Decreased mandibular cortical bone quality after botulinum toxin injections in masticatory muscles in female adults.

This study aimed to clarify how masticatory muscle atrophy induced by botulinum toxin (BTX) injection affects cortical bone quality of the mandible using 3D modeling technology. A total of 39 young (26.9 ± 6.0 years) and 38 post-menopausal (55.3 ± 6.3 years) females were included. Computed tomography (CT) images were obtained before and after 12 months of treatment. Predictor variables were application of a stabilization splint, and/or two times of BTX injection in the bilateral temporalis and masseter muscles within a six-month interval. Outcome variables were changes in average Hounsfield units (HU) and cortical thickness of region of interest (ROI). 3D mandibular models were reconstructed using CT images, and models were used to calculate average HU and cortical thickness of ROIs, including inferior half of the lateral surface of ascending ramus, coronoid process, and temporomandibular joint condyle. Cortical bone quality at muscle insertion site was influenced by decreased muscle thickness but seemed not to be affected by decreased functional loading. Reduced functional loading seemed to influence cortical bone quality of the condyles. These effects were more remarkable in post-menopausal females. Hence, decreased masticatory muscle thickness may lead to alterations of the mandibular cortical structures, especially in post-menopausal females.

Histological features of masticatory muscles after botulinum toxin A injection into the right masseter muscle of dystrophin deficient (mdx-) mice.

OBJECTIVE/BACKGROUND: The most frequently used animal model for human DMD (Duchenne muscular dystrophy) research is the mdx mouse. In both species, characteristic histological changes like inflammation, muscle fiber degeneration and fibrosis are the same, but in contrast to humans, in mdx mice, phases of muscle fiber degeneration are compensated by regeneration processes. AIM: Therefore, the interest of this study was to evaluate histological features in masticatory muscles after BTX-A injection into the right masseter muscle of wild type and dystrophic (mdx) mice, illustrating de- and regeneration processes induced by this substance. MATERIAL AND METHODS: The right masseter muscle of 100 days old healthy and mdx mice were selectively paralyzed by a single intramuscular BTX-A injection. Masseter as well as temporal muscle of injection and non-injection side were carefully dissected 21 days and 42 days after injection, respectively, and fiber diameter, cell nuclei position, necrosis and collagen content were analyzed histomorphologically in order to evaluate de- and regeneration processes in these muscles. Statistical analysis was performed using SigmaStat Software and Mann Whitney U-test (significance level: p < 0.05). RESULTS: At both investigation periods and in both mouse strains fiber diameter was significantly reduced and collagen content was significantly increased in the right injected masseter muscle whereas fiber diameters in mdx mice were much smaller, and these differences were even more apparent at the second investigation period. Necrosis and central located nuclei could generally be found in all mdx mice muscles investigated with an amount of centronucleation exceeding 60%, and a significant increase of necrosis six weeks after injection. In wild type mice central located nuclei could primarily be found in the treated masseter muscle with a portion of 2.7%, and this portion decreased after six weeks, whereas in mdx mice a decrease could also be seen in the non-injected muscles. In contrast, in wild type mice necrosis was not apparent at any time and in all muscles investigated. CONCLUSION: From our results it can be concluded that in mdx mice masticatory muscles de- and regeneration processes were extended, triggered by a selective BTX-A injection, or mdx mice at this age, independently of BTX-A treatment, went through another cycle of de- and regeneration as a characteristic of this disease.

Distribution of tropomyosin isoforms in different types of single fibers isolated from bovine skeletal muscles.

