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Home / Equine Research Bank / Vet Sci / Sarcoplasmic Reticulum from Horse Gluteal Muscle Is Poised f...
Veterinary sciences2021; 8(12); doi: 10.3390/vetsci8120289

Sarcoplasmic Reticulum from Horse Gluteal Muscle Is Poised for Enhanced Calcium Transport.

Abstract: We have analyzed the enzymatic activity of the sarcoplasmic reticulum (SR) Ca2+-transporting ATPase (SERCA) from the horse gluteal muscle. Horses are bred for peak athletic performance yet exhibit a high incidence of exertional rhabdomyolysis, with elevated levels of cytosolic Ca2+ proposed as a correlative linkage. We recently reported an improved protocol for isolating SR vesicles from horse muscle; these horse SR vesicles contain an abundant level of SERCA and only trace-levels of sarcolipin (SLN), the inhibitory peptide subunit of SERCA in mammalian fast-twitch skeletal muscle. Here, we report that the in vitro Ca2+ transport rate of horse SR vesicles is 2.3 ± 0.7-fold greater than rabbit SR vesicles, which express close to equimolar levels of SERCA and SLN. This suggests that horse myofibers exhibit an enhanced SR Ca2+ transport rate and increased luminal Ca2+ stores in vivo. Using the densitometry of Coomassie-stained SDS-PAGE gels, we determined that horse SR vesicles express an abundant level of the luminal SR Ca2+ storage protein calsequestrin (CASQ), with a CASQ-to-SERCA ratio about double that in rabbit SR vesicles. Thus, we propose that SR Ca2+ cycling in horse myofibers is enhanced by a reduced SLN inhibition of SERCA and by an abundant expression of CASQ. Together, these results suggest that horse muscle contractility and susceptibility to exertional rhabdomyolysis are promoted by enhanced SR Ca2+ uptake and luminal Ca2+ storage.
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Publication Date: 2021-11-23 PubMed ID: 34941816PubMed Central: PMC8705379DOI: 10.3390/vetsci8120289Google Scholar: Lookup
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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 study focuses on the examination of the sarcoplasmic reticulum (SR), a structure within muscle cells responsible for storing and releasing calcium, in horse gluteal muscle. The research findings suggest that the horse SR has a greater calcium transport rate and enhanced luminal calcium storage, which may factor into the animal’s athletic performance and predisposition to exertional rhabdomyolysis, a muscle disorder.

Research Methodology

  • The researchers utilized an improved protocol for isolating SR vesicles from horse muscle. The isolated vesicles demonstrated high levels of Ca-transporting ATPase (SERCA), an enzyme integral to calcium transport, and minimal traces of sarcolipin (SLN), a protein that inhibits SERCA in fast-twitch skeletal muscle.
  • The calcium transport rate of horse SR vesicles was compared with that of rabbit SR vesicles in vitro. The researchers found that the horse SR vesicles’ rate was over twice as much as that of the rabbit SR vesicles.
  • The research team also scrutinized the expression level of calsequestrin (CASQ), a protein responsible for calcium storage within the SR. They used a density measurement technique involving Coomassie-stained SDS-PAGE gels to establish this.

Research Findings

  • The horse SR demonstrated a significantly higher calcium transport rate than the rabbit SR, suggesting enhanced calcium cycling within the horse myofibers.
  • Horse SR vesicles contained a high level of CASQ, suggesting increased luminal calcium stores in the horse muscle cells. The CASQ-to-SERCA ratio in horse SR was about double that in rabbit SR vesicles, indicating a more efficient system in horses for storing calcium in the SR.
  • Together, these findings suggest that the diminished SLN inhibition on SERCA and the abundant presence of CASQ enhance the calcium cycling within horse muscles, which likely impacts muscle contractility and the high incidence of exertional rhabdomyolysis in horses.

Significance of the Research

  • This research provides informative insights into the unique muscle morphology of horses, particularly the advanced calcium transport and storage potential of their SR compared to other mammals.
  • The findings may help to better understand the underlying molecular mechanisms that contribute to the high athletic performance of horses.
  • The research findings may also shed light on why horses are prone to exertional rhabdomyolysis, which can inform preventative measures and treatment strategies for this condition.

Cite This Article

APA
Autry JM, Svensson B, Carlson SF, Chen Z, Cornea RL, Thomas DD, Valberg SJ. (2021). Sarcoplasmic Reticulum from Horse Gluteal Muscle Is Poised for Enhanced Calcium Transport. Vet Sci, 8(12). https://doi.org/10.3390/vetsci8120289

Publication

Veterinary sciences
ISSN: 2306-7381
NlmUniqueID: 101680127
Country: Switzerland
Language: English
Volume: 8
Issue: 12

Researcher Affiliations

Autry, Joseph M
  • Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Svensson, Bengt
  • Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Carlson, Samuel F
  • Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Chen, Zhenhui
  • Krannert Institute of Cardiology, Department of Medicine, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
Cornea, Razvan L
  • Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Thomas, David D
  • Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Valberg, Stephanie J
  • McPhail Equine Performance Center, Department of Large Animal Clinical Sciences, College of Veterinary Medicine, Michigan State University, East Lansing, MI 48823, USA.

Grant Funding

  • HL139065 / NIH HHS
  • R37 AG026160 / NIA NIH HHS
  • GM27906 / NIH HHS
  • AG026160 / NIH HHS
  • R01 HL139065 / NHLBI NIH HHS
  • D16EQ-004 / Morris Animal Foundation

Conflict of Interest Statement

The authors declare that they have no conflicts of interest with the contents of this article. S.J.V. is part-owner of the license for genetic testing of equine type 1 polysaccharide storage myopathy, glycogen branching enzyme deficiency, and myosin 1 myopathy, receiving sales income from their diagnostic use. S.J.V. also receives royalties from the sale of Re-Leve equine feed. The financial and business interests of S.J.V. have been reviewed and managed by Michigan State University in accordance with MSU conflict of interest policies. D.D.T. and R.L.C. hold equity in and serve as executive officers for Photonic Pharma LLC. The financial and business interests of D.D.T. and R.L.C. have been reviewed and managed by the University of Minnesota in accordance with UMN conflict of interest policies. Photonic Pharma LLC had no role in this study. Acronyms and Abbreviations. CASQ, calsequestrin; IU, international unit of enzyme activity, defined as the production of 1 µmol product per milligram protein per minute; KATP, ATP dissociation constant of SERCA; KCa, apparent Ca2+ dissociation constant of SERCA, defined as the Ca2+ concentration required for half-maximal activation of activity; lncRNA, long non-coding RNA; MRLN, myoregulin; PLN, phospholamban; ProtK, proteinase K; RER, recurrent exertional rhabdomyolysis; RNA-seq, whole transcriptome shotgun sequencing; RYR, ryanodine receptor Ca2+ release channel; SERCA, sarco/endoplasmic reticulum Ca2+-transporting ATPase; SLN, sarcolipin; SR, sarcoplasmic reticulum; Vmax, maximal enzyme velocity of SERCA, defined as the Ca2+-activated ATPase activity or Ca2+ transport activity at saturating concentrations of ionized Ca2+ (~1–10 µM) and MgATP (~3–10 mM).

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