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Glycosylation decrease

Decreased growth rate, increased glucose/ glutamine consumption Apoptosis, decreased growth rate, altered glycosylation Decreased growth and protein production... [Pg.1438]

The three N-linked glycosylation sites of the a-leader have been shown to be important - but not essential - for the ability of the a-factor leader to secrete a-factor [32, 33], In addition, mutation of all three-consensus sites for N-linked glycosylation decreased the quantity of secreted insulin precursor to 10% [34], In contrast to what was found with the a-leader, elimination of the two consensus sites for N-linked glycosylation in one of the newly developed leaders, actually improved the ability to facilitate secretion of the insulin precursor [31],... [Pg.1038]

The pKj, value (2.43) of the hydration constant of the cyanidin was found to be lower than the pKj, values of glycosylated and acylated cyanidins, meaning lower resistance of the anthocyanidin to hydration. The stability of nonacylated 3,5-diglucosides was lower compared to the 3-glucoside because the 5 position markedly lowered the hydration constant due to decreased electron density of the pyrilium ring that favors nucleophilic attack by water, enhancing hemiacetal formation. ... [Pg.260]

Studies have shown that in patients with chemotherapy-related anemia, therapy with erythropoietin products (epoetin-alfa and darbepoetin) can increase hemoglobin, decrease transfusion requirements, and improve quality of life.12 Epoetin is recombinant human erythropoietin, and darbepoetin is structurally similar to endogenous erythropoietin. Both bind to the same receptor to stimulate red blood cell production. Darbepoetin differs from epoetin in that it is a glycosylated form and exhibits a longer half-life in the body. The half-lives of a single subcutaneous injection of epoetin or darbepoetin in patients are roughly 27 and 43 hours, respectively. [Pg.983]

At present, antioxidants are extensively studied as supplements for the treatment diabetic patients. Several clinical trials have been carried out with vitamin E. In 1991, Ceriello et al. [136] showed that supplementation of vitamin E to insulin-requiring diabetic patients reduced protein glycosylation without changing plasma glucose, probably due to the inhibition of the Maillard reaction. Then, Paolisso et al. [137] found that vitamin E decreased glucose level and improved insulin action in noninsulin-dependent diabetic patients. Recently, Jain et al. [138] showed that vitamin E supplementation increased glutathione level and diminished lipid peroxidation and HbAi level in erythrocytes of type 1 diabetic children. Similarly, Skyrme-Jones et al. [139] demonstrated that vitamin E supplementation improved endothelial vasodilator function in type 1 diabetic children supposedly due to the suppression of LDL oxidation. Devaraj et al. [140] used the urinary F2-isoprostane test for the estimate of LDL oxidation in type 2 diabetics. They also found that LDL oxidation decreased after vitamin E supplementation to patients. [Pg.925]

Incomplete (N-linked) glycosylation prompts decreased in vivo activity due to more rapid hepatic clearance of the EPO molecule. Enzymatic removal of terminal sialic acid sugar residues from oligosaccharides exposes otherwise hidden galactose residues. These residues are then free to bind specific hepatic lectins, which promote EPO removal from the plasma. The reported plasma tm value for native EPO is 4-6 h. The tm for desialated EPO is 2 min. Comparison of native human EPO with its recombinant form produced in CHO cells reveals very similar glycosylation patterns. [Pg.273]

The efficiency of this approach could be demonstrated in a-fucosylation with donor 32a and the acceptors 19C and 33A-D (Table XXXIII). Thus, with the help of this inverse procedure, the versatile building blocks for syntheses of the Lea, Le, Ley, and H antigen determinants are readily accessible (176). Presumably, this procedure may become of general importance when reactive glycosylating agents are employed. Alternatively, the reactivity of the fucosyl donor could be decreased, as has been recently proven very successfully (177). [Pg.105]


See other pages where Glycosylation decrease is mentioned: [Pg.429]    [Pg.2290]    [Pg.286]    [Pg.429]    [Pg.2290]    [Pg.286]    [Pg.127]    [Pg.1187]    [Pg.867]    [Pg.229]    [Pg.75]    [Pg.121]    [Pg.447]    [Pg.531]    [Pg.172]    [Pg.330]    [Pg.71]    [Pg.262]    [Pg.131]    [Pg.281]    [Pg.343]    [Pg.570]    [Pg.594]    [Pg.254]    [Pg.867]    [Pg.315]    [Pg.310]    [Pg.340]    [Pg.35]    [Pg.41]    [Pg.44]    [Pg.103]    [Pg.213]    [Pg.166]    [Pg.31]    [Pg.305]    [Pg.106]    [Pg.24]    [Pg.101]    [Pg.218]    [Pg.219]    [Pg.41]    [Pg.310]    [Pg.227]    [Pg.176]    [Pg.201]    [Pg.207]   
See also in sourсe #XX -- [ Pg.275 ]




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