|
|
 Previous Article | Table of Contents | Next Article 
Prothymosin alpha gene expression correlates with proliferation, not
differentiation, of HL-60 cells
MR Smith, A al-Katib, R Mohammad, A Silverman, P Szabo, S Khilnani, W Kohler, R Nath and MG Mutchnick
Department of Medicine, Wayne State University School of Medicine, Detroit,
MI 48201-1998.
Accumulating evidence suggests that prothymosin alpha has an as yet
undefined intracellular, perhaps intranuclear, function related to cell
proliferation. Prothymosin alpha mRNA and/or peptide levels increase when
cells are stimulated to proliferate. Because proliferation and
differentiation events are often inversely correlated, we examined
prothymosin alpha gene expression during proliferation and differentiation
of HL-60 myeloid leukemia cells. Steady-state levels of prothymosin alpha
mRNA, which are high in exponentially growing HL-60, decrease within hours
after induction of HL-60 to differentiate along the neutrophil pathway with
dimethylsulfoxide (DMSO) or along the macrophage lineage with either
tetradecanoylphorbol acetate (TPA) or bryostatin 1. The decline in
prothymosin alpha mRNA in response to these differentiation signals
parallels that of c-myc mRNA under the same conditions. We then determined
whether the downregulation of prothymosin alpha and c-myc mRNA were due to
differentiation or cessation or proliferation. Recombinant human
gamma-interferon induces monocytic differentiation of HL-60, but permits
continued proliferation, and, under these conditions, expression of
prothymosin alpha, as well as of c-myc, mRNA remains elevated. We conclude
that prothymosin alpha and c-myc expression are coregulated in
differentiating HL-60 and that their expression correlates with the
proliferative state of HL-60 cells, rather than with the differentiated
state.
Volume 82,
Issue 4,
pp. 1127-1132,
08/15/1993
Copyright © 1993 by The American Society of Hematology
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
J. S. Knight, K. Lan, C. Subramanian, and E. S. Robertson
Epstein-Barr Virus Nuclear Antigen 3C Recruits Histone Deacetylase Activity and Associates with the Corepressors mSin3A and NCoR in Human B-Cell Lines
J. Virol.,
April 1, 2003;
77(7):
4261 - 4272.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
X. Jiang, H.-E. Kim, H. Shu, Y. Zhao, H. Zhang, J. Kofron, J. Donnelly, D. Burns, S.-c. Ng, S. Rosenberg, et al.
Distinctive Roles of PHAP Proteins and Prothymosin-alpha in a Death Regulatory Pathway
Science,
January 10, 2003;
299(5604):
223 - 226.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. A. Enkemann, K. S. Pavur, A. G. Ryazanov, and S. L. Berger
Does Prothymosin alpha Affect the Phosphorylation of Elongation Factor 2?
J. Biol. Chem.,
June 25, 1999;
274(26):
18644 - 18650.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. S. Orre, M. A. Cotter II, C. Subramanian, and E. S. Robertson
Prothymosin alpha Functions as a Cellular Oncoprotein by Inducing Transformation of Rodent Fibroblasts in Vitro
J. Biol. Chem.,
January 12, 2001;
276(3):
1794 - 1799.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
