Muscle proteins are often classified into three groups referred to as myofibrillar proteins (MP), sarcoplasmic proteins, and connective tissue or stromal proteins. The MP fraction is the structural proteins that make up the myofibrils, constitute about 55 to 60% of the total muscle protein, or 10% of fresh skeletal muscle; composed mainly of myosin, C-protein, M-protein, actin, tropomyosin, troponin complex and α-actinin among others. Sarcoplasmic and stromal proteins constitute approximately 30‒35% and 3‒10% of the total muscle proteins (Nip and others 2008).
MP is generally extracted in intermediate or high-ionic-strength buffer, which is required to disrupted the myofibrils enough to release myosin, therefore, known as “salt-soluble proteins”.
The polyacrylamide gel showed bands of proteins based upon their weight. The further away from the gel the protein band occurred, the heavier the protein was. The Precision Plus Protein Kaleidoscope prestained standard and actin and myosin standard ladders were very neatly spaced out, and one could easily detect the presence of different proteins. However, the fish proteins were not so easily discerned, especially since, in most cases, the lighter proteins had less color.
Muscle fibres, as shown in Diagram 1, consist of myofibrils, which contain the proteins, actin and myosin, in specific arrangements . The diagram illustrates how a muscle is made up of many fascicles, which in turn are made up of many endomysiums, and within them, many muscle fibres. Each muscle fibre is made up of many myofibrils that consist of sarcomeres bound end on end . Actin is a thin filament, about 7nm in diameter, and myosin is a thick filament, about 15nm in diameter , both of which reside in the sarcomere. They are held together by transverse bands known as Z lines . Diagram 2 shows actin and myosin filaments within a sarcomere, and the Z lines that connect them.
Myofibrils are made up of long proteins that include myosin, titin, and actin while other proteins bind them together. These proteins are arranged into thin and thick filaments that are repetitive along the myofibril in sectors known as sarcomeres. The sliding of actin and myosin filaments along each other is when the muscle is contracting. Dark A-bands and light I-bands reappear along myofibrils. The alignment of myofibrils causes an appearance of the cell to look banded or striated. A myofibril is made up of lots of sarcomeres. As the sarcomeres contract individually the muscle cells and myofibrils shorten in length. The longitudinal section of skeletal muscle exhibits a unique pattern of alternating light and dark bands. The dark staining, A-bands possess a pale region in the middle called the H-zone. In the middle of the H-zone the M-line is found, that displays filamentous structures that can join the thick filaments. The light-staining bands also known as I-bands are divided by thin Z-line. These striated patterns appear because of the presence of myofibrils in the sarcoplasm (IUPUI, 2016).
When a cell becomes damaged and undergoes apoptosis the muscle cells may not be able to regenerate at a proper rate to avoid a deficiency in the amount of the nuclei needed to maintain proper muscle mass. Support for this need and the suggestion that nuclei number may be size limiting and therefore a causation for atrophy was found in the study by the observation of damaged myonuclei were found in stage 3 mice but absent in stage 1, myonuclei reduction in the two muscle samples, nuclear domain size in regards to surface area was either maintained or increased, and the reappearance of a correlation between nuclei number and fiber size in stage 3 muscles. Particularly EDL IIb fibers may be most susceptible to sarcoma due to a generally lower nuclei number and that distribution of these fibers is impaired in the elderly which would not reduce capacity for synthesis but could increase transport distances causing decreased functionality. The nuclear shape also changed which has an unknown impact on functionality and may have been the cause of the nuclear fragmentation possibly leading to
1. Discuss the relationship between distribution of muscle fiber type and performance. How might exercise training modify or change a person’s fiber-type distribution?
