maackia/inflammation

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Sialyltransferase ST3Gal-IV controls CXCR2-mediated firm leukocyte arrest during inflammation.

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Recent in vitro studies have suggested a role for sialylation in chemokine receptor binding to its ligand (Bannert, N., S. Craig, M. Farzan, D. Sogah, N.V. Santo, H. Choe, and J. Sodroski. 2001. J. Exp. Med. 194:1661-1673). This prompted us to investigate chemokine-induced leukocyte adhesion in

Inflammation-dependent changes in alpha2,3-, alpha2,6-, and alpha2,8-sialic acid glycotopes on serum glycoproteins in mice.

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The expression of acute-phase serum proteins increases in response to inflammatory stimuli. Most of these proteins are glycoproteins that often contain sialic acids (Sia). It is unknown, however, how the expression of Sia in these glycoproteins changes during inflammation. This study demonstrates

Lotus tetragonolobus, Ulex europaeus, Maackia amurensis, and Arachis hypogaea (peanut) lectins influence the binding of Helicobacter pylori to gastric carbohydrates.

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BACKGROUND The carbohydrates of gastric mucins and other sugar structures are involved in interactions with Helicobacter pylori (H. pylori) adhesins. The binding of bacteria to mucins can protect the epithelium from direct contact with the pathogen and from developing infection because of a specific

Quantitative approach to lectin-based glycoprofiling of thymic tissues in the control- and the dexamethasone-treated mice.

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Dexamethasone (DEX) is the most commonly used synthetic glucocorticoid in treatment of various inflammatory conditions. Here we focused on evaluating the effect of DEX on apoptosis and glycan profile in the mouse thymic tissues. Histological examinations revealed that the DEX treatment cause severe

Decreased sialylation of the acute phase protein alpha1-acid glycoprotein in feline infectious peritonitis (FIP).

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Feline infectious peritonitis (FIP) is an immune-mediated disease of domestic and exotic felides infected with feline coronavirus. FIP is characterized by the overexpression of an acute phase protein, the alpha1-acid glycoprotein (AGP). In humans, AGP is a heavily glycosylated protein that undergoes

Glycan moiety modifications of feline alpha1-acid glycoprotein in retrovirus (FIV, FeLV) affected cats.

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alpha1-Acid glycoprotein (AGP) is considered one of the major acute phase proteins in cats. In humans, AGP is a heavily glycosylated protein that undergoes several modifications of its glycan moiety during acute and chronic inflammatory pathologies. In this paper we present the feline AGPs (fAGP)

New Therapeutic Strategies for Osteoarthritis by Targeting Sialic Acid Receptors.

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Osteoarthritis (OA) is the most common degenerative joint disease characterized by articular cartilage degradation and joint degeneration. The articular cartilage is mainly formed by chondrocytes and a collagen-proteoglycan extracellular matrix that contains high levels of glycosylated proteins. It

Altered N-glycan profile of IgG-depleted serum proteins in Hashimoto's thyroiditis.

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Hashimoto's thyroiditis (HT) is an autoimmune disease characterized by chronic inflammation of thyroid gland. Although HT is the most common cause of hypothyroidism, the pathogenesis of this disease is not fully understood. Glycosylation of serum proteins was examined in HT only to a

Fucose and sialic acid expressions in human seminal fibronectin and α{1} -acid glycoprotein associated with leukocytospermia of infertile men.

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BACKGROUND The aim of this study was to compare fucose and sialic acid residue expression on fibronectin and α{1}-acid glycoprotein in the seminal plasma of men suspected of infertility and suffering from leukocytospermia. METHODS Seminal ejaculates were collected from 27 leukocytospermic and 18

Permeability-related changes revealed at endothelial cell borders in inflamed venules by lectin binding.

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Plasma leakage in inflammation results from intercellular gaps that form in the endothelium of venules. These gaps and related morphological changes in endothelial cells are not readily seen by light microscopy. In this study we sought to visualize such changes by using the selective binding

Alterations of branching and differential expression of sialic acid on alpha-1-acid glycoprotein in human seminal plasma.

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BACKGROUND The degree of branching and types of fucosylation of glycans on alpha(1)-acid glycoprotein (AGP) have been found to be associated with alpha(1)-acid glycoprotein concentrations in human seminal plasma. The glycosylation pattern of alpha(1)-acid glycoprotein in seminal plasma obtained from

Lipopolysaccharide changes sialylation pattern in the mouse central nervous system.

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Sialylated glycoconjugates seem to play crucial role in the mechanisms that control the most important functions of the body. Sialylation is an important mechanism for the regulation of intercellular interactions that underlie neuronal plasticity as well as immune defense in the central nervous

Distribution of sialic acid receptors and experimental infections with different subtypes of influenza A viruses in Qinghai-Tibet plateau wild pika.

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BACKGROUND The plateau pika (Ochotona curzoniae) is a small rabbit-like mammal that lives at high altitudes in the Qinghai-Tibet plateau and is in close contact with birds. Following the outbreak of highly pathogenic avian influenza (HPAI) H5N1 during 2005 in the migratory birds of Qinghai Lake, two

Lactation stage-related expression of sialylated and fucosylated glycotopes of human milk α-1-acid glycoprotein.

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BACKGROUND Because terminal sugars of α-1-acid glycoprotein (AGP) are reported to be involved in anti-inflammatory and immunomodulatory processes, their expressions might have an influence on the proper function of immune system of newborns. Here, relative amounts of sialylated and fucosylated

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