SE. β-Hydroxy β-methylbutyrate supplementation to adult Thoroughbred geldings increases type IIA fiber content in the gluteus medius. J Anim Sci 2021 Oct 1;99(10).
          doi: 10.1093/jas/skab264pubmed: 34516615google scholar: lookup
        Subscribe to our newsletter
        Join 99,357 horse owners like you who receive our email updates on horse health and nutrition.