Abstract
The ornithine decarboxylase inhibitor DL-α-difluoromethyl ornithine inhibited a proliferation-associated increase in ornithine decarboxylase activity in cultured human promyelocytic leukemia cells, resulting in a marked suppression of cell proliferation and subsequent cell loss. It also inhibited increases in ornithine decarboxylase activity associated with the phorbol ester-induced conversion of promyelocytic HL-60 cells to monocyte-like cells and the retinoic acid-induced conversion to granulocyte-like cells. However, the inhibition of ornithine decarboxylase activity did not prevent cellular differentiation. These results suggest that polyamine biosynthesis has a specific role in cell proliferation rather than in inducing differentiation that is not accompanied by proliferation. The data also demonstrate that cessation of proliferation in HL-60 cells is not necessarily associated with differentiation.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 75-77 |
| Number of pages | 3 |
| Journal | Science |
| Volume | 216 |
| Issue number | 4541 |
| State | Published - 1982 |
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Cite this
Ornithine decarboxylase : Essential in proliferation but not differentiation of human promyelocytic leukemia cells. / Luk, Gordon D.; Civin, Curt I.; Weissman, Robert M.; Baylin, Stephen B.
In: Science, Vol. 216, No. 4541, 1982, p. 75-77.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ornithine decarboxylase
T2 - Essential in proliferation but not differentiation of human promyelocytic leukemia cells
AU - Luk, Gordon D.
AU - Civin, Curt I.
AU - Weissman, Robert M.
AU - Baylin, Stephen B
PY - 1982
Y1 - 1982
N2 - The ornithine decarboxylase inhibitor DL-α-difluoromethyl ornithine inhibited a proliferation-associated increase in ornithine decarboxylase activity in cultured human promyelocytic leukemia cells, resulting in a marked suppression of cell proliferation and subsequent cell loss. It also inhibited increases in ornithine decarboxylase activity associated with the phorbol ester-induced conversion of promyelocytic HL-60 cells to monocyte-like cells and the retinoic acid-induced conversion to granulocyte-like cells. However, the inhibition of ornithine decarboxylase activity did not prevent cellular differentiation. These results suggest that polyamine biosynthesis has a specific role in cell proliferation rather than in inducing differentiation that is not accompanied by proliferation. The data also demonstrate that cessation of proliferation in HL-60 cells is not necessarily associated with differentiation.
AB - The ornithine decarboxylase inhibitor DL-α-difluoromethyl ornithine inhibited a proliferation-associated increase in ornithine decarboxylase activity in cultured human promyelocytic leukemia cells, resulting in a marked suppression of cell proliferation and subsequent cell loss. It also inhibited increases in ornithine decarboxylase activity associated with the phorbol ester-induced conversion of promyelocytic HL-60 cells to monocyte-like cells and the retinoic acid-induced conversion to granulocyte-like cells. However, the inhibition of ornithine decarboxylase activity did not prevent cellular differentiation. These results suggest that polyamine biosynthesis has a specific role in cell proliferation rather than in inducing differentiation that is not accompanied by proliferation. The data also demonstrate that cessation of proliferation in HL-60 cells is not necessarily associated with differentiation.
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UR - http://www.scopus.com/inward/citedby.url?scp=0020032293&partnerID=8YFLogxK
M3 - Article
VL - 216
SP - 75
EP - 77
JO - Science
JF - Science
SN - 0036-8075
IS - 4541
ER -