To clarify the relationship between myosin heavy chain (MyHC) isoforms and tropomyosin (TPM) isoforms in single fibers, 64 single fibers were isolated from each of bovine three muscles (masseter, semispinalis and semitendinosus). mRNA expressions of MyHC and TPM isoforms were analyzed by real-time PCR. All single fibers from the masseter expressed MyHC-slow. The fibers from the semispinalis expressed both MyHC-slow and 2a. The fibers from the semitendinosus expressed MyHC-slow, 2a and 2x. TPM-1 and TPM-2 were co-expressed in 2a and 2x type fibers, and TPM-2 and TPM-3 were co-expressed in slow type fibers. The expression pattern of TPM isoforms in each fiber type was similar between fibers isolated from different muscles. These results suggest that TPM-1 and TPM-3 isoforms correspond to the function of 2a or 2x type fibers and slow type fibers, respectively, with TPM-2 in common. Furthermore, the patterns of MyHC and TPM isoform combinations did not vary among single fibers isolated from the individual muscles examined.

Chronic sleep deprivation alters the myosin heavy chain isoforms in the masseter muscle in rats.

To investigate the changes in myosin heavy chain (MyHC) isoforms of rat masseter muscle fibres caused by chronic sleep deprivation and a possible link with the pathogenesis of disorders of the temporomandibular joint (TMJ). A total of 180 male rats were randomly divided into three groups (n=60 in each): cage controls, large platform controls, and chronic sleep deprivation group. Each group was further divided into three subgroups with different observation periods (7, 14, and 21 days). We investigated he expression of MyHC isoforms in masseter muscle fibres by real-time quantitative polymerase chain reaction (PCR), Western blotting, and immunohistochemical staining. In rats with chronic sleep deprivation there was increased MyHC-I expression in layers of both shallow and deep muscles at 7 and 21 days compared with the control groups, whereas sleep deprivation was associated with significantly decreased MyHC-II expression. At 21 days, there were no differences in MyHC-I or MyHC-II expression between the groups and there were no differences between the two control groups at any time point. These findings suggest that chronic sleep deprivation alters the expression of MyHC isoforms, which may contribute to the pathogenesis of disorders of the TMJ.

Age-related changes in rat genioglossus, geniohyoid and masseter muscles.

OBJECTIVES: The aim of this study was to elucidate age-related changes from adult to middle age in the contractile properties of the masseter, genioglossus and geniohyoid muscles of the rat. MATERIALS AND METHODS: We analysed the expressions of myosin heavy chain (MyHC) mRNAs and proteins as indicators of the contractile properties in these muscles obtained from rats at 6, 12, 18 and 24 months of age using real-time PCR and SDS-PAGE. RESULTS: We found no marked age-related changes in the expressions of MyHC mRNAs and proteins in rat masseter and geniohyoid muscles, suggesting that the biological ageing process does not affect contractile properties in these muscles. However, we found a decrease in the expression of MyHC IIb mRNA with ageing in the rat genioglossus muscle, suggesting that biological ageing process induces at least some fast-to-slow myofibre phenotype transition. CONCLUSION: The biological ageing process from adult to middle age appears to differentially affect different types of craniofacial muscles.

Characterization of Longissimus thoracis, Semitendinosus and Masseter muscles and relationships with technological quality in pigs. 1. Microscopic analysis of muscles.

Three porcine muscles (Longissimus thoracis, Semitendinosus, Masseter), known to have large differences in biochemical and histological traits, were fully characterized and the link between muscle structure and quality evaluated. The oxidative Masseter had more pigment, higher content of metmyoglobin, haem iron, protein and collagen, and was redder with higher fibre numbers, fibre circularity, pH and water holding capacity than the glycolytic Longissimus. Fibre type distribution showed predominance of type IIB in Longissimus and Semitendinosus white, type I in Semitendinosus red and IIA in Masseter. Type I fibres were larger than type IIB and IIA in Semitendinosus and Masseter, respectively, but not in the Longissimus, indicating that fibre size is muscle dependent. Muscle redness was positively correlated with type I fibre traits, haem iron and metmyoglobin, and negatively associated with type II fibre characteristics, non-haem iron and oxymyoglobin. Expressible juice had positive correlation with fibre size and negative with fibre number and connective tissue.

Characterization of Longissimus thoracis, Semitendinosus and Masseter muscles and relationships with technological quality in pigs. 2. Composition of muscles.

