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Thyroid Hormone Responsive (THRSP) is a member of the SPOT14 family. THRSP is similar to the gene product of S14, a rat gene whose expression is limited to liver and adipose tissue and is controlled by nutritional and hormonal factors. THRSP is expressed in liver and adipocytes, specifically in lipomatous modules. In addition It is expressed in lipogenic breast cancers, which suggests a role in controlling tumor lipid metabolism.

Transferrin receptor protein 1 (TFRC) is required for iron delivery from transferring to cells. The TFRC protein is a transmembrane glycoprotein comprised of 2 disulfide-linked monomers joined by 2 disulfide bonds. Each monomer will bind one holo-transferrin molecule producing an iron-Tf-TfR complex which enters the cell by endocytosis.

Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

TRXR is a ubiquitous enzyme which participates in various cellular processes such as cell growth, p53 activity, and protection against oxidation stress. The mammalian Thioredoxin reductase cleaves thioredoxins as well as non-disulfide substrates such as selenite, lipoic acids, lipid hydroperoxides, and hydrogen peroxidec.

Troponin Complex is a heteromeric protein playing an important role in the regulation of skeletal and cardiac muscle contraction. It consists of three subunits, Troponin I, Troponin T and TroponinC. Each subunit is responsible for part of Troponin Complex function. E.g. Troponin I inhibits ATP-ase activity of acto-myosin.Troponin T and Troponin Iare presented in cardiac muscles in different forms than in skeletal muscles. Purified subunits of rcTnI, rcTnC and rcTnT are recomplexed in vitro under appropriate conditions.

Troponin-C2 (Troponin C, skeletal muscle) is the central regulatory antigen of striated muscle contraction, and modulates the Ca2+-activation characteristics of muscle fibers. Troponin-C2 has three subunits, Troponin I(Tn-1), Troponin T(Tn-T) and Troponin C(Tn-C). Tn-I subunit inhibits actomyosin ATPase and Tn-T subunit binds tropomyosin and Tn-C, while Tn-C subunit binds calcium and overcomes the inhibitory action of the troponin complex on actin filaments. Mutations in all components of this complex have been linked with skeletal muscle disease.

Troponin is a fundamental regulatory protein of striated muscle contraction, and together with tropomyosin, is positioned on the actin filament. Troponin has 3 subunits: TnI- the inhibitor of actomyosin ATPase; TnT- contains the binding site for tropomyosin; and TnC- the protein encoded by the TNNC1 gene. The binding of calcium to TnC stops the inhibitory action of TnI, consequently allowing the interaction of actin with myosin, the hydrolysis of ATP, and the generation of tension. Mutations in the TNNC1 gene are linked to cardiomyopathy dilated type 1Z.

Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney that regulates the production of platelets by the bone marrow. It stimulates the production and differentiation of megakaryocytes, the bone marrow cells that fragment into large numbers of platelets.

Troponin is a fundamental regulatory protein of striated muscle contraction, and together with tropomyosin, is positioned on the actin filament. Troponin has 3 subunits: TnI- the inhibitor of actomyosin ATPase; TnT- contains the binding site for tropomyosin; and TnC- the protein encoded by the TNNC1 gene. The binding of calcium to TnC stops the inhibitory action of TnI, consequently allowing the interaction of actin with myosin, the hydrolysis of ATP, and the generation of tension. Mutations in the TNNC1 gene are linked to cardiomyopathy dilated type 1Z.

Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

Prothrombin Complex Concentrate (PCC) is a combination of several blood clotting factors II, VII, IX and X. PCC is used in the treatment of the congenital bleeding disorders associated with Factors II, VII, IX, and X deficiencies. PCC reverses the effect of warfarin (a coumarin anti-coagulant) and is used in cases of significant bleeding in patients with a coagulopathy, for example, gastrointestinal haemorrhage or intracranial haemorrhage. The PCC is also extensively used in treating acquired coagulation abnormalities secondary to vitamin K deficiency, warfarin ingestion, and various types of liver disease.
Hepatitis, anaphylaxis and thrombosis have been reported as complications of prothrombin complex concentrates administration.

The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.

Serpin Peptidase Inhibitor, Clade C Member 1 (SERPINC1), which is a part of the serpin superfamily, is a plasma protease inhibitor. SERPINC1 inhibits thrombin and other activated serine proteases of the coagulation system, and regulates the blood coagulation cascade. SERPINC1 also inhibits Thrombin and Factors IXa, Xa and XIa. Deficiencies in SERPINC1 can cause ATIII deficiency, an autosomal dominant disease which might lead to a hereditary thrombophilia.

E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.

Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.

Platelet Factor 4 Variant 1 (PF4V1) is a member of the intercrine alpha (chemokine CxC) family. PF4V1 is an inhibitor of angiogenesis and inhibitor of endothelial cell chemotaxis (in vitro).

Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney which regulates the production of platelets by the bone marrow. TPO stimulates the production as well as differentiation of megakaryocytes, the bone marrow cells which fragment into large numbers of platelets.

TREM2 is a membrane protein that forms a receptor signaling complex with TYROBP. TREM2 may be involved in chronic inflammation by triggering the production of constitutive inflammatory cytokines. Defects in the TREM2 gene are a source of polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL).

Thrombopoietin or TPO or MGDF, is a protein (glycoprotein hormone) that can be found in the liver and kidney tissues. TPO regulates the creation of platelets. The protein enhances the production & differentiation of cells such as megakaryocytes that are part of the bone marrow cells that secretes a wide number of platelets. The cellular development process that ends up in the production of platelet calls (Megakaryocytopoiesis). Humoral growth factor is needed for the megakaryocyte proliferation & maturation of megakaryocyte, not apart from thrombopoiesis.

Uromodulin (Tamm–Horsfall protein) is produced mainly by cells in the kidney’s thick ascending limb and is the most abundant protein in normal urine.
Uromodulin takes part in salt and water regulation, helps prevent urinary tract infections and kidney stones, and influences inflammation and immune activity in the kidney.
Reduced Uromodulin levels is associated with chronic kidney disease.
UMOD mutations causes unproper protein folding and thus transported incorrectly, resulting in its accumulation inside kidney tubular cells that damages the tubules and cause kidney disease (ADTKD-UMOD), associated with high uric acid, gout, and progressive kidney failure.

Avidin is a tetrameric protein of 4 identical subunits (homotetramer) which can bind to biotin with a high degree of affinity and specificity. The estimated molecular weight of Avidin in its tetrameric form is between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of 4-5 mannose and 3 N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.

Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors.

TREM1 is a transmembrane receptor protein that is involved in monocytic activation and in the inflammatory response. TREM1 is expressed on the surface of neutrophils, mature monocytes and macrophages. TREM1 stimulates neutrophil and monocyte-mediated inflammatory responses. TREM1 also triggers the release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Furthermore, TREM1 is an amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a fundamental mediator of septic shock. The expression of the soluble form of TREM1 increases during sepsis and can consequently be used as a biological marker for septic shock. TREM1 is strongly expressed in acute inflammatory lesions caused by bacteria and fungi. Increased TREM1 expression on monocytes is related to both infectious and noninfectious inflammatory processes.
TREM1 is vastly expressed in adult liver, lung and spleen than in corresponding fetal tissue. TREM1 is also expressed in the lymph node, placenta, spinal cord and heart tissues. TREM1 expression is more elevated in peripheral blood leukocytes than in the bone marrow and in normal cells than malignant cells. TREM1 is expressed at low levels in the early development of the hematopoietic system and in the promonocytic stage and at high levels in mature monocytes.