Search results for "Glycoprotein"

Identification of monocyte subpopulations and signaling pathways responsible for the immune response to fungal immunomodulatory glycoprotein AMPD

2016

[1] Neoglycoproteins from synthetic glycopeptides

1994

Publisher Summary Saccharide side chains of glycoproteins influence the physicochemical properties of the biomacromolecules and their stability against proteolytic degradation. Saccharide side chains of glycoproteins also play important roles as ligands in biological recognition and in the organized distribution of these compounds within multicellular organisms. Carbohydrate-lectin interactions are important, for example, in viral infections and for the recruitment and invasion of leukocytes into injured tissues. Although in a number of processes carbohydrates were revealed to be decisive recognition labels, in other biological selections peptide sequences proved to be the recognized areas.…

Comment on “Local impermeant anions establish the neuronal chloride concentration”

2014

Glykys et al . (Reports, 7 February 2014, p. 670) proposed that cytoplasmic impermeant anions and polyanionic extracellular matrix glycoproteins establish the local neuronal intracellular chloride concentration, [Cl – ] i , and thereby the polarity of γ-aminobutyric acid type A (GABA A ) receptor signaling. The experimental procedures and results in this study are insufficient to support these conclusions. Contradictory results previously published by these authors and other laboratories are not referred to.

Tenascin in denervated human muscle

1996

Tenascin is a large oligomeric glycoprotein of the extracellular matrix. Its location is limited in innervated muscle tissues. We investigated immunohistologically, using two monoclonal antibodies (mab) against Tenascin, biopsied denervated human muscle of children and adults. Tenascin was present in the interstitial space among denervated muscle fibres. Accumulation of Tenascin in denervated adult muscle tissue was frequent, accumulation in denervated muscle tissue of children was sparse and weak. The two antibodies reacted correspondingly. Tenascin was not only found in the vicinity of atrophic muscle fibres, but also close to normally sized fibres, suggesting an early stage of denervatio…

Synthetic Tumor-Associated Glycopeptide Antigens from the Tandem Repeat Sequence of the Epithelial Mucin MUC4

2004

In cancer research, the development of vaccines against tumor-associated antigens is of particular interest. Epithelial cells express mucin type glycoproteins, which are extensively O-glycosylated. In case of cancer, the expression of these mucins is increased, and their carbohydrate side chains show an aberrant glycosylation pattern. A set of single and double glycosylated hexadecapeptides representing the tandem repeat sequence of the epithelial mucin MUC4 carrying different tumor-associated carbohydrate antigens was prepared by sequential solid-phase glycopeptide synthesis. The crucial glycosyl amino acid building blocks containing the T N , T, sialyl-T N and (2,6)-sialyl-T antigens were…

Glycoproteins In Large And Small Airways And In Lung Parenchyma Of COPD Patients

2011

Posttranslational Processing of Human α2-HS Glycoprotein (Human Fetuin)

2008

α2-HS glycoprotein (α2-HS) is a major protein occuring in human blood and calciferous tissues. Due to extensive sequence identity, α2-HS has been grouped with the fetuins, a family of proteins that occur in fetal plasma in high concentrations. Native α2-HS undergoes a series of posttranslational modifications including proteolytic processing, multiple N-glycosylations and O-glycosylations, and sulfation of the carbohydrate side chains. Various two-chain forms of α2-HS have been prepared from human plasma, however, the single-chain precursor has not yet been isolated. Here, we have studied the biosynthesis of α2-HS by a human hepatoma cell line, HepG2. We demonstrate that a single-chain form…

Secretion of Protein-bound Hydroxyproline from Moss Callus Cells

1988

Abstract A glycoprotein rich in hydroxyproline was found in wall preparations of callus cells of the moss Physcomitrium pyriforme Brid. It is apparently attached to the non-cellulosic polysaccharides of the wall, and the majority is extractable by boiling the wall fraction or by using a chaotropic salt at room temperature. A pulse-chase technique was used to study the transport of this protein to the wall. Cytochalasin B seems to inhibit its secretion from the callus cells. Some of this wall-associated protein is probably secreted from the cells into the medium. Electron microscopic evidence shows vesicular activity in the cytoplasm and secretion and incorporation into the wall layers (not …

Membrane oligo- and polysialic acids

2011

AbstractPolysialic acid (polySia) and oligosialic acid (oligoSia) chains are linear polysaccharides composed of sialic acid monomers. The majority of biological poly/oligoSia chains are bound to membranes. There is a large diversity of membrane poly/oligoSia in terms of chain length, occurrence, biological function, and the mode of membrane attachment. Poly/oligoSia can be anchored to a membrane via a phospholipid (polySia in bacteria), a glycosphingolipid (oligoSia in gangliosides), an integral membrane glycoprotein, or a glycoprotein attached to a membrane via glycosylphosphatidylinositol. In eukaryotic cells, the attachment of a poly/oligoSia chain to the membrane anchor is usually throu…

Aggregation of sponge cells. Isolation and characterization of an inhibitor of aggregation receptor from the cell surface.

1979

From the cell membranes of the sponge Geodia cydonium a component was isolated and purified which inhibits the aggregation factor isolated from the same source; the component was termed anti-aggregation receptor. This molecule was characterized as a glycoprotein (54% neutral carbohydrate) and its molecular weight is in the range of 180,000 One biological site of the anti-aggregation receptor was determined to be D-galactose. Indirect evidence presented seems to indicate that this molecule is present in an active form in aggregation-deficient cells and absent in aggregation-susceptible cells.