The composition of three porcine muscles (Longissimus thoracis: LT, Semitendinosus: ST, Masseter: MS) was characterized and its link with muscle quality was evaluated. The LT muscle had a higher content of tyrosine, tryptophan, and carbohydrates and a lower content of vitamin E and haem iron than the MS muscle, while the ST had similar composition to MS but a lower content of haem iron. Large differences between muscles were observed in relative amounts of most of the major fatty acids. The LT muscle had higher saturated fatty acids (SFA) and n-6:n-3 fatty acid ratio, and lower polyunsaturated fatty acids (PUFA), PUFA:SFA ratio, unsaturation index and average fatty acid chain length than the ST and MS muscles. Muscle pH, redness and chroma were positively correlated with vitamin E and unsaturated lipids and negatively correlated with tyrosine, tryptophan, carbohydrates and saturated lipids, whereas muscle lightness and expressible juice showed similar correlations but an opposite sign with these variables.

Sclerosing rhabdomyosarcoma presenting in the masseter muscle: a case report.

Sclerosing rhabdomyosarcoma (SRMS) is exceedingly rare, and may cause a great diagnostic confusion. Histologically, it is characterized by abundant extracellular hyalinized matrix mimicking primitive chondroid or osteoid tissue. So, it may be easily misdiagnosed as chondrosarcoma, osteosarcoma, angiosarcoma and so on. Herein, we report a case of SRMS occurring in the masseter muscle in a 40-year-old male. The tumor showed a diverse histological pattern. The tumor cells were arranged into nests, cords, pseudovascular, adenoid, microalveoli and even single-file arrays. Immunostaining showed that the tumor was positive for the Vimentin, Desmin and MyoD1, and was negative for CK, P63, NSE, CD45, CD30, S-100, CD99, Myoglobin, CD68, CD34, CD31, and α-SMA. Based on the morphological finding and immunostaining, it was diagnosed as a SRMS. In addition, focally, our case also displayed a cribriform pattern resembling adenoid cystic carcinoma. This may represent a new histological feature which can broaden the histological spectrum of this tumor and also may lead to diagnostic confusion. VIRTUAL SLIDES: The virtual slide(s) for this article can be found here: http://www.diagnosticpathology.diagnomx.eu/vs/1615846455818924.

Remarkable heterogeneity in myosin heavy-chain composition of the human young masseter compared with young biceps brachii.

Adult human jaw muscles differ from limb and trunk muscles in enzyme-histochemical fibre type composition. Recently, we showed that the human masseter and biceps differ in fibre type pattern already at childhood. The present study explored the myosin heavy-chain (MyHC) expression in the young masseter and biceps muscles by means of gel electrophoresis (GE) and immuno-histochemical (IHC) techniques. Plasticity in MyHC expression during life was evaluated by comparing the results with the previously reported data for adult muscles. In young masseter, GE identified MyHC-I, MyHC-IIa MyHC-IIx and small proportions of MyHC-fetal and MyHC-α cardiac. Western blots confirmed the presence of MyHC-I, MyHC-IIa and MyHC-IIx. IHC revealed in the masseter six isomyosins, MyHC-I, MyHC-IIa, MyHC-IIx, MyHC-fetal, MyHC α-cardiac and a previously not reported isoform, termed MyHC-IIx'. The majority of the masseter fibres co-expressed two to four isoforms. In the young biceps, both GE and IHC identified MyHC-I, MyHC-IIa and MyHC-IIx. MyHC-I predominated in both muscles. Young masseter showed more slow and less-fast and fetal MyHC than the adult and elderly masseter. These results provide evidence that the young masseter muscle is unique in MyHC composition, expressing MyHC-α cardiac and MyHC-fetal isoforms as well as hitherto unrecognized potential spliced isoforms of MyHC-fetal and MyHC-IIx. Differences in masseter MyHC expression between young adult and elderly suggest a shift from childhood to adulthood towards more fast contractile properties. Differences between masseter and biceps are proposed to reflect diverse evolutionary and developmental origins and confirm that the masseter and biceps present separate allotypes of muscle.

