• Journal of Veterinary Clinics
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• v.31 no.2
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• pp.77-84
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• 2014

The present study evaluated that responses of peripheral and bone marrow depends on the frequency of recombinant human granulocyte colony-stimulating factor (rhG-CSF) administration in dogs. The rhG-CSF has been revealed that have a beneficial effect for dogs with myelosuppression secondary to chemotherapy or radiation but there were no studies about the frequency of administration in dogs. In this research, rhG-CSF was administrated $5{\mu}g/kg$ subcutaneously for each two-dogs group as follows: (1) every day for trial, (2) every other day for trial, (3) every third day for trial. The peripheral blood analysis including direct microscopic differential counts of one hundred cells was performed every day. Bone marrow aspiration was performed before administration of rh G-CSF, on the day of 0, 3, 9 and when the WBC counts were decreased within the normal range (day 12 or 13). Rh G-CSF was well-tolerated and showed no side effects in all dogs. According to the present study, $5{\mu}g/kg$ administration of rhG-CSF have cell-specific, frequency-related effect on bone marrow and peripheral blood. Furthermore, the effects of rhG-CSF administration on bone marrow sustained during the study and prolonged at least 3 days after discontinuing of rhG-CSF treatment.

• Biomolecules & Therapeutics
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• v.6 no.1
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• pp.89-94
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• 1998

CJ50001 is a recombinant human granulocyte colony-stimulating facto, (rHuG-CSF) that stimulates the formation of neutrophils from bone marrow stem cells. It was produced in E. colt and purified through refolding and several processes. We produced CS970125(300) using purified C150001 and additives in order to test the stability of CJ50001. When CS970125(300) was stored at 50'S for more than 1 week, high molecular weight proteins were formed and those proteins were detected by non-reducing SDS-PAGE, gel filtration HPLC, and Western blot. Those proteins showed single band at the same position of CJ50001 in reducing SDS-PAGE. These data indicated that those high molecular weight proteins were the multimers of C150001. In biological assays, iu viro and in viro, the multimers did not have biological activity and inhibitory action to that of CJ 50001. The mutimers did not induce toxicity in mice and rats in acute toxicity test. These results suggest that if Cs970125(300) containing CJ50001 is stored at 5$0^{\circ}C$, CJ50001 will be the multimers that do not have biological activity and inhibitory effect to CJ50001 and do not induce acute toxicity.

• Journal of Life Science
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• v.21 no.12
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• pp.1778-1783
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• 2011

Hematopoietic cytokines regulate production of blood cells by stimulating proliferation and differentiation of bone marrow cells. Among these hematopoietic cytokines, called hematopoitic growth factors, glranulocyte-colony stimulating Factor (G-CSF), which regulates growth of neutrophils, is one of important therapeutic factors because cancer patients suffer with neutropenia which is severe reduction of neutrophils after chemotherapy. Two groups of recombinant G-CSF have approved and used for therapeutic purposes and many researches are still on-going to produce recombinant G-CSF by different techniques. We engineered human G-CSF with Bombyx specific endoplasmic reticulum (ER) signal sequence, therefore, secretion of human G-CSF protein was improved in Bombyx mori-origined cell line, Bm5. The Bombyx ER signal sequence and human G-CSF matured protein region chimera was further remodeled at the N-terminus of matured G-CSF protein to understand roles of N-terminus on outer cellular secretion and/or production. Three different mutants were generated deleting three amino acids in non alpha-helical region in N-terminus in order to scan important amino acids for G-CSF secretion. One of 3 different N-terminal deletion mutants showed dramatically reduction of secreted amount of G-CSF indicating its important role on secretion. The data suggest that remodeling in non alpha-helical region of N-terminus is also important for recombinant G-CSF production.