Widespread differentiation stage-specific expression of the gene encoding phosphoprotein p19 (metablastin) in mammalian cells

U. K. Schubart, J. Xu, W. Fan, G. Cheng, Harris Goldstein, G. Alpini, D. A. Shafritz, J. A. Amat, M. Farooq, W. T. Norton, T. A. Owen, J. B. Lian, G. S. Stein

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Abstract

p19 is a highly conserved 19 kD cytosolic protein that undergoes phosphorylation in response to diverse extracellular factors in mammalian cells. Its expression is abundant in brain and testis and is developmentally regulated. To gain insights regarding its function, we analyzed the expression of p19 mRNA in a variety of cell types during induction of differentiation. Murine erythroleukemia cells showed a moderate increase followed by a marked decrease in the abundance of p19 mRNA during induction of differentiation. In murine C2 myoblasts and primary fetal rat osteoblasts, p19 mRNA was abundant in replicating cells and decreased to undetectable levels during differentiation. In resting human peripheral blood Iymphocytes, p19 mRNA was virtually undetectable but was strongly induced during blast transformation of both B and T cells. In rat liver, p19 mRNA was abundant on embryonic day 17 and decreased during early postnatal development. Upon fractionation of adult rat liver cells by centrifugal elutriation, p19 mRNA was not detected in hepatocytes while a low level was observed in a fraction enriched in non-parenchymal epithelial cells. CCl4-induced liver regeneration resulted in induction of p19 mRNA in hepatocytes. Primary cultures of embryonic and neonatal rat brain were analyzed by indirect immunofluorescence using co-staining with stage-specific markers. p19 expression was restricted to immature neurons and oligodendrocyte precursors. In contrast to the other cell types examined, the neuronal and glial precursors that express p19 were shown, using BrdU labeling, to be postmitotic both in primary culture and in vivo. The data demonstrate widespread, stage-specific expression of p19 and suggest that the protein exerts a general, lineage-independent function during induction of differentiation of mammalian cells. In view of the available evidence on the stimulation of serine phosphorylation of p19 by several growth factors, our working hypothesis is that phosphorylation of p19 may be involved in the mechanism by which growth factors control cell differentiation.

Original languageEnglish (US)
Pages (from-to)21-32
Number of pages12
JournalDifferentiation
Volume51
Issue number1
StatePublished - 1992

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Stathmin
Gene Expression
Messenger RNA
Phosphorylation
Cell Differentiation
Hepatocytes
Intercellular Signaling Peptides and Proteins
Leukemia, Erythroblastic, Acute
Liver Regeneration
Myoblasts
Liver
Oligodendroglia
Brain
Bromodeoxyuridine
Indirect Fluorescent Antibody Technique
Lymphocyte Activation
Osteoblasts
Neuroglia
Serine
Testis

ASJC Scopus subject areas

  • Cell Biology
  • Developmental Biology
  • Pathology and Forensic Medicine

Cite this

Widespread differentiation stage-specific expression of the gene encoding phosphoprotein p19 (metablastin) in mammalian cells. / Schubart, U. K.; Xu, J.; Fan, W.; Cheng, G.; Goldstein, Harris; Alpini, G.; Shafritz, D. A.; Amat, J. A.; Farooq, M.; Norton, W. T.; Owen, T. A.; Lian, J. B.; Stein, G. S.

In: Differentiation, Vol. 51, No. 1, 1992, p. 21-32.

