Cells glycosylation

Takano, R., Muchmore, E and Dennis, J. (1994) Sialyation and malignant potential in tumor cell glycosylation mutants. Glycobiology 4, 665-674. 

Glycosylation. Carbohydrate modifications of proteins (glycosylation) are key factors in modulating protein structures and functions within cells. Glycosylation affects probably more than half of all proteins in a eukaryotic cell [40]. In the extracellular environment, the oligosaccharide moieties of... 

Certain thiazole-containing water-soluble glycosylated polyamides were synthesized and preliminary anticancer evaluation carried out against three types of cancer cells. Glycosyl moieties were introduced onto the polyamide backbone in order to increase the water solubility of the longer polymers <2003EJO4842>. 

Epoetin Alfa. Epoetin alfa. rEPO (Epogen. Procrii). is the recombinant human erythropoietin producc d in Chinese hamster ovary cells into which the human erylhropoielin gene has been inserted. These mammalian cells glycosylate the protein in a manner similar to (hat observed in human cells. ... 

With product yield at its near maximum, the BEVS community is currently focusing on the improvement of product quality by humanizing insect cell glycosylation patterns. The unique combination of transient expression implementation, high-yield protein production capacity and the prospect of human glycoprofiles in insect cultures indicates a bright future for BEVS technology in the production of biopharmaceuticals [4, 6, 7]. 

It has been shown that two independent lines of Lec3 Chinese hamster ovary cell glycosylation mutants carrying homozygous mutations of the Gtte gene have a reduced level of cellular sialic acid. This is reflected by a reduced amount of polysialic acid (PSA) on the neural cell adhesion molecule... 

Interferons [alFN, piFN and ylFN]. Interferons are a family of glycosylated proteins and are cytokines which are produced a few hours after cells have been infected with a virus. Interferons protect cells from viral infections and have antiviral activities at very low concentrations ( 3 x 10 M, less than 50 molecules are apparently sufficient to protect a single cell). Double stranded RNA are very efficient inducers of IFNs. There are three main types of IFNs. The aIFNs are synthesised in lymphocytes and the piFNs are formed in infected fibroblasts. The a and P families are fairly similar consisting of ca 166 to 169 amino acids. Although ylFNs are also small glycosylated proteins (ca 146 amino acids), they are different because they are not synthesised after viral infections but are produced by lymphocytes when stimulated by mitogens (agents that induced cell division). 

Interleukin 2 (IL-2) is a 15.5 kDa glycosylated protein produced by helper T-cells in response to an antigen and interleukin-1. Ligation of the IL-2 receptor (expressed by a number of lymphocytes) by IL-2 stimulates growth, differentiation and survival. 

Evolution has provided the cell with a repertoire of 20 amino acids to build proteins. The diversity of amino acid side chain properties is enormous, yet many additional functional groups have been selectively chosen to be covalently attached to side chains and this further increases the unique properties of proteins. Diese additional groups play a regulatory role allowing the cell to respond to changing cellular conditions and events. Known covalent modifications of proteins now include phosphorylation, methylation, acetylation, ubi-quitylation, hydroxylation, uridylylation and glycosyl-ation, among many others. Intense study in this field has shown the addition of a phosphate moiety to a protein... 

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