نتایج جستجو برای: signal regulatory proteins (sirp)
تعداد نتایج: 1068020 فیلتر نتایج به سال:
signal regulatory proteins (sirp) belong to immunoglobulin super family (igsf) and relate to integrin signaling cascades. it has been shown that sirpa is expressed in a variety of cells including myeloid cells and neurons. in the present study the expression of this igsf member in articular chondrocytes was investigated. methods: using a panel of anti-sirpalpha antibodies, immunohistochemistry,...
Signal regulatory proteins (SIRP) belong to immunoglobulin super family (IgSF) and relate to integrin signaling cascades. It has been shown that SIRPa is expressed in a variety of cells including myeloid cells and neurons. In the present study the expression of this IgSF member in articular chondrocytes was investigated. Methods: Using a panel of anti-SIRPalpha antibodies, immunohistochemistry...
Signal-regulatory proteins (SIRPs) are transmembrane glycoproteins belonging to the immunoglobulin (Ig) superfamily that are expressed in the immune and central nervous systems. SIRP binds CD47 and inhibits the function of macrophages, dendritic cells, and granulocytes, whereas SIRP 1 is an orphan receptor that activates the same cell types. A recently identified third member of the SIRP family...
Signal-regulatory proteins (SIRP) are transmembrane glycoproteins with three extracellular Ig-like domains, closely related to Ag receptors Ig, TCR, and MHC, and a cytoplasmic domain with two immunoreceptor with tyrosine-based inhibition motifs that can interact with src homology 2 domain-containing phosphatases. SIRP have previously been shown to inhibit signaling through receptor tyrosine kin...
Signal regulatory proteins (SIRPs) constitute a family of transmembrane glycoproteins with extracellular Ig-like domains. Several SIRP family members have thus far been identified on myeloid and other cells in man, mouse, rat, and cattle. In the present study, we provide a description of the SIRP multigene family, including a number of previously undescribed SIRP genes, based on the complete ge...
Signal-regulatory proteins (SIRPs) comprise a novel transmembrane glycoprotein family involved in the negative regulation of receptor tyrosine kinase-coupled signaling pathways. To analyze the expression and function of SIRPs, we prepared soluble recombinant fusion proteins of the extracellular regions of SIRPalpha1 and SIRPalpha2, as well as a variety of monoclonal antibodies (MoAbs) against t...
In autoimmune hemolytic anemia (AIHA), circulating red blood cells (RBCs) opsonized with autoantibody are recognized by macrophage Fc g and complement receptors. This triggers phagocytosis and elimination of RBCs from the circulation by splenic macrophages. We recently found that CD47 on unopsonized RBCs binds macrophage signal regulatory protein a (SIRP a ), generating a negative signal that p...
Signal-regulatory proteins (SIRPs) comprise a novel transmembrane glycoprotein family involved in the negative regulation of receptor tyrosine kinase-coupled signaling pathways. To analyze the expression and function of SIRPs, we prepared soluble recombinant fusion proteins of the extracellular regions of SIRPa1 and SIRPa2, as well as a variety of monoclonal antibodies (MoAbs) against these dom...
CD47 on live cells actively engages signal-regulatory protein-alpha (SIRP-alpha) on phagocytes and delivers a negative signal that prevents their elimination. We evaluated the biological consequences of SIRP-alpha ligation on the dendritic cell (DC) response to maturation signals and the potential interplay with the IL-10/IL-10R inhibitory pathway. At first, CD47/SIRP-alpha allowed the generati...
Kurihara H, Harita Y, Ichimura K, Hattori S, Sakai T. SIRP-CD47 system functions as an intercellular signal in the renal glomerulus. Am J Physiol Renal Physiol 299: F517–F527, 2010. First published June 16, 2010; doi:10.1152/ajprenal.00571.2009.—The renal glomerulus consists of endothelial cells, podocytes, and mesangial cells. These cells cooperate with each other for glomerular filtration; ho...
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