Receptor for thymic stromal lymphopoietin (TSLP). Forms a functional complex with TSLP and IL7R which is capable of stimulating cell proliferation through activation of STAT3 and STAT5. Also activates JAK2 (By similarity). Implicated in the development of the hematopoietic system. TSLP R expression is ubiquitous in the immune and hematopoietic cells, but is up-regulated in Th2-skewed cells. Cells expressing TSLP R alone bind TSLP with low affinity. Co-expression of TSLP R and IL-7 R alpha is required for high-affinity TSLP binding and signal transduction . The TSLP R and IL-7 R alpha are coexpressed primarily on monocytes and dendritic cells and at lower levels in lymphoid cells. TSLP has been shown to induce the release of T cell-attracting chemokines from monocytes and enhance the maturation of CD11c+ dendritic cells.
TSPAN1 belongs to the transmembrane 4 superfamily, also known as the tetraspanin family. Tetraspanins have four hydrophobic domains, intracellular N- and C-termini and two extracellular domains. Tetraspanins act as scaffolding proteins, anchoring multiple proteins to one area of the cell membrane. They also mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. TSPAN1 interacts with human thiamine transporter-1 (hTHTR-1). HTHTR-1 contributes to intestinal thiamine uptake, and its function is regulated at both the transcriptional and posttranscriptional levels. TSPAN1 and hTHTR-1 colocalize in human intestinal epithelial HuTu-80 cells. Coexpression of TSPAN1 in these cells led to a significant decrease in the rate of degradation of hTHTR-1 compared with cells expressing the hTHTR-1 alone; in fact the half-life of the TSPAN1 protein was twice longer in the former cell type compared with the latter cell type.
Tetraspanin 8 (TSPAN8) as an important modulator of melanoma invasiveness; and several of its transcriptional regulators; which affect TSPAN8 expression during melanoma progression toward an invasive stage. p53 as a negative regulator of Tspan8 expression. p53 as a regulator of melanoma invasion and the concept that reactivating p53 could provide a strategy for modulating not only proliferative but also invasive capacity in melanoma treatment. Tetraspanin 8 (TSPAN8) is a tumor-associated antigen implicated in tumor progression and metastasis. TSPAN8 may play an important role in mCRC cell invasion. TSPAN8 was overexpressed in human gastric cancer tissues and gastric cancer cell lines compared with the normal. TSPAN8 overexpression promoted cell proliferation and invasion; while TSPAN8 suppression inhibited cell proliferation and invasion. TSPAN8 could activate the ERK MAPK pathway in gastric cancer cells; and MEK-ERK inhibition reversed the effects of TSPAN8 overexpression on cell proliferation and invasion.
GDP-L-Fucose Synthase is a NADP(H)-binding protein. It catalyzes the two-step epimerase and the reductase reactions in GDP-D-mannose metabolism, converting GDP-4-keto-6-D-dexoymannose to GDP-L-fucose. GDP-L-Fucose is the substrate of several fucosyltransferase, involving the expression of mamy glycoconjugates, including blood group ABH antigens and development adhesion antigens. Mutations in the TSTA3 gene may cause leukocyte adhesion deficiency type II.
Tubulin Beta-4A Chain (TUBB4A) is a cytoplasmic peptide containing 444 amino acids. TUBB4A is a member of the Tubulin family. Tubulin is the major constituent of microtubules. Tubulin is a dimer composed of one alpha and one beta tubulin molecule; there are many forms of beta tubulins, Beta II and Beta IV Tubulin are ubiquitously expressed. Beta-III Tubulin, also known as Tubulin Beta-4, is regarded as a neuron-specific marker. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain.
Tubulin is the major constituent of microtubules. Gamma tubulin is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly.
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