1989 Fiscal Year Final Research Report Summary
PURIFICATION AND STRUCTURE ANALYSIS OF PEPTIDES ASSOCIATED WITH THE REGULATION OF ERYTHROID DIFFERENTIATION
| Project/Area Number |
63570583
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Hematology
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| Research Institution | CLINICAL RESEARCH INSTITUTE, NATIONAL MEDICAL CENTER |
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Principal Investigator |
KANEDA Tsuguhiro CLINICAL RESEARCH INSTITUTE, NATIONAL MEDICAL CENTER, SENIOR RESEARCHER, 臨床研究部(国立名古屋病院併任), 主任研究員 (60183274)
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| Co-Investigator(Kenkyū-buntansha) |
HOTTA Tomomitsu NAGOYA UNIVERSITY SCHOOL OF MEDICINE, FIRST DEPARTMENT OF INTERNAL MEDICINE, ASS, 医学部・第一内科, 助手 (70173606)
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| Project Period (FY) |
1988 – 1990
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| Keywords | erythroid differentiation / differentiation inhibitory activity / growth inhibitory activity / peptides / fetal calf serum |
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| Research Abstract |
We found the supperssive activity on the colony formation of erythroid burst and colony forming units (BFU-E and CFU-E) of human bone marrow cells. The activity also inhibited the spontaneous and hexamethylene bisacetamide mediated induction of erythroid differentiation of mouse erythroleukemia cells (MELC). As the activity did not inhibit the colony formation of granutocyte-macrophage colony forming unit, the existence of lineage-specific negative regulator of erythroid differentiation was expected in the activity. In this study, we aimed the purification of the factor. The activity passed through DEAE-cellulose, but it bound to phosphcellulose. Subsequently, it was easily separated from abundant serum proteins. The characteristic of the activity obtained was inhibitory activity of MELC growth. The activity was sequentially purified with Sephadex G-25, DEAE-cellulose and QAE Sephadex A-25 chromatography. The specific activity increased to 1500-fold. The HPLC-analysis with mu Bondasphere C18 revealed that the activity was associated with several peptides with low molecular weight. The partially purified fraction (QAE Sephadex-fraction) exhibited the growth arrest in high concentration, on the other hands, it elongated the doubling time of MELC. Further purification of the activity is needed to determine the structure of the peptides. The possibility that the suppression of erythroid colony formation previously found was resulted in the synergistic effects by several peptides in FCS was not excluded by the present study.
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