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Z-disk
A sarcomere (Greek σάρξ ''sarx'' "flesh", μέρος ''meros'' "part") is the smallest functional unit of striated muscle tissue. It is the repeating unit between two Z-lines. Skeletal muscles are composed of tubular muscle cells (called muscle fibers or myofibers) which are formed during embryonic myogenesis. Muscle fibers contain numerous tubular myofibrils. Myofibrils are composed of repeating sections of sarcomeres, which appear under the microscope as alternating dark and light bands. Sarcomeres are composed of long, fibrous proteins as filaments that slide past each other when a muscle contracts or relaxes. The costamere is a different component that connects the sarcomere to the sarcolemma. Two of the important proteins are myosin, which forms the thick filament, and actin, which forms the thin filament. Myosin has a long, fibrous tail and a globular head, which binds to actin. The myosin head also binds to ATP, which is the source of energy for muscle movement. Myosi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Costamere
The costamere is a structural-functional component of striated muscle cells which connects the sarcomere of the muscle to the cell membrane (i.e. the sarcolemma).20: 2327-2331 Costameres are sub-sarcolemmal protein assemblies circumferentially aligned in register with the Z-disk of peripheral myofibrils. They physically couple force-generating sarcomeres with the sarcolemma in striated muscle cells and are thus considered one of several " Achilles' heels" of skeletal muscle, a critical component of striated muscle morphology which, when compromised, is thought to directly contribute to the development of several distinct myopathies. The dystrophin-associated protein complex, also referred to as the dystrophin-associated glycoprotein complex (DGC or DAGC), contains various integral and peripheral membrane proteins such as dystroglycans and sarcoglycans, which are thought to be responsible for linking the internal cytoskeletal system of individual myofibers to structural proteins ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nebulin
Nebulin is an actin-binding protein which is localized to the thin filament of the sarcomeres in skeletal muscle. Nebulin in humans is coded for by the gene ''NEB''. It is a very large protein (600–900 kDa) and binds as many as 200 actin monomers. Because its length is proportional to thin filament length, it is believed that nebulin acts as a thin filament "ruler" and regulates thin filament length during sarcomere assembly and acts as the coats the actin filament. Other functions of nebulin, such as a role in cell signaling, remain uncertain. Nebulin has also been shown to regulate actin-myosin interactions by inhibiting ATPase activity in a calcium- calmodulin sensitive manner. Mutations in nebulin cause some cases of the autosomal recessive disorder nemaline myopathy. A smaller member of the nebulin protein family, termed nebulette, is expressed in cardiac muscle. Structure The structure of the SH3 domain of nebulin was determined by protein nuclear magnetic resona ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Actin
Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm. An actin protein is the monomeric subunit of two types of filaments in cells: microfilaments, one of the three major components of the cytoskeleton, and thin filaments, part of the contractile apparatus in muscle cells. It can be present as either a free monomer called G-actin (globular) or as part of a linear polymer microfilament called F-actin (filamentous), both of which are essential for such important cellular functions as the mobility and contraction of cells during cell division. Actin participates in many important cellular processes, including muscle contraction, cell motility, cell division and cytokinesis, vesicle and organelle movement, cell sign ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Striated Muscle
{{disambiguation ...
Striations means a series of ridges, furrows or linear marks, and is used in several ways: * Glacial striation * Striation (fatigue), in material * Striation (geology), a ''striation'' as a result of a geological fault * Striation Valley, in Antarctica * In hyperbolic geometry, a ''striation'' is a reflection across two parallel mirrors. * In anatomy, striated muscle * Striations can be found in certain glasses. These have been caused by turbulent flow during teeming (pouring) of the glass. * Striations can be observed in clouds. See Barber's pole. * Ballistic fingerprinting Forensic firearm examination is the forensic process of examining the characteristics of firearms or bullets left behind at a crime scene. Specialists in this field try to link bullets to weapons and weapons to individuals. They can raise and re ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Antonie Van Leeuwenhoek
Antonie Philips van Leeuwenhoek ( ; ; 24 October 1632 – 26 August 1723) was a Dutch microbiologist and microscopist in the Golden Age of Dutch science and technology. A largely self-taught man in science, he is commonly known as " the Father of Microbiology", and one of the first microscopists and microbiologists. Van Leeuwenhoek is best known for his pioneering work in microscopy and for his contributions toward the establishment of microbiology as a scientific discipline. Raised in Delft, Dutch Republic, van Leeuwenhoek worked as a draper in his youth and founded his own shop in 1654. He became well recognized in municipal politics and developed an interest in lensmaking. In the 1670s, he started to explore microbial life with his microscope. This was one of the notable achievements of the Golden Age of Dutch exploration and discovery (). Using single-lensed microscopes of his own design and make, van Leeuwenhoek was the first to observe and to experiment with micro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Troponin C
