Thymic stromal lymphopoietin (TSLP) is a novel member of the hemopoietic cytokine family that promotes the development of B cells and shares overlapping activity with IL-7. The human TSLP protein comprises a 28 amino acids (aa) signal sequence and 131 aa mature region. Human TSLP has two isoforms lfTSLP and sfTSLP produced by alternative splicing . lfTSLP is expressed in a number of tissues including heart, liver and prostate, and sfTSLP (63aa) is predominantly expressed in keratinocytes of oral mucosa, skin and in salivary glands. In aa sequence level, Human TSLP displays about 43% identity with mouse TSLP.TSLP is a cytokine that functions mainly on myeloid cells; it induces the release of T cell-attracting chemokines from monocytes and enhances the maturation of CD11c(+) dendritic cells.TSLP has proliferative effects on the myeloid cell line and may initiate asthma or atopic dermatitis responses by directly activating mast cells . TSLP signals cells via the interleukin-7 receptor-α chain (IL-7Rα),shared with IL-7, together with the TSLP receptor (TSLPR) subunit. Recent studies indicate that TSLP and its receptor are novel therapeutic targets for rheumatoid arthritis,for increased intraarticular TSLP concentrations in patients has caused chemotaxis and activation of arthritogenic T cells.
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.
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