ABSTRACT
SUMMARY: Both the masseter and medial pterygoid muscles elevate the mandible, raising the lower jaw by acting simultaneously on the lateral and medial surfaces of the mandibular ramus. Nevertheless, electromyographic studies indicate that these muscles, as well as the superficial and deep heads of the masseter, act in a different way during mastication. We have analyzed by real time quantitative polymerase chain reaction (RT-qPCR) the expression of myosin heavy chain (MHC) isoforms in the masseter and medial pterygoid muscles in humans in order to identify possible differences in the expression patterns that may be related to functional differences identified with electromyography. Our findings indicate that the expression pattern of MHC isoforms in the two muscles is characteristic of fast and powerful phasic muscles. We have also observed a high percentage of expression of the MHC-IIx isoform and the expression of the MHC-M isoform at the mRNA level in both muscles, an isoform that does not translate into protein in the masticatory muscles of humans. The high percentage of expression of the MHC-IIx isoform in humans can be related to a high contractile speed of the masseter and medial pterygoid in humans. On the other hand, the low percentage of expression of the MHC-M isoform at the mRNA level in both muscles can be related to the complex evolutionary process that has reduced the size and force of the masticatory muscles in humans.
RESUMEN: Los músculos masetero y pterigoideo medial elevan la mandíbula actuando de forma simultánea sobre las caras lateral y medial de su rama. Sin embargo, los estudios electromiográficos indican que estos dos músculos actúan de forma diferente durante la masticación, de la misma forma que lo hacen las porciones superficial y profunda del músculo masetero. En el presente estudio hemos analizado mediante PCR en tiempo real la expresión de las isoformas de la cadena pesada de la miosina o myosin heavy chain (MHC) en los músculos masetero y pterigoideo medial en humanos, con la finalidad de identificar diferencias en los patrones de expresión que se puedan relacionar con las diferencias funcionales identificadas con la electromiografía. Nuestros resultados indican que el patrón de expresión de las isoformas de la MHC en los dos músculos es la característica de los músculos rápidos y potentes. También hemos observado un elevado porcentaje de expresión de la isoforma MHC-IIx y la expresión a nivel de ARNm de la isoforma MHC-M en los dos músculos, una isoforma que no se detecta a nivel de proteína en los músculos masticadores humanos. El elevado porcentaje de expresión de la isoforma MHC-IIx que hemos observado se puede relacionar con una elevada velocidad de contracción de los músculos masetero y pterigoideo medial en los humanos. Por otro lado, el bajo porcentaje de expresión de la isoforma MHC-M a nivel de ARNm en ambos músculos se puede relacionar con los procesos evolutivos complejos que han reducido el tamaño y la fuerza de los músculos masticadores en los humanos.
Subject(s)
Humans , Male , Female , Adult , Middle Aged , Aged , Aged, 80 and over , Pterygoid Muscles/metabolism , Myosin Heavy Chains/metabolism , Masseter Muscle/metabolism , Cadaver , Myosin Heavy Chains/genetics , RNA Isoforms/metabolism , Real-Time Polymerase Chain ReactionABSTRACT
The maxilla and masseter muscles are components of the stomatognathic system involved in chewing, which is frequently affected by physical forces such as gravity, and by dental, orthodontic and orthopedic procedures. Thyroid hormones (TH) are known to regulate the expression of genes that control bone mass and the oxidative properties of muscles; however, little is known about the effects of TH on the stomatognathic system. This study investigated this issue by evaluating: i) osteoprotegerin (OPG) and osteopontine (OPN) mRNA expression in the maxilla and ii) myoglobin (Mb) mRNA and protein expression, as well as fiber composition of the masseter. Male Wistar rats (~250 g) were divided into thyroidectomized (Tx) and sham-operated (SO) groups (N = 24/group) treated with T3 or saline (0.9 percent) for 15 days. Thyroidectomy increased OPG (~40 percent) and OPN (~75 percent) mRNA expression, while T3 treatment reduced OPG (~40 percent) and OPN (~75 percent) in Tx, and both (~50 percent) in SO rats. Masseter Mb mRNA expression and fiber type composition remained unchanged, despite the induction of hypo- and hyperthyroidism. However, Mb content was decreased in Tx rats even after T3 treatment. Since OPG and OPN are key proteins involved in the osteoclastogenesis inhibition and bone mineralization, respectively, and that Mb functions as a muscle store of O2 allowing muscles to be more resistant to fatigue, the present data indicate that TH also interfere with maxilla remodeling and the oxidative properties of the masseter, influencing the function of the stomatognathic system, which may require attention during dental, orthodontic and orthopedic procedures in patients with thyroid diseases.
Subject(s)
Animals , Male , Rats , Masseter Muscle/drug effects , Maxilla/drug effects , Myoglobin/metabolism , Osteopontin/metabolism , Osteoprotegerin/metabolism , Thyroid Hormones/physiology , Triiodothyronine/pharmacology , Blotting, Northern , Hyperthyroidism/physiopathology , Masseter Muscle/anatomy & histology , Masseter Muscle/metabolism , Maxilla/metabolism , Myoglobin/genetics , Osteopontin/genetics , Osteoprotegerin/genetics , Rats, Wistar , Reverse Transcriptase Polymerase Chain Reaction , RNA , RNA, Messenger/metabolism , Thyroidectomy , Thyroid Hormones/metabolismABSTRACT
The frequency, the distribution of fiber types, the area, the number of nuclei per fiber, the number and the morphological, metabolic and contractile characteristics of the muscle of the Masseter and Longissimus Dorsi muscles of Piau, Sorocaba and Large White breeds of pigs were studied. Superficial segments of these muscles were frozen in n-Hexane at -70 degree. For morphological studies, some cryostat sections (10µm) were stained with Hematoxylin Eosin (HE). For fiber typing, subsequent sections were reacted for NADH-TR and myofibrilar ATPase (m-ATPase) after alkaline (pH 10.4) and acid(pH 4.6) preincubations. Masseter muscle of Piau, Sorocaba and Large White pigs revealed a mosaic pattern of Slow Oxydative (SO) and Fast Oxydative Glycolytic (FOG) fibers with the following frequencies: 34.9 per cent and 64.4 per cent; 47.4 per cent and 52.6 per cent; 25,3 per cent and 74,7 per cent, respectively. The area of SO fibers was smaller than of FOG. Longissimus Dorsi muscle revealed three kinds of fibers, SO, FOG and Fast Glycolytic (FG), with frequencies of 12.5 per cent, 29.5 per cent and 57.9 per cent; 21.8 per cent, 21.8 per cent 56.4 per cent; 13.2 per cent, 17.6 per cent and 69.2 per cent, respectively. SO and FOG fibers were arranged in metabolic groups of 5-15 fibers. In Large White pigs, the frequency of SO fibers was significantly lower, while its area was larger. The number of nuclei per fiber was significantly greater in Large White and Sorocaba pigs than in the Piau.