Human temporomandibular joint and myofascial pain biochemical profiles: a case-control study.

Neurobiological mechanisms of human musculoskeletal pain are poorly understood. This case-control study tested the hypothesis that biomarkers within temporomandibular muscle and joint disorders (TMJD) subjects' masseter muscles or temporomandibular joint (TMJ) synovial fluid correlate with plasma biomarker concentrations. Fifty subjects were recruited and categorized into TMJD cases (n=23) and pain-free controls (n=27) at the University of Minnesota School of Dentistry. Prior to specimen collection, pain intensity and pressure pain threshold masseter muscles and the TMJs were assessed. We collected venous blood; biopsied masseter muscle; and sampled TMJ synovial fluid on the subjects' side of maximum pain intensity. We assayed these tissues for the presence of nerve growth factor (NGF), bradykinin (BK), leukotreine B(4) (LTB(4) ) and prostaglandin E(2) (PGE(2) ), F(2) -isoprostane (F(2) I) and substance P (SP). The data was analyzed using Spearman Correlation Coefficients. We found that only plasma concentrations of bradykinin statistically correlated with synovial fluid concentrations (ρ=-0·48, P=0·005), but no association was found between pain intensities. The data suggests that biomarkers used to assess TMJD need to be acquired in a site-specific manner. We also discovered that F(2) I concentrations were associated with muscle pain intensity and muscle pressure pain threshold (PTT) (ß=0·4, 95%CI: 0·03-0·8) and joint PPT (ß=0·4, 95%CI: 0·07-0·8) suggesting that muscle oxidative stress is involved in myofascial pain and that F(2) -I may be a biomarker for myofascial pain.

Masseter myosin heavy chain composition varies with mandibular asymmetry.

Human jaw dysmorphologies are frequent and often affect young patients, resulting in malocclusion of teeth and inappropriate jaw relationships. Treatment is performed by means of orthodontics with orthognathic surgery as required. Mandibular asymmetry is one of the most frequent dysmorphologies, but in many cases, the specific cause is unknown.In healthy patients who were undergoing orthognathic surgery for correction of malocclusion, we tested the hypothesis that masseter muscle phenotype composition, which determines contractile properties, was different between sides in patients with mandibular asymmetry but not in those without mandibular asymmetry. After cephalometric analysis, 50 patients from whom we obtained samples of both right and left masseter muscles were separated into 2 groups: with or without mandibular lateral deviation. Samples were immunostained with myosin-isoform-specific antibodies to identify 4 skeletal muscle fiber types, and their fiber areas and proportions were measured. Two-tailed Wilcoxon test for paired samples was used to compare the 4 fiber-type compositions by means of percent occupancy and mean fiber area on both sides. Patients with mandibular asymmetry were associated with a significant increase of type II fiber occupancy (P = 0.0035) on the same side as the deviation. This finding that masseter muscle phenotype is significantly linked to mandibular asymmetry is of relevance to physiotherapeutic and surgical managements of jaw discrepancies and merits further investigation in the light of its possible role in the etiology of this condition.

Proteome analysis of whole and water-soluble proteins in masseter and semitendinosus muscles of Holstein cows.

To assess both quantitative and qualitative differences between the slow- and fast-type muscles, masseter (slow) and semitendinosus (fast) from four Holstein cows were analyzed by two-dimensional difference gel electrophoresis (2D DIGE) and mass spectrometry. The proteome analysis identified 27 spots as 20 proteins in the whole protein fraction extracted with 8 mol/L urea solution, and 16 spots were identified as 11 proteins in the water-soluble protein fraction. Two slow-type myofibrillar proteins (myosin light chain-1 slow-b and myosin light chain-2 slow), and aconitase-2 mitochondria were present at higher levels in the masseter muscle (P < 0.05). Four fast-type myofibrillar proteins (myosin light chain-1 fast, myosin light chain-2 fast, myosin light chain-3 fast and tropomyosin-1), and three enzymes of glycolytic pathway (enolase-3, aldolase-A and triosephosphate isomerase), were present at higher levels in the semitendinosus muscle (P < 0.05). Our proteome analysis showed that the composition of sarcoplasmic proteins as well as myofibrillar proteins was clearly different between slow- and fast-type muscles.

