Striated muscles contain repeating sarcomeres of overlapping arrays of long, thin actin and thicker myosin filaments. Myosin filaments contains the myosin heads, which are enzymes that can bind to actin, split and make use of the energy from ATP. When muscle contraction starts, myosin heads bind to actin, change their configuration on actin, liberating the products of ATP hydrolysis and causing slide of the actin and myosin filaments. The action of the proteins troponin and tropomyosin on the actin filaments regulates vertebrae striated muscle contraction. The release of calcium ions from the sarcoplasmic reticulum is triggered by the nervous stimulation which causes depolarization of muscle membrane. Calcium ions bind to troponin and thus cause or allow the tropomyosin strands on the actin filament to move so that the part of the actin surface where myosin heads need to bind is uncovered. Contraction then occurs and only stops when the sarcoplasmic reticulum pumps calcium out of the muscle interior.
So basically, what triggers the uncovering of the myosin binding site on actin is the calcium ions binding to troponin and changing configuration.
Because it is easily accessible and has a mild immune response, the retina makes a good target for gene therapy.
- In a mouse model, the inner retina was highly effectively transduced by an intravitreally injected adeno-associated virus (AAV) vector.
- The vitreous and internal limiting membrane (ILM) operated as obstacles to transduction in large animals, reducing the efficacy of retinal transduction.
- Before administering AAV vectors, we performed vitrectomy (VIT) and ILM peeling on cynomolgus monkeys to get around these obstacles.
- The findings suggest that surgical ILM peeling prior to AAV vector delivery would be beneficial for retinal disease treatment and safe for effective transduction of the nonhuman primate retina.
Learn more about the adeno-associated virus (AAV) with the help of the given link:
brainly.com/question/28205495
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Adp I think. don't hold me to it