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Troponin T (blue) anchors the complex on tropomyosin. Troponin is found in both skeletal muscle and cardiac muscle, but the specific versions of troponin differ between types of muscle. The main difference is that the TnC subunit of troponin in skeletal muscle has four calcium ion-binding sites, whereas in cardiac muscle there are only three.
Troponin I, fast skeletal muscle is a protein that in humans is encoded by the TNNI2 gene. [5] [6]The TNNI2 gene is located at 11p15.5 in the human chromosomal genome, encoding the fast twitch skeletal muscle troponin I (fsTnI). fsTnI is a 21.3 kDa protein consisting of 182 amino acids including the first methionine with an isoelectric point (pI) of 8.74.
Cardiac muscle troponin T (cTnT) is a protein that in humans is encoded by the TNNT2 gene. [ 5 ] [ 6 ] Cardiac TnT is the tropomyosin -binding subunit of the troponin complex, which is located on the thin filament of striated muscles and regulates muscle contraction in response to alterations in intracellular calcium ion concentration.
Tropomyosin dimers are composed of varying combinations of tropomyosin isoforms; human striated muscles express protein from the TPM1 (α-tropoomyosin), TPM2 (β-tropomyosin) and TPM3 (γ-tropomyosin) genes, with α-tropomyosin being the predominant isoform in striated muscle.
[2] Fetal Troponin T and Troponin I isoforms. Structure of Fetal Hemoglobin. Fetal Hemoglobin is a member of erythrocytes called F-cells. [3] It is a tetramer protein with 2 alpha and 2 gamma subunits. This is different from adult hemoglobin because it has 2 alpha and 2 beta subunits. Fetal hemoglobin is coded by a gene on chromosome 11.
The study found that Tropomyosin 3, an isoform that is not normally expressed in neuronal cells, was broadly distributed throughout the neuron, while exogenous expression of the neuronal isoform Tropomyosin 5NM1/2 was found to sort to the growth cone of neurons as does the endogenous Tropomyosin 5NM1/2.
Test Sensitivity and specificity Approximate peak Description Troponin test: The most sensitive and specific test for myocardial damage. Because it has increased specificity compared with CK-MB, troponin is composed of 3 proteins- Troponin C, Cardic troponin I, and Cardiac troponin T. Troponin I especially has a high affinity for myocardial injury.
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]