Three Trk family proteins, TrkA, TrkB, and TrkC, exhibiting different ligand specificities, have been identified. TrkA binds NGF and NT-3, TrkB binds BDNF, NT-3 and NT-4/5, and TrkC only binds NT-3. The primary location of TrkC expression is in the nervous system and, specifically, in regions of the CNS. Low level TrkC expression has also been observed in a wide variety of tissues outside the nervous system. Receptor tyrosine kinase involved in nervous system and probably heart development. Upon binding of its ligand NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different signaling pathways, including the phosphatidylinositol 3-kinase/AKT and the MAPK pathways, that control cell survival and differentiation.
NT-3 growth factor receptor also known as neurotrophic tyrosine kinase receptor type 3 or TrkC tyrosine kinase or Trk-C receptor, is a member of the neurotrophic tyrosine receptor kinase (NTRK) family. This kinase is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. TrkC/NTRK3 is widely expressed in the developing and adult nervous system. In later embryonic development, TrkC/NTRK3 is expressed in various structures of the CNS including the caudatoputamen, septal nuclei, cerebellum, and brainstem. Other neurotrophins include nerve growth factor(NGF), neurotrophin-3 and neurotrophin-4. In the PNS, trkC hybridization appears to correlate, both temporally and spatially, with the outgrowth of axons toward their peripheral targets. TrkC/NTRK3 is widely expressed in the three identified branches of the mammalian nervous system and appears to correlate with the expression of NT-3, its cognate ligand. The apparent colocalization of trkC transcripts with NT-3 raises the possibility this neurotrophin exerts its trophic effects by a paracrine and/or autocrine mechanism. Signalling through this kinase leads to cell differentiation and may play a role in the development of proprioceptive neurons that sense body position. Mutations in TrkC encoding gene have been associated with medulloblastomas, secretory breast carcinomas and other cancers.
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.
Tumor-associated calcium signal transducer 2(Tacstd2), also known as Cell surface glycoprotein Trop-2, belongs to the EPCAM family. Tacstd2 expressed in kidney, lung, ovary and testis and has high levels of expression in immortalized keratinocytes. Tacstd2 may functions as a growth factor receptor. It has negative regulation of branching involved in ureteric bud morphogenesis, cell motility, epithelial cell migration, ruffle assembly, stress fiber assembly and substrate adhesion-dependent cell spreading. Also, it has positive regulation of stem cell proliferation. Tacstd2 is capable of transducing an intracellular calcium signal and may play a role in tumor growth. It also has adhesive functions.
Trypsin-2, also known as Trypsin II, Anionic trypsinogen, Serine protease 2, PRSS2 and TRY2, is a secreted protein which 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 onepeptidase S1 domain. It is secreted into theduodenum,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 inactivezymogen,trypsinogen and cleaved to its active form in the small intestine when the pancreas is stimulated bycholecystokinin through the common activation mechanism.
Thymic stromal lymphopoietin (TSLP) is a protein belonging to the cytokine family, contains 140 amino acids. It is known to play an important role in the maturation of T cell populations through activation of antigen presenting cells. TSLP induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c+ dendritic cells. It can induce allergic inflammation by directly activating mast cells. TSLP is produced mainly by non-hematopoietic cells such as fibroblasts, epithelial cells and different types of stromal or stromal-like cells. These cells are located in regions where TSLP activity is required.
Thymic Stromal Lymphopoietin (TSLP) was originally identified as an activity from the conditioned medium of a Mouse thymic stromal cell line that promoted the development of B cells. The activities of Mouse TSLP overlap with , but are distinct from , those of Mouse IL-7. Both Mouse TSLP and IL-7 can co-stimulate growth of thymocytes and mature T cells , and support B lymphopoiesis in long-term cultures of fetal liver cells and bone-marrow cells. Whereas Mouse IL-7 facilitates the development of B220+/IgM-pre-B cells , Mouse TSLP promotes the development B220+/IgM+ B cells. Human TSLP was reported to preferentially stimulate myeloid cells, inducing the release of T cell-attracting chemokines from monocytes and enhancing the maturation of CD11c+ dendritic cells. Mouse TSLP cDNA encodes a 140 amino acid (aa) residue precursor protein with a 19 aa signal sequence. Within the mature region , there are three potential N-glycosylation sites and 7 cysteine residues. Mouse TSLP shares approximately 43% aa sequence identity with Human TSLP. The gene for Mouse TSLP has been localized to chromosome 18. By Northern and RT-PCR analysis , Mouse TSLP expression has been detected in spleen , thymus , kidney , lung and bone marrow. TSLP is proposed to signal through a heterodimeric receptor complex that consists of IL-7 R alpha and the TSLP R , a new member of the hemopoietin receptor family most closely related to R gamma c.
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