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glycan/atrofia

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Página 1 desde 128 resultados

Reduced gland mucin-specific O-glycan in gastric atrophy: A possible risk factor for differentiated-type adenocarcinoma of the stomach.

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OBJECTIVE O-glycans exhibiting terminal α1,4-linked N-acetylglucosamine (αGlcNAc) are attached to MUC6 in gastric gland mucins and serve as a tumor suppressor for gastric adenocarcinoma. Gastric atrophy is associated with risk for gastric cancer. However, the significance of αGlcNAc expression in

Alteration of N-glycans related to articular cartilage deterioration after anterior cruciate ligament transection in rabbits.

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OBJECTIVE Osteoarthritis (OA) is the most common of all joint diseases, but the molecular basis of its onset and progression is controversial. Several studies have shown that modifications of N-glycans contribute to pathogenesis. However, little attention has been paid to N-glycan modifications seen
The clinical symptoms and morphologic features of canine hepatocerebellar degeneration syndrome (CHD) bear striking resemblance to those of human carbohydrate-deficient glycoprotein syndrome (CDGS). The characteristic biochemical and molecular features of human CDGS lie in the truncated carbohydrate
Mutations in eyes shut homolog (EYS), a secreted extracellular matrix protein containing multiple laminin globular (LG) domains, and in protein O-mannose β1, 2-N-acetylglucosaminyl transferase 1 (POMGnT1), an enzyme involved in O-mannosyl glycosylation, cause retinitis pigmentosa (RP), RP25 and

S-opsin protein is incompletely modified during N-glycan processing in Rpe65(-/-) mice.

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Retinal pigment epithelium-specific protein 65 kDa (RPE65) is a key enzyme for the visual cycle in the eye. Rpe65(-/-) mice lack 11-cis-retinal, and show early cone degeneration and mislocalization of cone opsins. The present study investigated whether abnormal modification of cone opsins at the
Glycan modification prompts important concerns about the quality control of biopharmaceutical production. Conbercept is a multi-glycosylated recombinant fusion protein drug approved for the treatment of age-related macular degeneration (AMD). With 14 N-glycosites in the molecule and 7 N-glycosites

Subgroup differences in 'brain-type' transferrin and α-synuclein in Parkinson's disease and multiple system atrophy.

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Two transferrin (Tf) glycan-isoforms were previously found in cerebrospinal fluid (CSF); one appears to be derived from serum (Tf-2) and the other from choroid plexus, a CSF-producing tissue (Tf-1). To analyse metabolic differences associated with the two isoforms, their ratio (Tf-2/Tf-1) was

Specific anti-glycan antibodies are sustained during and after parasite clearance in Schistosoma japonicum-infected rhesus macaques.

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Human immunity to Schistosoma infection requires many years of exposure, and multiple infections and treatments to develop. Unlike humans, rhesus macaques clear an established schistosome infection naturally at the same time acquiring immunity towards re-infection. In macaques, schistosome egg
Excessive softening of fruits during the ripening process leads to deterioration. This is of significant global importance as softening-mediated deterioration leads to huge postharvest losses. N-glycan processing enzymes are reported to play an important role during climacteric fruit softening:

Potent antiscrapie activities of degenerate phosphorothioate oligonucleotides.

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Although transmissible spongiform encephalopathies (TSEs) are incurable, a key therapeutic approach is prevention of conversion of the normal, protease-sensitive form of prion protein (PrP-sen) to the disease-specific protease-resistant form of prion protein (PrP-res). Here degenerate

Possible role of sialylation of retinal protein glycans in the regulation of electroretinogram response in mice.

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OBJECTIVE To evaluate if the nature, degree and extent of Siaα2-3-/Siaα2-6-sialylation of retinal protein glycans plays a possible role in the development and regulation of electroretinogram response (ERG) in mice. METHODS Proteins extracted, from retinae of postnatal day 2 (PN2), PN7, and PN14 wild

Myo-Glyco disease Biology: Genetic Myopathies Caused by Abnormal Glycan Synthesis and Degradation.

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Glycosylation is a major form of post-translational modification and plays various important roles in organisms by modifying proteins or lipids, which generates functional variability and can increase their stability. Because of the physiological importance of glycosylation, defects in genes

GlcNAc6ST-1 regulates sulfation of N-glycans and myelination in the peripheral nervous system.

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Highly specialized glial cells wrap axons with a multilayered myelin membrane in vertebrates. Myelin serves essential roles in the functioning of the nervous system. Axonal degeneration is the major cause of permanent neurological disability in primary myelin diseases. Many glycoproteins have been

Dispersing the crowd: Adopting 13 C direct detection for glycans

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As a direct consequence of technological advancements, the interest in direct detection of low-gamma/low-sensitivity heteronuclei for NMR experiments has been revived. Until recently, experimental development of 13C/15N detected experiments has been focused on protein NMR. In
Carbohydrate structures between retinal neurons and retinal pigment epithelium (RPE) play an important role in maintaining the integrity of retinal adhesion to underlying RPE, and in retinal detachment pathogenesis. Since relevant knowledge is still in the primary stage, glycotopes on the adult
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