title: Influence of the sagittal advancement of mandibulae on myofibrillar ATPase activity and myosin heavy chain content in the masticatory muscles of pigs.
abstract: Endurance muscle stress leads to polymorphic expression of myosin heavy chains (MyHC). Histochemical and electrophoretic analyses were performed on different masticatory muscles (masseter, temporal, geniohyoid and medial pterygoid) of 10 weeks old pigs after 28 days of chronic sagittal advancement of the mandibulae. The differentiation between fiber types was investigated histochemically with the myofibrillar ATPase (mATPase) method and by immunohistochemistry. Expression of different MyHC isoforms was also assessed by means of immunoblotting with monoclonal antibodies. The results of both methods were compared. Chronic sagittal advancement of the mandibulae led to an increase in the cross-sectional area of type I fibers and type I MyHC in the anterior part of the masseter, the distal part of the temporal and the medial pterygoid muscle. In the present study, clear differentiation between type I and type II muscle fibers in all histological analyses was possible. However, mATPase classification of subtypes of type II fibers may lead to misinterpretations. Additionally, a direct correlation between the type I MyHC concentration and the type I fibers was seen in enzyme histochemical and immunohistochemical staining. The defined cross section of fibers is important for the histological investigation in small muscles. The immunoblot method seems to be more sensitive and less subjective for measurement of muscle changes. It can be concluded that the immunoblot method used for measuring the MyHC content is a valid alternative for fiber typing in small muscles as it is less time-consuming and more sensitive than qualitative histochemistry.
authors.affiliation: Department of Orthodontics, Technical University, Dresden, Germany. gedrange@rcs.urz.tu-dresden.de
authors.forename: T
authors.initials: T
authors.lastname: Gedrange
authors.forename: A
authors.initials: A
authors.lastname: Lupp
authors.forename: C
authors.initials: C
authors.lastname: Kirsch
authors.forename: W
authors.initials: W
authors.lastname: Harze
authors.forename: R
authors.initials: R
authors.lastname: Klinger
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D007150:Immunohistochemistry; D008334:Mandible / Q000502:physiology*; D008406:Masseter Muscle / Q000166:cytology / Q000502:physiology; D008410:Masticatory Muscles / Q000166:cytology / Q000502:physiology*; D018485:Muscle Fibers, Skeletal / Q000166:cytology / Q000502:physiology; D009210:Myofibrils / Q000201:enzymology* / Q000648:ultrastructure; D018995:Myosin Heavy Chains / Q000378:metabolism*; D011187:Posture; D020033:Protein Isoforms / Q000378:metabolism; D013314:Stress, Mechanical; D013552:Swine
chemical_list: D020033:Protein Isoforms; D000251:Adenosine Triphosphatases; D018995:Myosin Heavy Chains