| Project/Area Number |
04807016
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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 |
General medical chemistry
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| Research Institution | Shimane Medical University |
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Principal Investigator |
SHIMOYAMA Makoto Shimane Med. Univ., Dept. of Biochem., Prof., 医学部, 教授 (30084859)
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| Co-Investigator(Kenkyū-buntansha) |
YAMADA Kazuo Shimane Med. Univ., Dept. of Biochem., Instructor, 医学部, 助手 (30240005)
TERASHIMA Masaharu Shimane Med. Univ., Dept. of Biochem., Instructor, 医学部, 助手 (40227517)
TSUCHIYA Mikako Shimane Med. Univ., Dept. of Biochem., Associate Prof., 医学部, 助教授 (90188582)
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| Project Period (FY) |
1992 – 1993
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| Project Status |
Completed (Fiscal Year 1993)
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| Budget Amount *help |
¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 1993: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1992: ¥1,300,000 (Direct Cost: ¥1,300,000)
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| Keywords | p33 / mim-1 / ADP-ribosylation / leukocyte / myeloid leukemia / post-translational modification |
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| Research Abstract |
Arginine-specific ADP-ribosyltransferase catalyzes transfer of the ADP-ribose moiety from NAD to arginine residue(s) of target proteins. We observed the transferase and its target protein p33 in chicken bone-marrow cells and polymorphonuclear cells. Analysis of the amino acid sequence of p33 revealed that the protein was completely identical with the regions of the sequence deduced from mim-1 (myb-induced myeloid protein-1). The levels of p33 in bone-marrow celle from 6-week-old chiken were much higher than those of peripheral polymorphonuclear cells from the same chiken. The bone-marrow cells were cultured in CO_2 at 37ﾟC in growth medium containing 8% fetal calf serum and 2% heat-inactivated chiken serum. p33 and the transferase were detected in non-adherent cell fraction containing promyelocytes and polymorphonuclear cells but not in adherent cell fraction not containing those cells. These results indicate that p33 and the transferase may participate in the differentiation of bone-marrow cells to granulocytes. Auto-ADP-ribosylation of the transferase purified from chiken peripheral polymorphonuclear cells was investigated. The ADP-ribose-transferase linkage was labile in 0.5 M hydoroxylamine. The auto-ADP-ribosylated transferase showed higher activity than did the unmodified transferase in catalyzing ADP-ribosylation of the basic acceptor such as poly (L-arginine) and p33 while to ADP-ribosylate the acidic proteins such as casein, the modified transferase was less active. Thus, auto-modification of the transferase apparently alters the specificity of its own substrate.
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