scholarly journals A distinct cardiopharyngeal mesoderm genetic hierarchy establishes antero-posterior patterning of esophagus striated muscle

2019 ◽  
Author(s):  
Glenda Comai ◽  
Églantine Heude ◽  
Sebastien Mella ◽  
Sylvain Paisant ◽  
Francesca Pala ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Striated Muscle ◽  
Striated Muscles ◽  
Loss Of Function ◽  
Pharmacological Studies ◽  
Posterior Migration ◽  
Functional Relevance ◽  
Genetic Signatures ◽  
Genetic Hierarchy

SUMMARYIn most vertebrates, the upper digestive tract is composed of muscularised jaws linked to the esophagus that permit food uptake and swallowing. Masticatory and esophagus striated muscles (ESM) share a common cardiopharyngeal mesoderm (CPM) origin, however ESM are unusual among striated muscles as they are established in the absence of a primary skeletal muscle scaffold. Using mouse chimeras, we show that the transcription factors Tbx1 and Isl1 are required cell-autonomously for myogenic specification of ESM progenitors. Further, genetic loss-of-function and pharmacological studies point to Met/HGF signalling for antero-posterior migration of esophagus muscle progenitors, where HGF ligand is expressed in adjacent smooth muscle cells. These observations highlight the functional relevance of a smooth and striated muscle progenitor dialogue for ESM patterning. Our findings establish a Tbx1-Isl1-Met genetic hierarchy that uniquely regulate esophagus myogenesis and identify distinct genetic signatures that can be used as a framework to interpret pathologies arising within CPM derivatives.

scholarly journals A distinct cardiopharyngeal mesoderm genetic hierarchy establishes antero-posterior patterning of esophagus striated muscle

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Glenda Comai ◽  
Eglantine Heude ◽  
Sebastian Mella ◽  
Sylvain Paisant ◽  
Francesca Pala ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Striated Muscle ◽  
Striated Muscles ◽  
Food Ingestion ◽  
Loss Of Function ◽  
Pharmacological Studies ◽  
Posterior Migration ◽  
Functional Relevance ◽  
Genetic Signatures ◽  
Genetic Hierarchy

In most vertebrates, the upper digestive tract is composed of muscularized jaws linked to the esophagus that permits food ingestion and swallowing. Masticatory and esophagus striated muscles (ESM) share a common cardiopharyngeal mesoderm (CPM) origin, however ESM are unusual among striated muscles as they are established in the absence of a primary skeletal muscle scaffold. Using mouse chimeras, we show that the transcription factors Tbx1 and Isl1 are required cell-autonomously for myogenic specification of ESM progenitors. Further, genetic loss-of-function and pharmacological studies point to MET/HGF signaling for antero-posterior migration of esophagus muscle progenitors, where Hgf ligand is expressed in adjacent smooth muscle cells. These observations highlight the functional relevance of a smooth and striated muscle progenitor dialogue for ESM patterning. Our findings establish a Tbx1-Isl1-Met genetic hierarchy that uniquely regulates esophagus myogenesis and identify distinct genetic signatures that can be used as framework to interpret pathologies arising within CPM derivatives.

scholarly journals The subcellular distribution of dystrophin in mouse skeletal, cardiac, and smooth muscle.

1991 ◽  
Vol 115 (2) ◽  
pp. 411-421 ◽  
Author(s):  
T J Byers ◽  
L M Kunkel ◽  
S C Watkins
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Plasma Membrane ◽  
Cardiac Muscle ◽  
Striated Muscle ◽  
Adherens Junctions ◽  
Myotendinous Junction ◽  
Elevated Concentration ◽  
Western Blots ◽  
Functional Roles

We use a highly specific and sensitive antibody to further characterize the distribution of dystrophin in skeletal, cardiac, and smooth muscle. No evidence for localization other than at the cell surface is apparent in skeletal muscle and no 427-kD dystrophin labeling was detected in sciatic nerve. An elevated concentration of dystrophin appears at the myotendinous junction and the neuromuscular junction, labeling in the latter being more intense specifically in the troughs of the synaptic folds. In cardiac muscle the distribution of dystrophin is limited to the surface plasma membrane but is notably absent from the membrane that overlays adherens junctions of the intercalated disks. In smooth muscle, the plasma membrane labeling is considerably less abundant than in cardiac or skeletal muscle and is found in areas of membrane underlain by membranous vesicles. As in cardiac muscle, smooth muscle dystrophin seems to be excluded from membrane above densities that mark adherens junctions. Dystrophin appears as a doublet on Western blots of skeletal and cardiac muscle, and as a single band of lower abundance in smooth muscle that corresponds most closely in molecular weight to the upper band of the striated muscle doublet. The lower band of the doublet in striated muscle appears to lack a portion of the carboxyl terminus and may represent a dystrophin isoform. Isoform differences and the presence of dystrophin on different specialized membrane surfaces imply multiple functional roles for the dystrophin protein.