Interstitial glutamate concentration is elevated in the masseter muscle of myofascial temporomandibular disorder patients.

AIM: To determine if myofascial temporomandibular disorder (TMD) pain patients have elevated interstitial concentrations of glutamate in the masseter muscle. METHODS: Thirteen patients (3 men, 10 women) diagnosed with myofascial TMD pain and 10 (2 men, 8 women) age-matched healthy controls participated in a single microdialysis session. Microdialysis was performed in the patients in the most painful point of the masseter muscle, while in the healthy subjects a standardized point in the muscle was chosen. Two microdialysis samples were collected over 40-minute epochs. A blood sample was also taken for analysis of plasma glutamate concentration. Numeric rating scale (NRS) scores of pain intensity and unpleasantness, McGill Pain Questionnaire data, pain drawing areas, pressure pain thresholds, pressure pain tolerances, maximum voluntary bite force, and maximum voluntary mouth opening were collected as secondary measurements. RESULTS: The median concentration of glutamate in the masseter muscle of the myofascial TMD pain patients (7.5 ± 2.6 ΜM) was significantly higher (P < .023, Mann-Whitney test) than the concentration in healthy controls (0.5 ± 0.4 ΜM). There were, however, no significant correlations between glutamate concentrations in the masseter muscle and NRS pain scores. Plasma concentrations of glutamate were similar in patients and healthy controls. CONCLUSIONS: The present study demonstrates a marked increase in interstitial glutamate concentration in the masseter muscle of myofascial TMD pain patients. These novel findings suggest that peripheral glutamate could be involved in the pathophysiology of myofascial TMD pain.

Effects of increased occlusal vertical dimension on daily activity and myosin heavy chain composition in rat jaw muscle.

Mammalian skeletal muscles change their contractile-protein phenotype in response to mechanical loading and/or chronic electrical stimulation, implying that the phenotypic changes in masticatory muscles might result from new masticatory-loading conditions. To analyze the effects of increased occlusal vertical dimension (OVD) on daily activities and fibre-type compositions in jaw muscles, we measured the total duration of daily activity (duty time) and the myosin heavy chain (MyHC) compositions in the masseter and digastric muscles of freely moving control and bite-opened rats. In the control state, the duty time of the digastric muscle was higher than that of the masseter muscle at activity levels exceeding 5 and 20% of the day's peak activity. The opposite was true at activity levels exceeding 50 and 80% of the day's peak activity. The MyHCs consisted of a mixture of fast and slow types in the digastric muscle. The masseter consisted of mostly fast-type MyHC. The increment of OVD increased not only the duty time at activity levels exceeding 5, 20, 50 and 80% of the day' peak activity in both muscles but also the proportion of MyHC IIa in the masseter muscle and MyHC I in the digastric muscle at the expense of that of MyHC IIb. These results suggest that the increment of OVD changes masseter and digastric muscles towards slower phenotypes by an increase in their daily activities.

Seasonal variation in glucose and neutral amino acid uptake in the estuarine crab Neohelice granulata.

This study investigates the mechanisms of glucose and amino acid transport in gills and jaw muscle of N. granulata collected from an estuarine natural population. The physicochemical parameters of the estuarine environment and of this crustacean's hemolymph were measured during different seasons of the year. In summer, the lagoon water osmolality increased (5-6 times), and hemolymph osmolality decreased. In fall, water pH increased, whereas hemolymph pH decreased markedly. In all seasons, 2-deoxi glucose (DG) uptake in gills was significantly higher than 3-O methyl-glucose (MG) uptake. Phloretin reduced DG uptake in gills; phloretin and phlorizin did not affect MG uptake in this organ. DG and MG uptake was highest in gills during spring and summer. In jaw muscle, MG uptake in winter and spring was higher than DG uptake. In fall, gill methyl aminoisobutyric acid (MeAIB) uptake increased. In jaw muscle, MeAIB uptake was higher in spring. The observed changes in glucose uptake and in the type of glucose and amino acid transporter used in gills and muscle appear to be strategies used by N. granulata to minimize seasonal oscillations in the environmental parameters of their estuarine habitat.

