Trefoil Factor 3 (TFF3) is one of three trefoil peptides secreted by epithelial cells that line mucus membranes. Trefoils contribute to protection and repair of the gastrointestinal tract. TFF3 is secreted by mucus-producing goblet cells in the large and small intestines and lower respiratory tract. It is mainly active as a disulfide-linked homodimer. The mature 59 aa, 6.5 kDa human TFF3 contains one trefoil structure formed by intramolecular disulfides and shows 76% aa identity with mouse TFF3.
TREM1 (triggering receptor expressed on myeloid cells) is a type I transmembrane protein with a single Ig-like domain; and is selectively expressed on blood neutrophils and a subset of monocytes. As a member of the growing family of receptors related to NK cell receptors; TREM1 activates downstream signaling events with the help of an adapter protein called DAP12. Expression of TREM1 is up-regulated by bacterial LPS; a ligand for TLR4; as well as lipoteichoic acid. Although its natural ligand has not been identified; engagement of TREM1 with agonist mAbs triggers secretion of the proinflammatory cytokines TNF-α and IL-1β; as well as chemokines such as IL-8 and monocyte chemoattractant protein (MCP)-1. Intracellularly; TREM1 induces Ca2+ mobilization and tyrosine phosphorylation of extracellular signal-related kinase 1 (ERK1); ERK2 and phospholipase C-γ. In an animal model of LPS-induced septic shock; blockade of TREM1 signaling inhibited hyperresponsiveness and death. Thus; it has been demonstrated that TREM1 performs a critical function in immune responses involved in host defense against microbial challenges; and is suggested to be a potential therapeutic target for septic shock.
TREM1 (triggering receptor expressed on myeloid cells) is a type I transmembrane protein with a single Ig-like domain, and is selectively expressed on blood neutrophils and a subset of monocytes. As a member of the growing family of receptors related to NK cell receptors, TREM1 activates downstream signaling events with the help of an adapter protein called DAP12. Expression of TREM1 is up-regulated by bacterial LPS, a ligand for TLR4, as well as lipoteichoic acid. Although its natural ligand has not been identified, engagement of TREM1 with agonist mAbs triggers secretion of the proinflammatory cytokines TNF-α and IL-1β, as well as chemokines such as IL-8 and monocyte chemoattractant protein (MCP)-1. Intracellularly, TREM1 induces Ca2+ mobilization and tyrosine phosphorylation of extracellular signal-related kinase 1 (ERK1), ERK2 and phospholipase C-γ. In an animal model of LPS-induced septic shock, blockade of TREM1 signaling inhibited hyperresponsiveness and death. Thus, it has been demonstrated that TREM1 performs a critical function in immune responses involved in host defense against microbial challenges, and is suggested to be a potential therapeutic target for septic shock.
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. Human TREM-1 shares 42% sequence homology with mouse TREM-1.
Triggering Receptor Expressed on Myeloid cells 2 (TREM2)is a 35 kDa type I transmembrane member of the TREM family and Ig superfamily. Mature human TREM2 consists of a 156 amino acid (aa) extracellular domain (ECD) with one V-type Ig-like domain, a 21 aa transmembrane (TM) domain, and a 35 aa cytoplasmic tail. Soluble forms of the TREM2 ECD are generated by alternative splicing or proteolytic cleavage, and the cytoplasmic domain can be liberated by gamma-Secretase mediated intramembrane cleavage. A positively charged lysine within the transmembrane segment allows association with the signal adapter protein, DAP12 and inhibition of macrophage activation. TREM2 is expressed on macrophages, immature myeloid dendritic cells, osteoclasts, microglia, and adipocytes.It promotes the differentiation and function of osteoclasts, the production of inflammatory cytokines by adipocytes, insulin resistance, and the phagocytic clearance of bacteria.
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