scholarly journals THE ULTRASTRUCTURE OF FROG VENTRICULAR CARDIAC MUSCLE AND ITS RELATIONSHIP TO MECHANISMS OF EXCITATION-CONTRACTION COUPLING

1968 ◽  
Vol 38 (1) ◽  
pp. 99-114 ◽  
Author(s):  
Nancy A. Staley ◽  
Ellis S. Benson
Keyword(s):  
Skeletal Muscle ◽  
Cardiac Muscle ◽  
Striated Muscle ◽  
Structural Features ◽  
Mammalian Skeletal Muscle ◽  
Striated Muscles ◽  
Thin Filaments ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Dense Granules

Frog ventricular cardiac muscle has structural features which set it apart from frog and mammalian skeletal muscle and mammalian cardiac muscle. In describing these differences, our attention focused chiefly on the distribution of cellular membranes. Abundant inter cellular clefts, the absence of tranverse tubules, and the paucity of sarcotubules, together with exceedingly small cell diameters (less than 5 µ), support the suggestion that the mechanism of excitation-contraction coupling differs in these muscle cells from that now thought to be characteristic of striated muscle such as skeletal muscle and mammalian cardiac muscle. These structural dissimilarities also imply that the mechanism of relaxation in frog ventricular muscle differs from that considered typical of other striated muscles. Additional ultrastructural features of frog ventricular heart muscle include spherical electron-opaque bodies on thin filaments, inconstantly present, forming a rank across the I band about 150 mµ from the Z line, and membrane-bounded dense granules resembling neurosecretory granules. The functional significance of these features is not yet clear.

scholarly journals Chemical and immunochemical characteristics of tropomyosins from striated and smooth muscle

1974 ◽  
Vol 141 (1) ◽  
pp. 43-49 ◽  
Author(s):  
Peter Cummins ◽  
S. Victor Perry
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Cardiac Muscle ◽  
Skeletal Muscles ◽  
Striated Muscle ◽  
Β Subunit ◽  
Muscle Type ◽  
Amphibian Species ◽  
Species Specific ◽  
Immunochemical Characteristics

1. On electrophoresis in dissociating conditions the tropomyosins isolated from skeletal muscles of mammalian, avian and amphibian species migrated as two components. These were comparable with the α and β subunits of tropomyosin present in rabbit skeletal muscle. 2. The α and β components of all skeletal-muscle tropomyosins contained 1 and 2 residues of cysteine per 34000g respectively. 3. The ratio of the amounts of α and β subunit present in skeletal muscle tropomyosins was characteristic for the muscle type. Muscle consisting of slow red fibres contained a greater proportion of β-tropomyosin than muscles consisting predominantly of white fast fibres. 4. Mammalian and avian cardiac muscle tropomyosins consisted of α-tropomyosin only. 5. Mammalian and avian smooth-muscle tropomyosins differed both chemically and immunologically from striated-muscle tropomyosins. 6. Antibody raised against rabbit skeletal α-tropomyosin was species non-specific, reacting with all other striated muscle α-tropomyosin subunits tested. 7. Antibody raised against rabbit skeletal β-tropomyosin subunit was species-specific.

Proteins of the contractile mechanism of mammalian smooth muscle and their possible location in the cell

1964 ◽  
Vol 160 (981) ◽  
pp. 517-524 ◽  
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Sedimentation Rate ◽  
Striated Muscle ◽  
Muscle Actin ◽  
Trypsin Treatment ◽  
Skeletal Muscle Myosin ◽  
Uterine Smooth Muscle ◽  
Muscle Myosin ◽  
Viscous Behaviour