Troponin C is a protein which is part of the troponin complex. It contains four calcium-binding EF hands, although different isoforms may have fewer than four functional calcium-binding subdomains. It is a component of thin filaments, along with actin and tropomyosin. It contains an N lobe and a C lobe. The C lobe serves a structural purpose and binds to the N domain of troponin I (TnI). The C lobe can bind either Ca2+ or Mg2+. The N lobe, which binds only Ca2+, is the regulatory lobe and binds to the C domain of troponin I after calcium binding. Isoforms The tissue specific subtypes are: * Slow troponin C, TNNC1 (3p21.1 ) * Fast troponin C, TNNC2 (20q12-q13.11, ) Mutations Point mutations can occur in troponin C inducing alterations to Ca2+ and Mg2+ binding and protein structure, leading to abnormalities in muscle contraction. In cardiac muscle, they are related to dilated cardiomyopathy (DCM) and hypertrophic cardiomyopathy (HCM). These known point mutations are: ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tropomyosin
Tropomyosin is a two-stranded alpha-helical, coiled coil protein found in actin-based cytoskeletons. Tropomyosin and the actin skeleton All organisms contain organelles that provide physical integrity to their cells. These type of organelles are collectively known as the cytoskeleton, and one of the most ancient systems is based on filamentous polymers of the protein actin. A polymer of a second protein, tropomyosin, is an integral part of most actin filaments in animals. Tropomyosins are a large family of integral components of actin filaments that play a critical role in regulating the function of actin filaments in both muscle and nonmuscle cells. These proteins consist of rod-shaped coiled-coil hetero- or homo- dimers that lie along the α-helical groove of most actin filaments. Interaction occurs along the length of the actin filament, with dimers aligning in a head-to-tail fashion. Tropomyosins are often categorised into two groups, muscle tropomyosin isoforms and nonmus ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sliding Filament Model
Sliding may refer to: *Sliding (dance), also floating or gliding, a group of footwork-oriented dance techniques *Slide (baseball), an attempt by a baseball runner to avoid getting tagged out *Sliding (motion) See also *Slide (other) Slide or Slides may refer to: Places * Slide, California, former name of Fortuna, California Arts, entertainment, and media Music Albums * ''Slide'' (Lisa Germano album), 1998 * ''Slide'' (George Clanton album), 2018 *''Slide'', by Patrick Glees ... * Slider (other) {{disambig ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Muscle Contraction
Muscle contraction is the activation of tension-generating sites within muscle cells. In physiology, muscle contraction does not necessarily mean muscle shortening because muscle tension can be produced without changes in muscle length, such as when holding something heavy in the same position. The termination of muscle contraction is followed by muscle relaxation, which is a return of the muscle fibers to their low tension-generating state. For the contractions to happen, the muscle cells must rely on the interaction of two types of filaments which are the thin and thick filaments. Thin filaments are two strands of actin coiled around each, and thick filaments consist of mostly elongated proteins called myosin. Together, these two filaments form myofibrils which are important organelles in the skeletal muscle system. Muscle contraction can also be described based on two variables: length and tension. A muscle contraction is described as isometric if the muscle tension changes ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Myomesin
Myomesin is a protein family found in the M-line of the sarcomere structure. Myomesin has various forms throughout the body in striated muscles with specialized functions. This includes both slow and fast muscle fibers. Myomesin are made of 13 domains including a unique N-terminal followed by two immunoglobulin-like (Ig) domains, five fibronectin type III (Fn) domains, five more Ig domains. These domains all promote binding which indicates that myomesin is regulated through binding. Functions Sarcomere structure Myomesin plays an important role in the structure of sarcomeres. They are found in the M-band region of the sarcomere, between the thick filaments (myosin). Its main purpose in this setting is to provide structural integrity by linking the antiparallel myosin fibers and titin filaments which are connected to the Z-discs. These myosin filaments form a hexagonal lattice with titin and myomesin. This shape allows the M-band to withstand large conformational changes du ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Titin
Titin (contraction for Titan protein) (also called connectin) is a protein that in humans is encoded by the ''TTN'' gene. Titin is a giant protein, greater than 1 µm in length, that functions as a molecular spring that is responsible for the passive elasticity of muscle. It comprises 244 individually folded protein domains connected by unstructured peptide sequences. These domains unfold when the protein is stretched and refold when the tension is removed. Titin is important in the contraction of striated muscle tissues. It connects the Z line to the M line in the sarcomere. The protein contributes to force transmission at the Z line and resting tension in the I band region. It limits the range of motion of the sarcomere in tension, thus contributing to the passive stiffness of muscle. Variations in the sequence of titin between different types of striated muscle (cardiac or skeletal) have been correlated with differences in the mechanical properties of these muscles. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cardiac Sarcomere Structure
The heart is a muscular organ in most animals. This organ pumps blood through the blood vessels of the circulatory system. The pumped blood carries oxygen and nutrients to the body, while carrying metabolic waste such as carbon dioxide to the lungs. In humans, the heart is approximately the size of a closed fist and is located between the lungs, in the middle compartment of the chest. In humans, other mammals, and birds, the heart is divided into four chambers: upper left and right atria and lower left and right ventricles. Commonly the right atrium and ventricle are referred together as the right heart and their left counterparts as the left heart. Fish, in contrast, have two chambers, an atrium and a ventricle, while most reptiles have three chambers. In a healthy heart blood flows one way through the heart due to heart valves, which prevent backflow. The heart is enclosed in a protective sac, the pericardium, which also contains a small amount of fluid. The wal ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
