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The myosin-binding protein C, cardiac-type is a protein that in humans is encoded by the MYBPC3 gene. [5] This isoform is expressed exclusively in heart muscle during human and mouse development, [6] and is distinct from those expressed in slow skeletal muscle and fast skeletal muscle ().
In the thick myofilaments of the heart tissue, the predominant gene mutations occur in “myosin-binding protein C (MYBPC3)” and “myosin heavy chain (MYH7).” Myocardial infarction, atrial fibrillation, ventricular fibrillation, embolic events, and/or congestive heart failure are all possible outcomes of this condition.
Its subsequent release is prolonged with degradation of actin and myosin filaments. Isoforms of the protein, T and I, are specific to myocardium. Differential diagnosis of troponin elevation includes acute infarction, severe pulmonary embolism causing acute right heart overload, heart failure, myocarditis.
This gene encodes a member of the myosin-binding protein C family. This family includes the fast-, slow- and cardiac-type isoforms, each of which is a myosin-associated protein found in the cross-bridge-bearing zone (C region) of A bands in striated muscle. The protein encoded by this locus is referred to as the fast-type isoform.
When calcium becomes bound to specific sites in the N-domain of TnC, a series of protein structural changes occurs, [citation needed] such that tropomyosin is rolled away from myosin-binding sites on actin, allowing myosin to attach to the thin filament and produce force and shorten the sarcomere. [citation needed]
The two main myofilaments in cardiac (and skeletal) muscle are actin and myosin. Ca 2+ binds to a protein called troponin, which is bound to the actin filament. This binding causes a shape change in the troponin which exposes areas on the actin, to which the head of the myosin filament binds. The binding of the myosin head to actin is known as ...
When calcium binds to the troponin C, it causes conformational changes which lead to dislocation of troponin I. Afterwards, tropomyosin leaves the binding site for myosin on actin leading to contraction of muscle. The letter I is given due to its inhibitory character. It is a useful marker in the laboratory diagnosis of heart attack. [2]
These calcium ions bind to a protein called troponin, which initiates the process of muscle contraction. [50] Calcium sensitizers function by binding to cardiac troponin C, thereby enhancing the sensitivity of heart muscle cells to naturally occurring calcium ions. [51]