Analyze Diet
Veterinary research communications2001; 25(7); 577-583; doi: 10.1023/a:1017977200420

Activities of enzymes related to the malate-aspartate shuttle in the blood cells of thoroughbred horses undergoing training exercise.

Abstract: The activities of the enzymes related to the malate-aspartate shuttle, which convert cytosolic NADH into mitochondrial NADH, were measured in red and white blood cells from thoroughbred horses undergoing continuous training (race horses) and compared with those in blood cells from riding horses. The activities of malate dehydrogenase (MDH), a rate-limiting enzyme for the malate-aspartate shuttle, were significantly elevated in the white blood cells (WBC) from race horses compared with those from riding horses. There were no significant differences in the activities of the enzymes in the red blood cells between race horses and riding horses. This increase in the MDH activity in their WBC is considered to reflect the increased metabolic activity in the race horses resulting from the training.
Publication Date: 2001-10-05 PubMed ID: 11583380DOI: 10.1023/a:1017977200420Google 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.
  • Comparative Study
  • 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.

This research study investigated the enzyme activity related to the malate-aspartate shuttle in thoroughbred horses engaged in rigorous exercise during training, comparing the results to those found in riding horses.

Overview of the Malate-Aspartate Shuttle

  • The malate-aspartate shuttle is a biochemical system within cells that transports electrons across the membrane of mitochondria. This is important for converting cytosolic NADH (a compound that carries electrons) into mitochondrial NADH.
  • This conversion is key to the cell’s process of producing energy, specifically during aerobic metabolism where oxygen is used to convert nutrients into ATP (adenosine triphosphate), the body’s primary energy source.

Enzyme Activity in Blood Cells

  • The study examined the activities of enzymes related to the malate-aspartate shuttle in the red and white blood cells of race horses compared to riding horses.
  • The specific enzyme investigated was malate dehydrogenase (MDH), a rate-limiting enzyme for the malate-aspartate shuttle. A rate-limiting enzyme is one that regulates the rate of a biochemical reaction.
  • The researchers found that levels of MDH were significantly higher in the white blood cells of race horses compared to riding horses. However, no significant differences in enzyme activity were observed in the red blood cells of the two groups.

Implications for Training and Metabolic Activity

  • The increase in MDH activity in the white blood cells of race horses, but not in their red blood cells, implies a link between this enzymatic activity and the metabolic demands of high-intensity training.
  • As such, the study suggests that the increase in MDH activity observed reflects increased metabolic activity in the race horses as a result of their training program.
  • This understanding could potentially be harnessed to optimize training programs for race horses, helping to enhance their performance by more effectively managing their biochemical energy production.

Cite This Article

APA
Arai T, Takahashi M, Araki K, Washizu T. (2001). Activities of enzymes related to the malate-aspartate shuttle in the blood cells of thoroughbred horses undergoing training exercise. Vet Res Commun, 25(7), 577-583. https://doi.org/10.1023/a:1017977200420

Publication

ISSN: 0165-7380
NlmUniqueID: 8100520
Country: Switzerland
Language: English
Volume: 25
Issue: 7
Pages: 577-583

Researcher Affiliations

Arai, T
  • Division of Veterinary Biochemistry, Nippon Veterinary and Animal Science University, Musashino, Tokyo, Japan. t-arai@mtc.biglobe.ne.jp
Takahashi, M
    Araki, K
      Washizu, T

        MeSH Terms

        • Animals
        • Blood Glucose / analysis
        • Cytosol / enzymology
        • Erythrocytes / enzymology
        • Fatty Acids, Nonesterified / blood
        • Female
        • Horse Diseases
        • Horses / blood
        • Horses / metabolism
        • Insulin / blood
        • Leukocytes / enzymology
        • Malate Dehydrogenase / metabolism
        • Malates / metabolism
        • Male
        • Mitochondria / enzymology
        • NAD / metabolism
        • Physical Conditioning, Animal / physiology

