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)

Terminal sialic acids on cell surface glycoconjugates can carry 9-O-acetyl esters. For technical reasons, it has previously been difficult to determine their precise distribution on different cell types. Using a recombinant soluble form of the Influenza C virus hemagglutinin-esterase as a probe for 9-O-acetylated sialic acids, we demonstrate here their preferential expression on the CD4 T cell lineage in normal B10.A mouse lymphoid organs. Of total thymocytes, 8-10% carry 9-O-acetylation; the great majority of these are the more mature PNA-, HSA-, and TCRhi medullary cells. While low levels of 9-O-acetylation are seen on some CD4/CD8 double positive (DP) and CD8 single positive (SP) cells, high levels are present primarily on 80- 85% of CD4 SP cells. Correlation with CD4 and CD8 levels suggests that 9-O-acetylation appears as an early differentiation marker as cells mature from the DP to the CD4 SP phenotype. This high degree of 9-O-acetylation is also present on 90-95% of peripheral spleen and lymph node CD4 T cells. In contrast, only a small minority of CD8 T cells and B cells show such levels of 9-O-acetylation. Among mature peripheral CD4 T lymphocytes, the highly O-acetylated cells are Mel 14(hi), CD44(lo), and CD45R(exon B)hi, features typical of naive cells. Digestions with trypsin and O-sialoglycoprotease (OSGPase) and ELISA studies of lipid extracts indicate that the 9-O-acetylated sialic acids on peripheral CD4 T cells are predominantly on O-linked mucintype glycoproteins and to a lesser degree, on sialylated glycolipids (gangliosides). In contrast, sialic acids on mucin type molecules of CD8 T cells are not O-acetylated; instead these molecules mask the recognition of O-acetylated gangliosides that seem to be present at similar levels as on CD4 cells. The 9-O-acetylated gangliosides on mouse T cells are not bound by CD60 antibodies, which recognize O-acetylated gangliosides in human T cells. Tethering 9-O-acetylated mucins with the Influenza C probe with or without secondary cross-linking did not cause activation of CD4 T cells. However, activation by other stimuli including TCR ligation is associated with a substantial decrease in surface 9-O-acetylation, primarily in the mucin glycoprotein component. Thus, 9-O-acetylation of sialic acids on cell surface mucins is a novel marker on CD4 T cells that appears on maturation and is modulated downwards upon activation.
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PMID:9-O-Acetylation of sialomucins: a novel marker of murine CD4 T cells that is regulated during maturation and activation. 916 29

Conjugates of pancreatic RNase and ligand-free human serum albumin (LFHSA) have been obtained. The number of hydrophobic binding sites both for initial HSA and LFHSA has been determined by the polarised luminescence method. Interaction between RNase and HSA involves additional electrovalent linkage. Unlike initial enzyme, conjugates exhibit activity toward double-strand RNA. After intravenous injection, transferase activity of unmodified enzyme remains in the blood during 20 min., whereas 30-40% of this activity is detected at the fourth day after administration of RNase conjugates. A single dose administration of LFHSA-RNAse conjugates exhibited high antiviral activity in mice, infected with influenza A and influenza B viruses.
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PMID:[Conjugates of pancreatic ribonuclease and ligand-free human serum albumin]. 1611 87

The incorporation of a polyoxometalate, octamolybdate (TBA4Mo8O26), into a metal-organic framework, mesoporous chromium terephthalate MIL-101(Cr), produces a novel hybrid Mo8O26@MIL-101(Cr). The covalent interactions of the Mo8O26 moiety in the hybrid with the N-terminal site and the multi-metal binding site of proteins offer Mo8O26@MIL-101(Cr) favorable adsorption performance towards histidine-rich proteins, giving rise to adsorption capacities of 785.6 mg g-1 for HSA and 420.1 mg g-1 for IgG at pH 5.0. Thus, a protocol for the depletion of high abundance proteins from human plasma is proposed. The percentages of serum albumin and IgG are reduced from 50.15% and 13.18% to 7.41% and 3.42%, respectively. Meanwhile, low abundance proteins, e.g., Ig heavy chains, rheumatoid factors, protein IGKV3-11, anti-H1N1 influenza HA, and cDNA FLJ53691, are enriched to a certain extent by ultra-filtration. After the depletion of high abundance proteins, 335 protein species are identified in human plasma, with respect to 265 identified from the raw plasma. This illustrates well the potential of Mo8O26@MIL-101(Cr) in the application of proteomic studies.
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PMID:An octamolybdate-metal organic framework hybrid for the efficient adsorption of histidine-rich proteins. 3226 75