Recombinant Murine TFF-2 is an 11.9 kDa polypeptide of 106 amino acid residues, which includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds. The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are expressed in the gastrointestinal tract, and appear to play an important role in intestinal mucosal defense and repair. TFF2 has been shown to inhibit gastrointestinal motility and gastric acid secretion. Recent data suggests a potential role for TFF2 in acute and chronic asthma.
Trefoil factors (TFF) are secretory products of mucin producing cells. They play a key role in the maintenance of the surface integrity of oral mucosa and enhance healing of the gastrointestinal mucosa by a process called restitution. TFF comprises the gastric peptides (TFF1), spasmolytic peptide (TFF2), and the intestinal trefoil factor (TFF3). They have an important and necessary role in epithelial restitution within the gastrointestinal tract. Members of the trefoil family are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfide bonds. They are stable secretory proteins expressed in gastrointestinal mucosa. Trefoil Factor 3(TFF3) is involved in the maintenance and repair of the intestinal mucosa. TFF3 promotes the mobility of epithelial cells in healing processes (motogen).
Triggering Receptor Expressed on Myeloid Cells 1 (TREM-1) is a transmembrane protein with a single Ig-like domain. TREM-1 associates with the adapter protein, DAP12, to deliver an activating signal. TREM-1 is expressed on blood neutrophils and monocytes, and the expression is up-regulated by bacterial LPS. TREM-1 is expressed at high levels on neutrophils of patients with microbial sepsis and in mice with a TREM-1/Fc fusion protein protected mice against LPS-induced shock. It stimulates neutrophil and monocyte-mediated inflammatory responses. Triggers release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. TREM-1 is amplifier of inflammatory responses that are triggered by bacterial and fungal infections and are a crucial mediator of septic shock.
Triggering receptor expressed on myeloid cells-2 (TREM-2) is a cell surface receptor primarily expressed on macrophages, osteoclasts, microglia and dendritic cells. TREM-2 is one member of the TREM family, inhibiting the releasing of inflammatory mediators, so it is an important in vivo anti-inflammatory receptor. TREM-2 consists of an 18 aa signal sequence, a 153 aa extracellular domain (ECD) with one V-type Ig-like domain, a 21 aa transmembrane (TM) domain, and a 35 aa cytoplasmic tail. A soluble form of TREM-2 (TREM-2b) created by alternate splicing diverges at aa 161. TREM-2 transduces intracellular signals through the adaptor DAP12. After binding of TREM-2 with ligand, the TREM-2/DAP12 (dead-cell-activated-receptor-associated protein)-mediated signal transduction pathway causes a series of intracellular protein tyrosine phosphorylation reactions and enzymatic reactions, which then activate the myeloid cells and participate T cell responses.
Trem-like transcript 2 protein (TLT2), also known as Triggering receptor expressed on myeloid cells-like protein 2, TLT2 and C6orf76, is single-pass type I membrane protein. TREML2 contains one Ig-like V-type domain, which can be induced in CD4 T-cell by concanavalin-A. As a cell surface receptor, TREML2 may play a role in the innate and adaptive immune response. TREML2 also acts as a counter-receptor for CD276 and interaction with CD276 on T-cells enhances T-cell activation. It has shown that TREML2 may be involved in the innate immune response based on its expression profile and the fact that it is up-regulated in response to inflammation.
Transferrin is a glycoprotein with an approximate molecular weight of 76.5 kDa. This glycoprotein is thought to have been created as a result of an ancient gene duplication event that led to generation of homologous C and N-terminal domains each of which binds one ion of ferric iron. The function of Transferrin is to transport iron from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. This protein may also have a physiologic role as granulocyte / pollen-binding protein (GPBP) involved in the removal of certain organic matter and allergens from serum. Transferrins are iron binding transport proteins which bind Fe3+ ion in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. When a transferrin loaded with iron encounters with a transferring receptor on cell surface, transferring binds to it and, as a consequence, is transported into the cell in a visicle by receptor-mediated endocytosis. The PH is reduced by hydrogen iron pumps. The lower pH causes transferrin to release its iron ions. The receptor is then transported through the endocytic cycle back to the cell surface, ready for another round of iron uptake. Each transferrin molecule has the ability to carry two iron ions in the ferric form.
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