Interleukin 7 Receptor alpha (IL-7RA) , also known as CD127 , is a 75 kDa hematopoietic receptor superfamily member that plays an important role in lymphocyte differentiation , proliferation , and survival. IL-7 receptor alpha (CD127) signaling is essential for T-cell development and regulation of naive and memory T-cell homeostasis. IL-7RA is critically required for the proper development and function of lymphoid cells. Therefore , the IL-7RA is critically required for the proper development and function of lymphoid cells. Studies from both pathogenic and controlled HIV infection indicate that the containment of immune activation and preservation of CD127 expression are critical to the stability of CD4(+) T cells in infection. A better understanding of the factors regulating CD127 expression in HIV disease , particularly on T(CM) cells , might unveil new approaches exploiting the IL-7/IL-7R receptor pathway to restore T cell homeostasis and promote immune reconstitution in HIV infection. Factors relevant to HIV infection that could potentially decrease CD127 expression on Human CD8(+) T cells. CD127 down-regulation may be an important contributor to HIV-associated T-cell dysfunction. In addition to IL-7 , IL-7RA also associates with TSLPR to form the functional receptor for thymic stromal lymphopoietin (TSLP) which indirectly regulates T cell development by modulating dendritic cell activation. Mutations in the Human IL-7RA gene cause a type of severe combined immunodeficiency in which the major deficiencies are in T cell development , whereas B and NK cells are relatively normal in number. Variation in the IL7RA gene was recently found associated with multiple sclerosis (MS). The polymorphisms in the IL7RA gene is involved in MS pathogenesis and suggest that IL7RA variation may primarily affect chronic disease courses. Soluble CD127 (sCD127) appears to play an important role in the immunopathogenesis of several chronic infections , multiple sclerosis , and various cancers.
Interleukin-9 (IL-9) is a secreted protein that belongs to the IL-7/IL-9 family.Mature mouse IL-9 shares 57% and 74% amino acid sequence identity with human and rat IL-9, respectively. IL-9 supports IL-2 independent and IL-4 independent growth of helper T-cells. IL-9 stimulates cell proliferation and prevents apoptosis. It functions through the IL-9 receptor (IL-9R), which activates different signal transducer and activator (STAT) proteins and thus connects this cytokine to various biological processes. IL-9 has been identified as a candidate gene for asthma. IL-9 is a determining factor in the pathogenesis of bronchial hyperresponsiveness.
IMPAD1 protein (IMPA3, gPAPP or IMPase 3) belongs to the inositol monophosphatase family. It is found in Purkinje cells, brain stem, lung and chondrocytes. Mouse IMPAD1 gene encodes a type II transmembrane Golgi-embedded glycoprotein with 356 amino acid residues which generates a 306 amino acid residues mature protein after processing. It is expressed in embryo, and in theory may catalyze myo-inositol monophosphate to myo-inositol. Free myo-inositol is used to generate inositol phospholipid, an essential component of intracellular signaling pathways that mobilize calcium. Mouse IMPAD1 exhibits 91% sequence identity with the human homologue.
Insulin is a disulfide-linked heterodimeric protein secreted by the pancreatic Islets of Langerhans. Mature insulin is generated by the proteolytic removal of a peptide from proinsulin. It is involved in the regulation of glucose metabolism through interactions with the Insulin Receptor.
At least 23 different variants of Interferon-α are known. The individual proteins have molecular masses between 19-26 kD and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-α subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-α subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxyl-terminal end.
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