Masticatory myosin unveiled: first determination of contractile parameters of muscle fibers from carnivore jaw muscles.

Masticatory myosin heavy chain (M MyHC) is a myosin subunit isoform with expression restricted to muscles derived from the first branchial arch, such as jaw-closer muscles, with pronounced interspecies variability. Only sparse information is available on the contractile properties of muscle fibers expressing M MyHC (M fibers). In this study, we characterized M fibers isolated from the jaw-closer muscles (temporalis and masseter) of two species of domestic carnivores, the cat and the dog, compared with fibers expressing slow or fast (2A, 2X, and 2B) isoforms. In each fiber, during maximally calcium-activated contractions at 12 degrees C, we determined isometric-specific tension (P(o)), unloaded shortening velocity (v(o)) with the slack test protocol, and the rate constant of tension redevelopment (K(TR)) after a fast shortening-relengthening cycle. At the end of the mechanical experiment, we identified MyHC isoform composition of each fiber with gel electrophoresis. Electrophoretic migration rate of M MyHC was similar in both species. We found that in both species the kinetic parameters v(o) and K(TR) of M fibers were similar to those of 2A fibers, whereas P(o) values were significantly greater than in any other fiber types. The similarity between 2A and M fibers and the greater tension development of M fibers were confirmed also in mechanical experiments performed at 24 degrees C. Myosin concentration was determined in single fibers and found not different in M fibers compared with slow and fast fibers, suggesting that the higher tension developed by M fibers does not find an explanation in a greater number of force generators. The specific mechanical characteristics of M fibers might be attributed to a diversity in cross-bridge kinetics.

Kinetic analysis of the slow skeletal myosin MHC-1 isoform from bovine masseter muscle.

Several heavy chain isoforms of class II myosins are found in muscle fibres and show a large variety of different mechanical activities. Fast myosins (myosin heavy chain (MHC)-II-2) contract at higher velocities than slow myosins (MHC-II-1, also known as beta-myosin) and it has been well established that ADP binding to actomyosin is much tighter for MHC-II-1 than for MHC-II-2. Recently, we reported several other differences between MHC-II isoforms 1 and 2 of the rabbit. Isoform II-1 unlike II-2 gave biphasic dissociation of actomyosin by ATP, the ATP-cleavage step was significantly slower for MHC-II-1 and the slow isoforms showed the presence of multiple actomyosin-ADP complexes. These results are in contrast to published data on MHC-II-1 from bovine left ventricle muscle, which was more similar to the fast skeletal isoform. Bovine MHC-II-1 is the predominant isoform expressed in both the ventricular myocardium and slow skeletal muscle fibres such as the masseter and is an important source of reference work for cardiac muscle physiology. This work examines and extends the kinetics of bovine MHC-II-1. We confirm the primary findings from the work on rabbit soleus MHC-II-1. Of significance is that we show that the affinity of ADP for bovine masseter myosin in the absence of actin (represented by the dissociation constant K(D)) is weaker than originally described for bovine cardiac myosin and thus the thermodynamic coupling between ADP and actin binding to myosin is much smaller (K(AD)/K(D) approximately 5 instead of K(AD)/K(D) approximately 50). This may indicate a distinct type of mechanochemical coupling for this group of myosin motors. We also find that the ATP-hydrolysis rate is much slower for bovine MHC-II-1 (19 s(-1)) than reported previously (138 s(-1)). We discuss how this work fits into a broader characterisation of myosin motors from across the myosin family.