Dorothy M. Needham speaking. Since the pioneer work of Csapo and his colleagues, beginning about fifteen years ago, it has been realized that from uterine smooth muscle can be extracted a protein closely resembling skeletal-muscle actomyosin in its viscous behaviour, sedimentation rate and electrophoretic mobility. (See, for example, Csapo 1948, 1949, 1950, 1959; Csapo, Erdos, Naeslund & Snellman 1950; Naeslund & Snellman 1951). Later work, in which the properties of purified preparations of myosin, actin and actomyosin have been studied, bears out these earlier conclusions. Thus, for example, we have shown (Needham & Williams 1963 b ) that skeletal-muscle myosin will react normally with uterus actin to give the highly viscous actomyosin; and similarly uterus myosin with skeletal-muscle actin. In both types of experiment the results indicated that the two proteins associated together in about the same proportions as when both are derived from skeletal muscle. Uterus actomyosin may be fragmented by carefully controlled trypsin treatment giving light and heavy meromyosins which, so far as they have been studied, show similar properties to the meromyosins from skeletal-muscle actomyosin (Needham & Williams 1959; Cohen, Lowey & Kucera 1961). Smooth muscle, however, does contain very strikingly less actomyosin than striated muscle, only 6 to 10 mg/g wet wt as compared with about 70 mg/g wet wt in skeletal muscle (Needham & Williams 1963 a ).

scholarly journals Troponin Variants as Markers of Skeletal Muscle Health and Diseases

2021 ◽  
Vol 12 ◽  
Author(s):  
Monica Rasmussen ◽  
Jian-Ping Jin
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Striated Muscle ◽  
Troponin T ◽  
Muscle Quality ◽  
Striated Muscles ◽  
Thin Filaments ◽  
Age Related ◽  
Development And Aging ◽  
Regulation Of Muscle Contraction

Ca2+-regulated contractility is a key determinant of the quality of muscles. The sarcomeric myofilament proteins are essential players in the contraction of striated muscles. The troponin complex in the actin thin filaments plays a central role in the Ca2+-regulation of muscle contraction and relaxation. Among the three subunits of troponin, the Ca2+-binding subunit troponin C (TnC) is a member of the calmodulin super family whereas troponin I (TnI, the inhibitory subunit) and troponin T (TnT, the tropomyosin-binding and thin filament anchoring subunit) are striated muscle-specific regulatory proteins. Muscle type-specific isoforms of troponin subunits are expressed in fast and slow twitch fibers and are regulated during development and aging, and in adaptation to exercise or disuse. TnT also evolved with various alternative splice forms as an added capacity of muscle functional diversity. Mutations of troponin subunits cause myopathies. Owing to their physiological and pathological importance, troponin variants can be used as specific markers to define muscle quality. In this focused review, we will explore the use of troponin variants as markers for the fiber contents, developmental and differentiation states, contractile functions, and physiological or pathophysiological adaptations of skeletal muscle. As protein structure defines function, profile of troponin variants illustrates how changes at the myofilament level confer functional qualities at the fiber level. Moreover, understanding of the role of troponin modifications and mutants in determining muscle contractility in age-related decline of muscle function and in myopathies informs an approach to improve human health.

scholarly journals The 3-methylhistidine content of human tissues

1979 ◽  
Vol 42 (3) ◽  
pp. 567-570 ◽  
Author(s):  
M. Elia ◽  
A. Carter ◽  
R. Smith
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Dry Weight ◽  
Human Tissues ◽  
Post Mortem ◽  
Striated Muscles ◽  
Significant Difference ◽  
Use Values ◽  
Liver And Kidney ◽  
The Mean

1. The amount of 3-methylhistidine (3-MeH) has been measured in eighty-eight samples of tissue taken Post-mortem from five adults.2. The highest concentration (μmol/g fat-free dry weight) of 3-MeH was in skeletal muscle (3.31 ± 0.05); intermediate values (2–3) were found in cardiac muscle and those tissues containing smooth muscle; and low values (less than I) occurred in parenchymal tissues such as liver and kidney.3. There was little variation between the mean 3-MeH content of striated muscles in different individuals, and no significant difference between the 3-MeH concentrations of striated muscles taken from six different sites.4. The results suggest that it is justifiable to use values obtained from single muscles to calculate the rate of myofibrillar breakdown from urinary 3-MeH excretion.

scholarly journals Contractile Properties of Esophageal Striated Muscle: Comparison with Cardiac and Skeletal Muscles in Rats

