Recombinant human thrombopoietin

Vadhan-Raj S. Clinical experience with recombinant human thrombopoietin in chemotherapy-induced thrombocytopenia. Semin Hematol 2000 37(2 Suppl 4) 28-34. 

Results with these agents have been mixed. In cancer patients, recombinant human thrombopoietin therapy has reduced the duration of severe thrombocytopenia and the need for platelet transfusions. On the other hand, in patients treated for 7 days with standard therapy for acute leukemia, the addition of recombinant thrombopoietin failed to accelerate platelet recovery. 

Sensory systems In a multicenter, randomised trial of 140 patients, there were 16 adverse events related to recombinant human thrombopoietin treatment [147 ]. With the exception of one patient who developed a grade 3 paroxysmal visual field defect that resolved with discontinuation of thrombopoietin, all adverse events were mild and resolved with just symptomatic treatment. 

Wang S, Yang R, Zou P, Hou M, Wu D, Shen Z, et al. A multicenter randomized controlled trial of recombinant human thrombopoietin treatment in patients with primary immune thrombocytopenia. Int J Hematol 2012 96(2) 222-8. 

Recombinant human IL-11 was under evaluation in human clinical trials for use as a thrombopoietin product for chemotherapy support.18 An ELISA was developed to measure adsorption (residual concentration in various containers over time). The ELISA was formatted with an anti-IL-11 MAb for capture and a biotinylated antibody for detection.18 A combination of HSA and Tween-20 was required to address both the adsorption of IL-11 to glass and retention of biological activity postlyophilization. 

Thrombopoietin, a 65-85 kDa glycosylated protein, is constitutively expressed by a variety of organs and cell types. Hepatocytes appear to be the major source of human thrombopoietin, and patients with cirrhosis and thrombocytopenia have low serum thrombopoietin levels. Recombinant thrombopoietin is produced by expression in human cells the recombinant product contains two intramolecular disulfide bonds and a number of carbohydrate side chains. 

Basser, R. (2002). The impact of thrombopoietin on clinical practice. Curr. Pharmaceut. Design 8(5), 369-377. Bottomley, A. et al. (2002). Human recombinant erythropoietin and quality of life a wonder drug or something to wonder about Lancet Oncol. 3(3), 145-153. 

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