Myosin heavy chain mRNA isoforms in masseter muscle before and after orthognathic surgery.

OBJECTIVES: Orthognathic surgery leads to changed jaw position and force vector of mastication to which the muscles must adapt. The aim of the present study was to determine the relative expression of myosin heavy chain (MyHC) messenger RNA (mRNA) isoforms in different types of human masseter muscle fiber under consideration of change in the number of occlusal contacts before and 6 months after surgery. STUDY DESIGN: Muscle biopsies were taken from the anterior and posterior parts of both sides in 30 patients with prognathic and retrognathic mandibles. Specific mRNA MyHC analysis was made by real-time polymerase chain reaction to quantify the isoforms I, IIa, and IId/x. RESULTS: There was a shift in the relative content from type I (46% before, 37% after) to type IIa (29% before, 42% after). This shift correlates with number of teeth in occlusion. CONCLUSIONS: Correlation between isoform shift and number of teeth in occlusion indicates higher mastication force which stabilizes the treatment result.

Cross-bridge kinetics of fast and slow fibres of cat jaw and limb muscles: correlations with myosin subunit composition.

Mechanical properties of the jaw-closing muscles of the cat are poorly understood. These muscles are known to differ in myosin and fibre type compositions from limb muscles. This work aims to correlate mechanical properties of single fibres in cat jaw and limb muscles with their myosin subunit compositions. The stiffness minimum frequency, f(min), which reflects isometric cross-bridge kinetics, was measured in Ca(2+)-activated glycerinated fast and slow fibres from cat jaw and limb muscles for temperatures ranging between 15 and 30 degrees C by mechanical perturbation analysis. At 15 degrees C, f(min) was 0.5 Hz for limb-slow fibres, 4-6 Hz for jaw-slow fibres, and 10-13 Hz for limb-fast and jaw-fast fibres. The activation energy for f(min) obtained from the slope of the Arrhenius plot for limb-slow fibres was 30-40% higher than values for the other three types of fibres. SDS-PAGE and western blotting using highly specific antibodies verified that limb-fast fibres contained IIA or IIX myosin heavy chain (MyHC). Jaw-fast fibres expressed masticatory MyHC while both jaw-fast and jaw-slow fibres expressed masticatory myosin light chains (MLCs). The nucleotide sequences of the 3' ends of the slow MyHC cDNAs isolated from cat masseter and soleus cDNA libraries showed identical coding and 3'-untranslated regions, suggesting that jaw-slow and limb-slow fibres express the same slow MyHC gene. We conclude that the isometric cross-bridge cycling kinetics of jaw-fast and limb-fast fibres detected by f(min) are indistinguishable in spite of differences in MyHC and light chain compositions. However, jaw-slow fibres, in which the same slow MyHCs are found in combination with MLCs of the jaw type, show enhanced cross-bridge cycling kinetics and reduced activation energy for cross-bridge detachment.

Change of mRNA amount of myosin heavy chain in masseter muscle after orthognathic surgery of patients with malocclusion.

INTRODUCTION: Surgical correction of malocclusion changes the force to moment ratio of masticatory muscles inserting at the mandible caused by shortening, lengthening and rotation of the bone following osteotomy. During muscle adaptation the expression of mRNA for the myosin heavy chain (MyHC) of type I and type II fibres may be changed. MATERIAL AND METHODS: The adaptation of the masseter muscle was investigated at the mRNA level in 10 patients 6 months after orthognathic surgery in the mandible. The competitive polymerase chain reaction (cPCR) is a suitable method for quantification of MyHC mRNA. For application of this minimal invasive method an amount of 35 mg muscle tissue was sufficient. RESULTS: 6 month postoperatively there was a deficiency of about 87% of MyHC mRNA for fibre type I and II in both groups of patients. The deficiency in patients with mesial position of the mandible was higher but not significant different to patients with distal malocclusion. CONCLUSION: Patients should use the postoperative interval for training their masticatory muscles. This improves the stability of treatment result and prevents relapse.