2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Takahiko Shiina ◽  
Takeshi Shima ◽  
Kazuaki Masuda ◽  
Haruko Hirayama ◽  
Momoe Iwami ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Striated Muscle ◽  
Electrical Field Stimulation ◽  
Muscle Layer ◽  
Contractile Properties ◽  
High Frequency Stimulation ◽  
Striated Muscles ◽  
High Potassium ◽  
Contractile Responses ◽  
Esophageal Muscle

The external muscle layer of the mammalian esophagus consists of striated muscles. We investigated the contractile properties of esophageal striated muscle by comparison with those of skeletal and cardiac muscles. Electrical field stimulation with single pulses evoked twitch-like contractile responses in esophageal muscle, similar to those in skeletal muscle in duration and similar to those in cardiac muscle in amplitude. The contractions of esophageal muscle were not affected by an inhibitor of gap junctions. Contractile responses induced by high potassium or caffeine in esophageal muscle were analogous to those in skeletal muscle. High-frequency stimulation induced a transient summation of contractions followed by sustained contractions with amplitudes similar to those of twitch-like contractions, although a large summation was observed in skeletal muscle. The results demonstrate that esophageal muscle has properties similar but not identical to those of skeletal muscle and that some specific properties may be beneficial for esophageal peristalsis.

scholarly journals An invertebrate smooth muscle with striated muscle myosin filaments

2015 ◽  
Vol 112 (42) ◽  
pp. E5660-E5668 ◽  
Author(s):  
Guidenn Sulbarán ◽  
Lorenzo Alamo ◽  
Antonio Pinto ◽  
Gustavo Márquez ◽  
Franklin Méndez ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Actin Filaments ◽  
Striated Muscle ◽  
Smooth Muscles ◽  
Structural Similarity ◽  
Striated Muscles ◽  
Muscle Tissues ◽  
Myosin Filaments ◽  
Muscle Myosin ◽  
Surprising Finding

Muscle tissues are classically divided into two major types, depending on the presence or absence of striations. In striated muscles, the actin filaments are anchored at Z-lines and the myosin and actin filaments are in register, whereas in smooth muscles, the actin filaments are attached to dense bodies and the myosin and actin filaments are out of register. The structure of the filaments in smooth muscles is also different from that in striated muscles. Here we have studied the structure of myosin filaments from the smooth muscles of the human parasite Schistosoma mansoni. We find, surprisingly, that they are indistinguishable from those in an arthropod striated muscle. This structural similarity is supported by sequence comparison between the schistosome myosin II heavy chain and known striated muscle myosins. In contrast, the actin filaments of schistosomes are similar to those of smooth muscles, lacking troponin-dependent regulation. We conclude that schistosome muscles are hybrids, containing striated muscle-like myosin filaments and smooth muscle-like actin filaments in a smooth muscle architecture. This surprising finding has broad significance for understanding how muscles are built and how they evolved, and challenges the paradigm that smooth and striated muscles always have distinctly different components.

scholarly journals Anatomy of Cowper’s gland in humans suggesting a secretion and emission mechanism facilitated by cooperation of striated and smooth muscles

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Satoru Muro ◽  
Janyaruk Suriyut ◽  
Keiichi Akita
Keyword(s):  
Smooth Muscle ◽  
Striated Muscle ◽  
Three Dimensional ◽  
Smooth Muscles ◽  
Levator Ani ◽  
Striated Muscles ◽  
External Urethral Sphincter ◽  
Macroscopic Anatomy ◽  
Dimensional Reconstruction ◽  
Perineal Muscle

AbstractThis study presents the detailed anatomy of the Cowper’s gland in humans. Elucidating the mechanism of secretion and emission of the Cowper’s gland requires analysis of the muscles around the Cowper’s gland. We hypothesized that the Cowper’s gland involves not only smooth muscle but also the striated muscles of the pelvic floor. Here, we provide comprehensive and three-dimensional anatomy of the Cowper’s gland and its surrounding structures, which overcomes the current local and planar understanding. In this study, seven male corpses of body donors were used to conduct macroscopic anatomy, histology, and three-dimensional reconstruction. The Cowper’s gland was surrounded laterally and posterosuperiorly by striated and smooth muscles, respectively. The striated muscle bundle was connected from the superficial transverse perineal muscle, levator ani, and external anal sphincter to the external urethral sphincter (rhabdosphincter). The smooth muscle was part of the deep transverse perineal muscle and entered between the bilateral Cowper’s glands and lobules. Our findings indicate that the secretion and emission of the Cowper’s gland in humans are carried out through the cooperation of striated and smooth muscles.

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