title: Muscle responses of thoroughbreds to conventional race training and detraining.
abstract: Ten healthy sedentary Thoroughbreds with previous race training experience were trained conventionally for 9 weeks. Muscle biopsy samples were obtained before and after training and after 6 weeks of detraining pasture rest. Biopsy samples were obtained from the right deltoid, triceps, vastus lateralis, middle gluteal, biceps femoris, and semitendinosus muscles. The deep-frozen biopsy samples were analyzed for activities of succinate dehydrogenase (SDH), 3-hydroxy-acylcoenzyme A dehydrogenase (HAD), and phosphorylase (PHOS) and for glycogen concentration. The triceps and gluteal muscle samples were also serially sectioned and stained for myofibrillar actomyosin adenosine triphosphatase (ATPase) activity after alkaline (pH 10.3) and sequential acidic (pH 4.34) ATPase inactivation. Fiber types I (alkaline preincubation), IIA1, IIA2, and IIA3 (sequential acidic preincubation over 5 minutes) were identified and were evaluated for fiber-type distribution and fiber areas. Increases in response to training were observed in deltoid and vastus muscle SDH and gluteal muscle HAD activities, and deltoid muscle glycogen concentration (P less than 0.05 to P less than 0.01). Changes in PHOS activity were not observed. Type-IIA1, -IIA2, and -IIA3 fiber areas in triceps muscle were increased in response to training (P less than 0.05 to P less than 0.01). Changes in fiber-type distribution did not occur in response to training. Changes in muscle enzyme activities, glycogen concentration, fiber types, and fiber areas were not seen from posttraining to detraining. Further increases were observed when detraining values were compared with pretraining values in deltoid, triceps, vastus, gluteal, and biceps femoris muscle SDH activities and in gluteal muscle glycogen concentration (P less than 0.05 to P less than 0.01).(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: Department of Veterinary Clinical Medicine, College of Veterinary Medicine, Washington State University, Pullman 99164.
authors.forename: J H
authors.initials: JH
authors.lastname: Foreman
authors.forename: W M
authors.initials: WM
authors.lastname: Bayly
authors.forename: J R
authors.initials: JR
authors.lastname: Allen
authors.forename: H
authors.initials: H
authors.lastname: Matoba
authors.forename: B D
authors.initials: BD
authors.lastname: Grant
authors.forename: P D
authors.initials: PD
authors.lastname: Gollnick
mesh_terms: D015094:3-Hydroxyacyl CoA Dehydrogenases / Q000378:metabolism; D000818:Animals; D005552:Forelimb; D006003:Glycogen / Q000378:metabolism; D006614:Hindlimb; D006736:Horses / Q000502:physiology*; D009132:Muscles / Q000033:anatomy & histology / Q000201:enzymology / Q000378:metabolism / Q000502:physiology*; D009210:Myofibrils / Q000502:physiology; D006005:Phosphorylases / Q000378:metabolism; D010805:Physical Conditioning, Animal; D013385:Succinate Dehydrogenase / Q000378:metabolism; D013997:Time Factors
chemical_list: D006003:Glycogen; D015094:3-Hydroxyacyl CoA Dehydrogenases; D013385:Succinate Dehydrogenase; D006005:Phosphorylases