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.
Thymic stromal lymphopoietin (TSLP) is an interleukin 7 (IL-7)-like cytokine originally characterized by its ability to promote the activation of B cells and dendritic cells (DCs). Thymic stromal lymphopoietin (TSLP) is a cytokine expressed by epithelial cells, including keratinocytes, and is important in allergic inflammation. Subsequent studies have shown that TSLP promotes T helper type 2 (TH2) cell responses associated with immunity to some helminth parasites and the pathogenesis of many inflammatory diseases, including atopic dermatitis and asthma. TSLP can promote TH2 cytokine-associated inflammation by directly promoting the effector functions of CD4+ TH2 cells, basophils and other granulocyte populations while simultaneously limiting the expression of DC-derived proinflammatory cytokines and promoting regulatory T cell responses in peripheral tissues.
The cytokine thymic stromal lymphopoietin receptor (TSLPR) is consisting of a common γ receptor–like chain (TSLPR-γ) and a common interleukin 7 (IL-7) Rα chain that belongs to the type 1 cytokine receptor family. Transfection of TSLPR cDNA result in only low affinity binding, while cotransfection of the IL-7Rα chain cDNA shows high affinity binding. TSLP and TSLPR play a critical role in the initiation of allergic diseases in mice. The TSLP R cDNA encodes a transmembrane receptor containing 370 amino acids (aa) with two potential N-linked glycosylation sites and a cytoplasmic domain of 104 aa including a single tyrosine residue. TSLPR can mediate signaling of the signal transducer and activator of transcription 5 (Stat5) by TSLP. TSLP R is broadly expressed in the immune and hematopoietic cells, particularly in hematopoietic progenitors and myeloid cells.
TWSG1 belongs to the twisted gastrulation protein family. TWSG1 from different species are functionally equivalent. In contrast to Drosophila where TWSG1 expression is limited to early embryos, expression of TWSG1 is found throughout mouse and human development. Mutations in the TWSG1 gene cause at least some of the cells on the dorsal half of the embryo to adopt more ventral cell fates. This is thought to involve gradients of the signaling molecule decapentaplegic. TWSG1 may function as a bone morphogenetic protein signalling agonist or antagonize these activities. It can dislodge latent bone morphogenetic proteins and thus provides a permissive signal that allows high BMP signaling in the embryo. TWSG1 is a cofactor in the antagonism of chordin to BMP signaling. It also binds both the vertebrate Decapentaplegic ortholog BMP4 and chordin and forms ternary complexes. Meanwhile, TWSG1 increases binding of chordin to BMP4, potentiates the ability of chordin to induce secondary axes in Xenopus embryos, and enhances chordin cleavage by vertebrate proteases related to tolloid at a site poorly used in the absence of TWSG1. The presence of TWSG1 enhances the secondary axis-inducing activity of 2 products of chordin cleavage.
Dtk, also called Tyro3, belongs to the TAM receptor family of receptor protein tyrosine kinases (RPTKs) composed of three receptors Tyro3, Axl, and Mer. These receptors share a characteristic molecular structure of two immunoglobulin-like and two fibronectin type III repeats and have been best characterized for their roles in immune regulation, fertility, thrombosis and phagocytosis. Gas6 and protein S have been identified as ligands for these receptors. Gas6 binding induces tyrosine phosphorylation and downstream signaling pathways that can lead to cell proliferation, migration, or the prevention of apoptosis. Tyro3 and Axl play important regulatory roles in a variety of tissues, including the central nervous, reproductive, immune, and vascular systems. Tyro3 is widely expressed during embryonic development and preferentially expressed during neurogenesis in the central nervous system.
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