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Organization of Muscle Tissue • An aponeurosis is essentially a thick fascia that connects two muscle bellies. This epicranial aponeurosis connects the muscle bellies of the occipitalis and the frontalis to form “one” muscle: The occipitofrontalis Epicranial aponeurosis Frontal belly of the occipitofront alis m.

Organization of Muscle Tissue An aponeurosis is essentially a thick fascia that connects two muscle bellies. This epicranial aponeurosis connects the muscle

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Chapter 9 Joints

Organization of Muscle TissueAn aponeurosis is essentially a thick fascia that connects two muscle bellies. This epicranial aponeurosis connects the muscle bellies of the occipitalis and the frontalis to form one muscle: The occipitofrontalis

Epicranial aponeurosisFrontal belly of the occipitofrontalis m.1An aponeurosis is essentially a thick fascia that connects two muscle bellies. This epicranial aponeurosis connects the muscle bellies of the occipitalis and the frontalis to form one muscle: The occipitofrontalisVeins, arteries, and nerves are located in the deep fascia between muscles of the thigh.Organization of Muscle Tissue

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Beneath the connective tissue endomysium is found the plasma membrane (called the sarcolemma) of an individual skeletal muscle fiberThe cytoplasm (sarcoplasm) of skeletal muscle fibers is chocked full of contractile proteins arranged in myofibrilsThe Skeletal Muscle Fiber3

You should learn the names of the internal structures of the muscle fiberSarcolemmaSarcoplasmMyofibrilT-tubulesTriad (with terminal cisternsSarcoplasmic reticulumSarcomereThe Skeletal Muscle Fiber4The Skeletal Muscle FiberIncreasing the level of magnification, the myofibrils are seen to be composed of filamentsThick filamentsThing filaments

Sarcomeres are multi-protein complexes composed of three different filament systems. The thick filament system is composed of myosin protein which is connected from the M-line to the Z-disc by titin. It also contains myosin-binding protein C which binds at one end to the thick filament and the other to actin.The thin filaments are assembled by actin monomers bound to nebulin, which also involves tropomyosin (a dimer which coils itself around the F-actin core of the thin filament) and troponin.Nebulin and titin give stability and structure to the sarcomere.5

A scanning electron micrograph of a sarcomereThe basic functional unit of skeletal muscle fibers is the sarcomere: An arrangement of thick and thin filaments sandwiched between two Z discsThe Skeletal Muscle Fiber Z-line (from the German "Zwischenscheibe). Each myofibril is made up of thin filament proteins and thick filament proteins, arranged (configured) in sarcomeres.6

The Z line is really a Z disc when considered in 3 dimensions. A sarcomere extends from Z disc to Z disc.Muscle contraction occurs in the sarcomeresThe Skeletal Muscle FiberEach myofibril is made up of thin filament proteins, and thick filament proteins, arranged (configured) in sarcomeres7Myofibrils are built from three groups of proteinsContractile proteins generate force during contractionRegulatory proteins help switch the contraction process on and offStructural proteins keep the thick and thin filaments in proper alignment and link the myofibrils to the sarcolemma and extracellular matrixMuscle Proteins8The thin filaments are comprised mostly of the structural protein actin, and the thick filaments are comprised mostly of the structural protein myosinHowever, in both types of filaments, there are also other structural and regulatory proteins

Muscle Proteins9In the thin filaments actin proteins are strung together like a bead of pearls

In the thick filaments myosin proteins look like golf clubs bound together

Muscle Proteins10

In this first graphic, the myosin binding sites on the actin proteins are readily visible.

The regulatory proteins troponin and tropomyosin have been added to the bottom graphic: The myosin binding sites have been covered

Muscle Proteins11In this graphic the troponin-tropomyosin complex has slid down into the gutters of the actin molecule unblocking the myosin binding site

The troponin-tropomyosin complex can slide back and forth depending on the presence of Ca2+

Myosin binding site exposedMuscle Proteins12Ca2+ binds to troponin which changes the shape of the troponin-tropomyosin complex and uncovers the myosin binding sites on actin

Muscle Proteins13Besides contractile and regulatory proteins, muscle contains about a dozen structural proteins which contribute to the alignment, stability, elasticity, and extensibility of myofibrilsTitan is the third most plentiful protein in muscle, after actin and myosin - it extends from the Z disc and accounts for much of the elasticity of myofibrilsDystrophin is discussed later as it relates to the disease of muscular dystrophyMuscle ProteinsTitin is the largest known protein, consisting of 34,350 amino acids. Titin, also known as connectin is a protein that is important in the contraction of striated muscle tissues. Dystrophin, not Titin, is the protein absent in muscular dystrophy.14With exposure of the myosin binding sites on actin (the thin filaments)in the presence of Ca2+ and ATPthe thick and thin filaments slide on one another and the sarcomere is shortenedThe Sliding-Filament Mechanism

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