Role of recombinant human erythropoietin in the treatment of cancer-related anaemia

Oncoreview ◽  
2017 ◽  
Vol 7 (2) ◽  
Author(s):  
Tomasz Jankowski ◽  
Tomasz Kubiatowski
Keyword(s):  
Recombinant Human Erythropoietin ◽  
Human Erythropoietin

scholarly journals The role of carbohydrate in recombinant human erythropoietin

1990 ◽  
Vol 188 (2) ◽  
pp. 405-411 ◽  
Author(s):  
Eisuke TSUDA ◽  
Gosei KAWANISHI ◽  
Masatsugu UEDA ◽  
Seiji MASUDA ◽  
Ryuzo SASAKI
Keyword(s):  
Recombinant Human Erythropoietin ◽  
Human Erythropoietin

scholarly journals Structural role of amino acids 99-110 in recombinant human erythropoietin

1991 ◽  
Vol 202 (2) ◽  
pp. 225-229 ◽  
Author(s):  
Yijuang CHERN ◽  
Taeowan CHUNG ◽  
Arthur J. SYTKOWSKI
Keyword(s):  
Amino Acids ◽  
Recombinant Human Erythropoietin ◽  
Structural Role ◽  
Human Erythropoietin

scholarly journals Survival of recombinant erythropoietin in the circulation: the role of carbohydrates

Blood ◽  
1989 ◽  
Vol 73 (1) ◽  
pp. 84-89
Author(s):  
MN Fukuda ◽  
H Sasaki ◽  
L Lopez ◽  
M Fukuda
Keyword(s):  
Recombinant Human Erythropoietin ◽  
Binding Protein ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Recombinant Erythropoietin ◽  
Lectin Affinity Chromatography ◽  
Glycoprotein Hormone ◽  
Human Erythropoietin

Recombinant human erythropoietin produced in transfected Chinese hamster ovary cells is glycosylated much the same way as the erythropoietin present in human urine. To determine the role of carbohydrates in the stability of recombinant human erythropoietin in vivo, [125I]-labeled recombinant erythropoietin was intravenously infused into rats. The erythropoietin was slowly cleared from the blood with a half-life of approximately two hours. Asialoerythropoietin, which was produced by treatment of recombinant human erythropoietin with sialidase, was found to be cleared rapidly from circulation within ten minutes. These data suggest that the galactose binding protein of hepatic cells is involved in the clearance of asialoerythropoietin. Erythropoietin also contains N-glycans with a few N-acetyllactosamine repeats, which can be enriched by tomato lectin affinity chromatography. The lectin-bound fraction was cleared to a larger extent than was the unfractionated erythropoietin, while the component that did not bind the lectin was found to be stable in the circulation. Authentic N-acetyllactosamine repeats (polylactosaminoglycans) prepared from erythrocytes were similarly rapidly cleared from the circulation to the liver, and this clearance was inhibitable with asialo-alpha 1- acid glycoprotein. These results suggest that (a) the sialic acid of the recombinant erythropoietin is necessary for this glycoprotein hormone to circulate stably and (b) glycoproteins with more than three lactosaminyl repeat units may be cleared by the galactose binding protein of hepatocytes.

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