Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
Trefoil Factor 1 (TFF1) belongs to the three structurally related secreted proteins that contain trefoil domains.TFF1 is an approximately peptide that has an important effect in epithelial regeneration and wound healing.It originates from musculus and highly expressed by goblet cells of the gastric and intestinal mucosa and by conjunctival goblet cells. TFF1 is a copper-binding protein that can form disulfide-linked homodimers, associate into disulfide-linked complexes with Gastrokine 2, and form non-covalent complexes with the mucin MUC5AC. TFF1 is down-regulated during the progression from gastritis to gastric dysplasia to gastric cancer, although it is up-regulated in breast and prostate cancers. TFF1 inhibits the formation of calcium oxalate crystals, and its excretion in the urine is reduced in patients with kidney stones.
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.
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