Tumor associated calcium signal transducer 2 (TACSTD2; TROP-2) is a type I cell surface glycoprotein that is highly expressed on human carcinomas. It was originally identified as an antigen present on human gastrointestinal tumors and is the second of two members of this family. Human and mouse TROP-2 share 87% amino acid (aa) similarity. TROP-2 is capable of transducing an intracellular calcium signal and may play a role in tumor growth. It also has adhesive functions.
TROP-2, also referred to as tumor associated calcium signal transducer 2 (TACSTD2), GA733-1 or M1S1, is a cell surface glycoprotein highly expressed in a wide variety of epithelial cancers. In contrast, there is little or no expression of Trop-2 in adult somatic tissue. Because it is a cell surface protein that is selectively expressed in tumor cells, Trop-2 is a potential therapeutic target. The cytoplasmic tail of Trop-2 possesses potential serine and tyrosine phosphorylation sites and a phosphatidyl-inositol binding consensus sequence. Trop-2 transduces an intracellular calcium signal, are consistent with the hypothesis that it acts as a cell surface receptor and support a search for a physiological ligand. TROP2 encoding by an intronless gene was originally defined by the monoclonal antibody GA733, and is a member of a family of at least two type I membrane proteins. The other known member is GA733-2, also called EpCAM and TROP1. It has been suggested by studies that the GA733-1 gene was formed by the retroposition of the GA733-2 gene via an mRNA intermediate.
Tropomyosin Alpha-3 Chain (TPM3) is a member of the Tropomyosin family. TPM3 exists as a heterodimer consisting of an alpha and a beta chain. TPM3 plays a central role in association with the Troponin complex and in the calcium dependent regulation of vertebrate striated muscle contraction. Defects in TPM3 are the cause of thyroid papillary carcinoma. Mutations in the TPM3 gene cause autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are linked with cancer.
Troponin I, also known as TNNC1, is part of the troponin complex. This complex contains 3 subunits: troponin I (TnI), troponin T (TnT) and troponin C (TnC). Troponin I is the inhibitory subunit, blocking actin-myosin interactions and thereby mediating striated muscle relaxation. It binds to actin in thin myofilaments to hold the actin-tropomyosin complex in place. Because of it myosin cannot bind actin in relaxed muscle. When calcium binds to the Troponin C it causes conformational changes which lead to dislocation of troponin I and finally tropomyosin leaves the binding site for myosin on actin leading to contraction of muscle.
Troponin I, also known as TNI, is a 24 kDa component of a protein complex on striated muscle thin filaments.Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. Troponin I inhibits the calcium-dependent muscle contraction mediated by Troponins C and T. The expression of cardiac Troponin I (TNNI3) is restricted to cardiac muscle, while TNNI1 and TNNI2(encoded by distinct genes) are expressed in skeletal muscle. Mutations of cardiac Troponin I are associated with heriditary cardiomyopathy. Human cardiac Troponin I shares 93% amino acid sequence identity with mouse and rat cardiac Troponin I.
Tyrosinase-related protein 1; also known as TYRP1 or TRP1; is a melanosomal enzyme that belongs to the tyrosinase family and plays an important role in the melanin biosynthetic pathway. Mutations in this enzyme are the cause of rufous oculocutaneous albinism and oculocutaneous albinism type III. TYRP1 / TRP1 is involved in the oxidation of 5;6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5;6-quinone-2-carboxylic acid. This enzyme may regulate or influence the type of melanin synthesized. The expression of Tyrosinase-related protein 1 (TYRP1) is regulated by the microphthalmia-associated transcription factor (MITF). There is mounting evidence demonstrating that in addition to its role in eumelanin synthesis; TYRP1 is involved in maintaining stability of tyrosinase proliferation and melanocyte cell death.
Trypsin-2, also known as Trypsin II, Anionic trypsinogen, Serine protease 2, PRSS2 and TRY2, is a secreted protein that belongs to the trypsin serine protease family including Trypsin, PRSS1, PRSS2 and PRSS3. It consists of a signal peptide (residues 1-15), a pro region (residues 16-23), and a proteolytically active mature chain (residues 24-247). PRSS2 contains one peptidase S1 domain. It is secreted into the duodenum, hydrolysing peptides into their smaller building blocks, which is necessary for the uptake of protein in the food. It is secreted by the pancreas in the form of inactive zymogen, trypsinogen and cleaved to its active form in the small intestine when the pancreas is stimulated by cholecystokinin throμgh the common activation mechanism.
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