        References

        This article includes 13 references
        1. SIEGEL A, BING RJ. Plasma enzyme activity in myocardial infarction in dog and man.. Proc Soc Exp Biol Med 1956 Apr;91(4):604-7.
          pubmed: 13323017doi: 10.3181/00379727-91-22344google scholar: lookup
        2. Arai T, Kawaue T, Abe M, Kuramoto E, Kawakami E, Sako T, Washizu T. Comparison of glucokinase activities in the peripheral leukocytes between dogs and cats.. Comp Biochem Physiol C Pharmacol Toxicol Endocrinol 1998 Jul;120(1):53-6.
          pubmed: 9827016doi: 10.1016/s0742-8413(98)00005-xgoogle scholar: lookup
        3. Washizu T, Kuramoto E, Abe M, Sako T, Arai T. A comparison of the activities of certain enzymes related to energy metabolism in leukocytes in dogs and cats.. Vet Res Commun 1998 Apr;22(3):187-92.
          pubmed: 9618890doi: 10.1023/a:1006073305479google scholar: lookup
        4. Kaloustian HD, Stolzenbach FE, Everse J, Kaplan NO. Lactate dehydrogenase of lobster (Homarus americanus) tail muscle. I. Physical and chemical properties.. J Biol Chem 1969 Jun 10;244(11):2891-901.
          pubmed: 4306287
        5. Matschinsky FM. Banting Lecture 1995. A lesson in metabolic regulation inspired by the glucokinase glucose sensor paradigm.. Diabetes 1996 Feb;45(2):223-41.
          pubmed: 8549869doi: 10.2337/diab.45.2.223google scholar: lookup
        6. Hedeskov CJ, Capito K, Thams P. Cytosolic ratios of free [NADPH]/[NADP+] and [NADH]/[NAD+] in mouse pancreatic islets, and nutrient-induced insulin secretion.. Biochem J 1987 Jan 1;241(1):161-7.
          pubmed: 3551925doi: 10.1042/bj2410161google scholar: lookup
        7. HUGGETT AS, NIXON DA. Use of glucose oxidase, peroxidase, and O-dianisidine in determination of blood and urinary glucose.. Lancet 1957 Aug 24;273(6991):368-70.
          pubmed: 13464070doi: 10.1016/s0140-6736(57)92595-3google scholar: lookup
        8. Eto K, Tsubamoto Y, Terauchi Y, Sugiyama T, Kishimoto T, Takahashi N, Yamauchi N, Kubota N, Murayama S, Aizawa T, Akanuma Y, Aizawa S, Kasai H, Yazaki Y, Kadowaki T. Role of NADH shuttle system in glucose-induced activation of mitochondrial metabolism and insulin secretion.. Science 1999 Feb 12;283(5404):981-5.
          pubmed: 9974390doi: 10.1126/science.283.5404.981google scholar: lookup
        9. Arai T, Machida Y, Sasaki M, Oki Y. Hepatic enzyme activities and plasma insulin concentrations in diabetic herbivorous voles.. Vet Res Commun 1989;13(6):421-6.
          pubmed: 2561034doi: 10.1007/BF00402563google scholar: lookup
        10. Arai T, Washizu T, Hamada S, Sako T, Takagi S, Yashiki K, Motoyoshi S. Glucose transport and glycolytic enzyme activities in erythrocytes of two-year-old thoroughbreds undergoing training exercise.. Vet Res Commun 1994;18(6):417-22.
          pubmed: 7701778doi: 10.1007/BF01839417google scholar: lookup
        11. MacDonald MJ. High content of mitochondrial glycerol-3-phosphate dehydrogenase in pancreatic islets and its inhibition by diazoxide.. J Biol Chem 1981 Aug 25;256(16):8287-90.
          pubmed: 6790537
        12. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.. Anal Biochem 1976 May 7;72:248-54.
          pubmed: 942051doi: 10.1006/abio.1976.9999google scholar: lookup
        13. MacDonald MJ. Evidence for the malate aspartate shuttle in pancreatic islets.. Arch Biochem Biophys 1982 Feb;213(2):643-9.
          pubmed: 6462111doi: 10.1016/0003-9861(82)90594-xgoogle scholar: lookup

        Citations

        This article has been cited 6 times.
        1. Francis RO, D'Alessandro A, Eisenberger A, Soffing M, Yeh R, Coronel E, Sheikh A, Rapido F, La Carpia F, Reisz JA, Gehrke S, Nemkov T, Thomas T, Schwartz J, Divgi C, Kessler D, Shaz BH, Ginzburg Y, Zimring JC, Spitalnik SL, Hod EA. Donor glucose-6-phosphate dehydrogenase deficiency decreases blood quality for transfusion. J Clin Invest 2020 May 1;130(5):2270-2285.
          doi: 10.1172/JCI133530pubmed: 31961822google scholar: lookup
        2. D'Alessandro A, Hansen KC, Silliman CC, Moore EE, Kelher M, Banerjee A. Metabolomics of AS-5 RBC supernatants following routine storage. Vox Sang 2015 Feb;108(2):131-40.
          doi: 10.1111/vox.12193pubmed: 25200932google scholar: lookup
        3. Li G, Lee P, Mori N, Yamamoto I, Arai T. Long term intensive exercise training leads to a higher plasma malate/lactate dehydrogenase (M/L) ratio and increased level of lipid mobilization in horses. Vet Res Commun 2012 Jun;36(2):149-55.
          doi: 10.1007/s11259-012-9515-0pubmed: 22297553google scholar: lookup
        4. Tanaka A, Urabe S, Takeguchi A, Mizutani H, Sako T, Imai S, Yoshimura I, Kimura N, Arai T. Comparison of activities of enzymes related to energy metabolism in peripheral leukocytes and livers between Holstein dairy cows and ICR mice. Vet Res Commun 2006 Jan;30(1):29-38.
          doi: 10.1007/s11259-005-3223-ypubmed: 16362608google scholar: lookup
        5. Kimura N, Yoshimura I, Sako T, Inoue A, Tadami K, Arai T. Changes in activities of enzymes related to energy metabolism in peripheral leukocytes of fattening steers. Vet Res Commun 2005 Jan;29(1):19-26.
        6. Washizu T, Nakamura M, Izawa N, Suzuki E, Tsuruno S, Washizu M, Nakajo S, Arai T. The activity ratio of the cytosolic MDH/LDH and the isoenzyme pattern of LDH in the peripheral leukocytes of dogs, cats and rabbits. Vet Res Commun 2002 Jul;26(5):341-6.
          doi: 10.1023/a:1016278409138pubmed: 12212723google scholar: lookup