Skeletal muscle

The myonuclei are quite uniformly arranged along the fiber with each nucleus having its own myonuclear domain where it is responsible for supporting the volume of cytoplasm in that particular section of the myofiber.

However, fast twitch fibers also demonstrate a higher capability for electrochemical transmission of action potentials and a rapid level of calcium release and uptake by the sarcoplasmic reticulum.

[55] In addition to having a genetic basis, the composition of muscle fiber types is flexible and can vary with a number of different environmental factors.

[57] Skeletal muscle exhibits a distinctive banding pattern when viewed under the microscope due to the arrangement of two contractile proteins myosin, and actin – that are two of the myofilaments in the myofibrils.

During embryonic development in the process of somitogenesis the paraxial mesoderm is divided along the embryo's length to form somites, corresponding to the segmentation of the body most obviously seen in the vertebral column.

Myoblast migration is preceded by the formation of connective tissue frameworks, usually formed from the somatic lateral plate mesoderm.

[3] Following contraction, skeletal muscle functions as an endocrine organ by secreting myokines – a wide range of cytokines and other peptides that act as signalling molecules.

Calcium-bound troponin undergoes a conformational change that leads to the movement of tropomyosin, subsequently exposing the myosin-binding sites on actin.

As the ryanodine receptors open, Ca2+ is released from the sarcoplasmic reticulum into the local junctional space and diffuses into the bulk cytoplasm to cause a calcium spark.

The Ca2+ released into the cytosol binds to Troponin C by the actin filaments, to allow crossbridge cycling, producing force and, in some situations, motion.

In this case, the signal from the afferent fiber does not reach the brain, but produces the reflexive movement by direct connections with the efferent nerves in the spine.

Commands are routed through the basal ganglia and are modified by input from the cerebellum before being relayed through the pyramidal tract to the spinal cord and from there to the motor end plate at the muscles.

The cerebellum and red nucleus in particular continuously sample position against movement and make minor corrections to assure smooth motion.

Cardiac muscle on the other hand, can readily consume any of the three macronutrients (protein, glucose and fat) aerobically without a 'warm up' period and always extracts the maximum ATP yield from any molecule involved.

The heart, liver and red blood cells will also consume lactic acid produced and excreted by skeletal muscles during exercise.

The mechanical energy output of a cyclic contraction can depend upon many factors, including activation timing, muscle strain trajectory, and rates of force rise & decay.

[71] Some invertebrate muscles, such as in crab claws, have much longer sarcomeres than vertebrates, resulting in many more sites for actin and myosin to bind and thus much greater force per square centimeter at the cost of much slower speed.

The maximum holding time for a contracted muscle depends on its supply of energy and is stated by Rohmert's law to exponentially decay from the beginning of exertion.

Part of the training process is learning to relax the antagonist muscles to increase the force input of the chest and anterior shoulder.

A peroxisome proliferator-activated receptor δ (PPARδ)-mediated transcriptional pathway is involved in the regulation of the skeletal muscle fiber phenotype.

Thus—through functional genomics—calcineurin, calmodulin-dependent kinase, PGC-1α, and activated PPARδ form the basis of a signaling network that controls skeletal muscle fiber-type transformation and metabolic profiles that protect against insulin resistance and obesity.

These include a switch from fat-based to carbohydrate-based fuels, a redistribution of blood flow from nonworking to exercising muscles, and the removal of several of the by-products of anaerobic metabolism, such as carbon dioxide and lactic acid.

Moreover, the hypoxia-inducible factor 1-α (HIF1A) has been identified as a master regulator for the expression of genes involved in essential hypoxic responses that maintain ATP levels in cells.

Physical exercise is often recommended as a means of improving motor skills, fitness, muscle and bone strength, and joint function.

Aerobic exercise (e.g. marathons) involves activities of low intensity but long duration, during which the muscles used are below their maximal contraction strength.

[80] During anaerobic exercise, type II fibers consume little oxygen, protein and fat, produce large amounts of lactic acid and are fatigable.

[5][84] Some inflammatory myopathies include polymyositis and inclusion body myositis Neuromuscular diseases affect the muscles and their nervous control.

Diagnostic procedures that may reveal muscular disorders include testing creatine kinase levels in the blood and electromyography (measuring electrical activity in muscles).

[103] Of these individuals, 1,605 participants (19.4%) were considered to have a low skeletal muscle mass at baseline, with less than 7.30 kg/m2 for males, and less than 5.42 kg/m2 for females (levels defined as sarcopenia in Canada).

