Recombinant granulocyte colony-stimulating factor-transferrin fusion protein as an oral myelopoietic agent
Document Type
Article
Publication Date
2005
Abstract
An expression construct harboring granulocyte colony-stimulating factor (G-CSF)-transferrin (Tf) fusion protein (G-CSF-Tf) was engineered by fusing human cDNAs encoding G-CSF and Tf to explore the feasibility of using Tf as a carrier moiety for oral delivery of therapeutic proteins. The recombinant protein, G-CSF-Tf, was harvested from protein-free, conditioned medium of transfected HEK293 cells. The in vitro studies demonstrated that the purified G-CSF-Tf fusion protein possesses the activity of both Tf receptor (TfR) binding in Caco-2 cells and G-CSF-dependent stimulation of NFS-60 cell proliferation. Subcutaneous administration of G-CSF-Tf fusion protein to BDF1 mice demonstrated a pharmacological effect comparable to the commercial G-CSF on the increase of absolute neutrophil counts (ANC). However, the fusion protein elicited a significant increase in ANC upon oral administration to BDF1 mice, whereas G-CSF had no effect. This study also showed that orally administered G-CSF-Tf elicits a sustained myelopoietic effect up to 3 days, whereas the s.c. administered G-CSF or G-CSF-Tf lasts only 1 day. Furthermore, coadministration of free Tf abolished the increase of ANC by orally delivered G-CSF-Tf, suggesting that the recombinant protein is absorbed via a TfR-mediated process in the gastrointestinal tract. Taken together, we conclude that the Tf-based recombinant fusion protein technology represents a promising approach for future development of orally effective peptide and protein drugs.
Publication Title
Proceedings of the National Academy of Sciences of the United States of America
Volume
102
Issue
20
First Page
7292
Last Page
7296
Recommended Citation
Bai, Yun; Ann, David K.; and Shen, Wei-Chiang, "Recombinant granulocyte colony-stimulating factor-transferrin fusion protein as an oral myelopoietic agent" (2005). PCOM Scholarly Works. 1015.
https://digitalcommons.pcom.edu/scholarly_papers/1015
Comments
This article was published in Proceedings of the National Academy of Sciences of the United States of America, Volume 102, Issue 20, Pages 7292-7296.
The published version is available at http://dx.doi.org/10.1073/pnas.0500062102.Copyright © 2005 National Academies.