An introduction to the glycoprotein erythropoietin

Recombinant erythropoietin was successfully expressed in P.

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Dependent on the underlying disease and endogenous EPO levels, EPO treatment has also been shown to be effective in correcting anemia and reducing the need for blood transfusions in cancer and other diseases.

EPO production increases in response to tissue hypoxia, low arterial oxygen concentration and increased oxygen affinity of RBCs. One of these assays, the exhypoxic polycythemic mouse assay,31 is still used as the reference standard for testing and calibrating EPO preparations and EPO assays.

The total glycoprotein weighs 30 kDa with the peptide backbone weighing 18 kDa.

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The primer sets used are indicated in Table 1. In healthy individuals and patients with various types of anemia e. Some studies reported EPO-R expression on endothelial cells at levels as high as 27, molecules per cell. Recombinant EPO produced in mammalian cells is fully glycosylated. These include steroid hormones, prostaglandins, metals e. Erythropoietin after a century of research: younger than ever. After the biniding of EPO, 8 tyrosine residues are phosphoralated which activates the [14]. These molecules can bind to and activate EPO-R and are effective in vivo. This phenomenon is not unusual since hyperglycosylation or hypermannosylation is frequent in yeast expression systems Wu et al. Clinical trials in humans with ischemic heart, neural and renal tissues have not demonstrated the same benefits seen in animals.

However, indirect dependence of red cell longevity in the blood on plasma erythropoietin levels has been reported, a process termed neocytolysis.

The extracellular sinding site 1 and Binding site 2 are composed of [12].

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Efficiency of signalling through cytokine receptors depends critically on receptor orientation.

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