[102] The main pathways found to be affected by secreted exercise-regulated proteins were related to cardiac, cognitive, kidney and platelet functions.

Muscle types by fiber arrangement
ATPase staining of a muscle cross section. Type II fibers are dark, due to the alkaline pH of the preparation. In this example, the size of the type II fibers is considerably less than the type I fibers due to denervation atrophy.
Structure of muscle fibre showing a sarcomere under electron microscope with schematic explanation
Diagram of sarcoplasmic reticulum with terminal cisternae and T-tubules
Human embryo showing somites labelled as primitive segments
Classes of levers present in the human skeletal muscular system
When a sarcomere contracts, the Z lines move closer together, and the I band becomes smaller. The A band stays the same width. At full contraction, the thin and thick filaments overlap.
Contraction in more detail
(a) Some ATP is stored in a resting muscle. As contraction starts, it is used up in seconds. More ATP is generated from creatine phosphate for about 15 seconds. (b) Each glucose molecule produces two ATP and two molecules of pyruvic acid, which can be used in aerobic respiration or converted to lactic acid . If oxygen is not available, pyruvic acid is converted to lactic acid, which may contribute to muscle fatigue . This occurs during strenuous exercise when high amounts of energy are needed but oxygen cannot be sufficiently delivered to muscle. (c) Aerobic respiration is the breakdown of glucose in the presence of oxygen (O2) to produce carbon dioxide, water, and ATP. Approximately 95 percent of the ATP required for resting or moderately active muscles is provided by aerobic respiration, which takes place in mitochondria.
Exercise-induced signaling pathways in skeletal muscle that determine specialized characteristics of slow- and fast-twitch muscle fibers
Jogging is one form of aerobic exercise.
In muscular dystrophy , the affected tissues become disorganized and the concentration of dystrophin (green) is greatly reduced.
Prisoner of war exhibiting muscle loss as a result of malnutrition
Skeletal muscle cell types include: very large multinuclear muscle fiber cells ; small endothelial cells that line the inside of capillary blood vessels; small fibro-adipogenic progenitor cells (FAPs) which are muscle-fiber-adjacent multipotent mesenchymal stem cells that under different conditions can differentiate into adipocytes, fibroblasts or osteocytes. Also shown are pericytes situated on the outer surface of blood capillaries where they interact with the underlying endothelial cells. In addition, satellite cells are shown that can fuse with muscle fibers and contribute new myonuclei to muscle fibers, grow into new myocytes , or support focal membrane damage repair. [ 98 ]
Regulation of transcription in mammals. An active enhancer regulatory region is enabled to interact with the promoter region of its target gene by formation of a chromosome loop. This can allow initiation of messenger RNA (mRNA) synthesis by RNA polymerase II (RNAP II) bound to the promoter at the transcription start site of the gene. The loop is stabilized by one architectural protein anchored to the enhancer and one anchored to the promoter, and these proteins are joined together to form a dimer (red zigzags). Specific regulatory transcription factors bind to DNA sequence motifs on the enhancer. General transcription factors bind to the promoter. When a transcription factor is activated by a signal (here indicated as phosphorylation shown by a small red star on a transcription factor on the enhancer), the enhancer is activated and can now activate its target promoter. The active enhancer is transcribed on each strand of DNA in opposite directions by bound RNAP IIs. Mediator (a complex consisting of about 26 proteins in an interacting structure) communicates regulatory signals from the enhancer DNA-bound transcription factors to the promoter.
A nucleosome with histone tails set for transcriptional activation ....DNA in the nucleus generally consists of segments of 146 base pairs of DNA wrapped around nucleosomes connected to adjacent nucleosomes by linker DNA . Nucleosomes consist of four pairs of histone proteins in a tightly assembled core region plus up to 30% of each histone remaining in a loosely organized polypeptide tail (only one tail of each pair is shown). The pairs of histones, H2A, H2B, H3 and H4, each have lysines (K) in their tails, some of which are subject to post-translational modifications consisting, usually, of acetylations [Ac] and methylations {me}. The lysines (K) are designated with a number showing their position as, for instance, (K4), indicating lysine as the 4th amino acid from the amino (N) end of the tail in the histone protein. The particular acetylations [Ac] and methylations {Me} shown are those that occur on nucleosomes close to, or at, some DNA regions undergoing transcriptional activation of the DNA wrapped around the nucleosome.