Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0393754 (HSA)
 2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

P-selectin is a Ca(2+)-dependent lectin that participates in leukocyte adhesion to vascular endothelium and platelets. Myeloid cells and a subset of T lymphocytes express carbohydrate ligands at the cell surface. Previously, we suggested that heat stable antigen (HSA/mouse CD24), an extensively glycosylated cell surface molecule on many mouse cells, is a ligand for P-selectin. Here we show that HSA mediates the binding of monocytic cells and neutrophils to P-selectin. The monocytic cell lines ESb-MP and J774, peritoneal exudate cells, and bone marrow neutrophils could bind to lipopolysaccharide-activated bend3 endothelioma cells under rotation-induced shear forces and this binding was inhibited by mAb to P-selectin and HSA. Blocking was weak at room temperature but more efficient at 4 degrees C when integrin-mediated binding was decreased. Also the adhesion of neutrophils to stimulated platelets expressing P-selectin was blocked by HSA- and P-selectin-specific mAb. Latex beads coated with purified HSA from myeloid cells bound to activated endothelioma cells or platelets, and the binding was similarly blocked by mAb to P-selectin and HSA respectively. The HSA-coated beads were stained with P-selectin-IgG, very weakly with L-selectin-IgG but not with E-selectin-IgG. The staining was dependent on divalent cations and treatment with endoglycosidase F or neuraminidase indicated that sialylated N-linked glycans were recognized. The presence of these glycans was confirmed by biosynthetic labeling studies. Our data suggest that HSA, in addition to the recently identified 160 kDa glycoprotein ligand on mouse neutrophils, belongs to a group of monospecific P-selectin ligands on myeloid cells.
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PMID:Heat stable antigen (mouse CD24) supports myeloid cell binding to endothelial and platelet P-selectin. 856

Heat-stable antigen (HSA/mouse CD24) is expressed in both haematopoietic and neural cells. The small core protein of the molecule is extensively glycosylated and anchored to the membrane via glycosylphosphatidylinositol. The role of HSA in the developing brain as well as its functional properties are poorly understood. Here we show that the brain HSA is associated with N- and O-linked oligosaccharide moieties and decorated with the HNK-1 sulfated carbohydrate epitope. It can bind P-selectin but not E-selectin and this interaction requires divalent cations and is sensitive to high salt. Brain derived HSA is also capable of binding to the L1 adhesion molecule. This interaction is distinct from the P-selectin binding as it is resistant to high salt and does not require bivalent cations. Treatment of HSA with OSGE significantly reduced binding of both P-selectin and I.1. Our data suggest that HSA can bind P-selectin and I.1 by distinct mechanism and that the binding epitopes on HSA are in close proximity.
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PMID:Heat-stable antigen (mouse CD24) in the brain: dual but distinct interaction with P-selectin and L1. 904 6

Glycated human serum albumin (Glc-HSA) has previously been reported (Higai K., et al., 2006) to induce E-selectin expression on human umbilical vein endothelial cells through activation of NADPH oxidase; however, Glc-HSA signaling in monocytes remains obscure. To clarify the influence on human monocyte-derived U937 cells, U937 cells were stimulated with Glc-HSA and glycoaldehyde-dimer-modified HSA (GA-HSA) for 2 h in the absence and presence of the protein kinase C (PKC) inhibitor calphostin and the reactive oxygen species (ROS) scavenger N-acetyl-L-cysteine (NAC) and NADPH oxidase inhibitor apocynin; interleukin-8 (IL-8) mRNA expression was determined by RT-PCR. As a result, IL-8 mRNA expression in U-937 cells was time- and dose-dependently enhanced by stimulation with Glc-HSA and GA-HSA. Furthermore, promoter activity of the IL-8 reporter gene was enhanced approximately 2-fold by stimulation with Glc-HSA and GA-HSA. Nuclear factor kappaB (NFkappaB) and activator protein-1 (AP-1) reporter genes were also enhanced although CCAAT/enhancer binding protein (C/EBP) was not affected. IL-8 mRNA expression was suppressed by NAC and apocynin but not calphostin in cells stimulated with Glc-HSA; however, its expression in cells stimulated with GA-HSA was suppressed by calphostin but not NAC. These results indicated that IL-8 mRNA expression was upregulated by NFkappaB and AP-1 in U937 cells stimulated with Glc-HSA and GA-HSA, but the signaling pathways were different.
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PMID:Glycated human serum albumin induces interleukin 8 mRNA expression through reactive oxygen species and NADPH oxidase-dependent pathway in monocyte-derived U937 cells. 1791 46