I think anatomical and metabolic makes where fast, slow and intermediate muscle fibers. The type one makes it where it is red in the color in the myoglobin. This fiber arc needs to be rich in this mitochondria and oxidative enzymes because it is where a poor in phosphorylases this is because it makes a well-developed aerobic metabolism and this where the slow fiber makes it to where its highly resistant to where you can become fatigue. Features that can summarized the slow muscle are the large enough amounts of myoglobin to so many mitochondria to having to many blood capillaries and having to generate atp by having the aerobic system to hence term to oxidative fibers to where splitting ATP to the slow rate. To having the slowest contraction velocity to
The contractile unit of a muscle cell is the sarcomere. Sarcomeres are mostly comprised of actin and myosin which pull and slide upon each other. These contractile units are linked end to end, like a chain, throughout the length of any given muscle. Certain proteins link the ends of these chains to the cell membrane. When a normally healthy individual exercises, some of these fibers, both in the sarcomere and at the connections to the cell wall, will be broken down due to damage (Leyva, 2013). Associated with this process includes the rebuilding of these fibers, in which the body builds back what was damaged stronger than before the damage occurred (Leyva, 2013). One of these end proteins is dystrophin. The purpose of this paper is to explore the implications of insufficient production of dystrophin, as in DMD.
The ubiquitin-proteasome system is needed to rid muscles of sarcomeric proteins when there are muscle changes. “A decrease in muscle mass is associated with: (1) An increased conjugation of ubiquitin to muscle proteins; (2) an increased proteasomal ATP-dependent activity; (3) increased protein breakdown that can be efficiently blocked by proteasome inhibitors; and (4) upregulation of transcripts encoding ubiquitin, some ubiquitin-conjugating enzymes (E2), a few ubiquitin- protein ligases (E3) and several proteasome subunits” (Lecker et al., 2006, p. 25). Muscle atrophy is best defined as an active process that is controlled by a specific set of signaling pathways
Muscle activity. Muscle activity was recorded using a Bagnoli EMG system (Delsys, Boston, MA, USA) from 7 upper extremities muscles: flexor carpi ulnaris (FCU), extensor carpi ulnaris (ECU), extensor carpi radialis brevis (ECRB), triceps, anterior deltoid, middle deltoid, and upper trapezius using single differential electrodes. The muscle activity data were normalized to muscle–specific maximum voluntary exertions. The data acquired using a Motion Monitor data acquisition system (Innsport, Chicago, USA) which were sampled at 1200 Hz, and filtered using a Butterworth filter and notch filters (at 60 Hz increments).
This is the muscle which covers the bones. Human body contains over 400 skeletal muscles. 40-50% of total body weight. It is soft muscle. Most are attached by tendons to bones. It is attached to skeleton by strong and directly connected to rough patches of bones. Muscles are striated and have visible banding. It works voluntary.
Skeletal muscles contain cells called muscle fibres with the help of nerves, carries messages to and fro the brain. This therefore enables the muscles to contract when messages from the brain travel along the nerves to the fibre, either telling them to shorten, or tense. The fibres are made up of contractile protein myofibrils in which, each myofibril is made of overlapping protein threads called myofilaments. Every single muscle fibre is a long cylindrical cell encased by a sarcolemma, the cell membrane surrounding a muscle fibre. It is specifically designed for contraction. Muscles work across joints in which one end is attached to the fixed bone and the other, to the moveable bone. Movement would therefore occur when the muscle contracts,
Muscles are contractile tissues that bring movements of different body parts. They can be considered as motors of the human body since they provide all the force necessary to perform different types of movements.
Our body contains many different parts and different functions. Each body function is essential and when all of them are put together, it’s a perfect combination. The function of the body is fascinating and quite amazing to see how our body can cooperate with one another. Our body is like a team that works together. One of these organ system is the muscular system.
Bodyweight lifting routines - The regimen of stretching and contracting muscle underneath weighted loads, damages the tissue from the muscle less than the anxiety of the load. Myosin and Actin are filamentous proteins located in the cells and fibers of one's muscle. These proteins go through micro tears, resulting within
As a result, the interactions between protein molecules exceed protein-water interactions, and the solubility decreases. Moreover, the differences in the amino acid sequence makes proteins differ in their salting in and salting out behavior. This is the basis for the fractional precipitation of proteins by means of salt. Most commonly used salt is ammonium sulfate because it is available in highly purified form and because of its high solubility. (Boyer, 2000)