Research output: Contribution to journalArticle

Schubart, UK, Xu, J, Fan, W, Cheng, G, Goldstein, H, Alpini, G, Shafritz, DA, Amat, JA, Farooq, M, Norton, WT, Owen, TA, Lian, JB & Stein, GS 1992, 'Widespread differentiation stage-specific expression of the gene encoding phosphoprotein p19 (metablastin) in mammalian cells', Differentiation, vol. 51, no. 1, pp. 21-32.
Schubart, U. K. ; Xu, J. ; Fan, W. ; Cheng, G. ; Goldstein, Harris ; Alpini, G. ; Shafritz, D. A. ; Amat, J. A. ; Farooq, M. ; Norton, W. T. ; Owen, T. A. ; Lian, J. B. ; Stein, G. S. / Widespread differentiation stage-specific expression of the gene encoding phosphoprotein p19 (metablastin) in mammalian cells. In: Differentiation. 1992 ; Vol. 51, No. 1. pp. 21-32.
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abstract = "p19 is a highly conserved 19 kD cytosolic protein that undergoes phosphorylation in response to diverse extracellular factors in mammalian cells. Its expression is abundant in brain and testis and is developmentally regulated. To gain insights regarding its function, we analyzed the expression of p19 mRNA in a variety of cell types during induction of differentiation. Murine erythroleukemia cells showed a moderate increase followed by a marked decrease in the abundance of p19 mRNA during induction of differentiation. In murine C2 myoblasts and primary fetal rat osteoblasts, p19 mRNA was abundant in replicating cells and decreased to undetectable levels during differentiation. In resting human peripheral blood Iymphocytes, p19 mRNA was virtually undetectable but was strongly induced during blast transformation of both B and T cells. In rat liver, p19 mRNA was abundant on embryonic day 17 and decreased during early postnatal development. Upon fractionation of adult rat liver cells by centrifugal elutriation, p19 mRNA was not detected in hepatocytes while a low level was observed in a fraction enriched in non-parenchymal epithelial cells. CCl4-induced liver regeneration resulted in induction of p19 mRNA in hepatocytes. Primary cultures of embryonic and neonatal rat brain were analyzed by indirect immunofluorescence using co-staining with stage-specific markers. p19 expression was restricted to immature neurons and oligodendrocyte precursors. In contrast to the other cell types examined, the neuronal and glial precursors that express p19 were shown, using BrdU labeling, to be postmitotic both in primary culture and in vivo. The data demonstrate widespread, stage-specific expression of p19 and suggest that the protein exerts a general, lineage-independent function during induction of differentiation of mammalian cells. In view of the available evidence on the stimulation of serine phosphorylation of p19 by several growth factors, our working hypothesis is that phosphorylation of p19 may be involved in the mechanism by which growth factors control cell differentiation.",
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AU - Schubart, U. K.

AU - Xu, J.

AU - Fan, W.

AU - Cheng, G.

AU - Goldstein, Harris

AU - Alpini, G.

AU - Shafritz, D. A.

AU - Amat, J. A.

AU - Farooq, M.

AU - Norton, W. T.

AU - Owen, T. A.

AU - Lian, J. B.

AU - Stein, G. S.

PY - 1992

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N2 - p19 is a highly conserved 19 kD cytosolic protein that undergoes phosphorylation in response to diverse extracellular factors in mammalian cells. Its expression is abundant in brain and testis and is developmentally regulated. To gain insights regarding its function, we analyzed the expression of p19 mRNA in a variety of cell types during induction of differentiation. Murine erythroleukemia cells showed a moderate increase followed by a marked decrease in the abundance of p19 mRNA during induction of differentiation. In murine C2 myoblasts and primary fetal rat osteoblasts, p19 mRNA was abundant in replicating cells and decreased to undetectable levels during differentiation. In resting human peripheral blood Iymphocytes, p19 mRNA was virtually undetectable but was strongly induced during blast transformation of both B and T cells. In rat liver, p19 mRNA was abundant on embryonic day 17 and decreased during early postnatal development. Upon fractionation of adult rat liver cells by centrifugal elutriation, p19 mRNA was not detected in hepatocytes while a low level was observed in a fraction enriched in non-parenchymal epithelial cells. CCl4-induced liver regeneration resulted in induction of p19 mRNA in hepatocytes. Primary cultures of embryonic and neonatal rat brain were analyzed by indirect immunofluorescence using co-staining with stage-specific markers. p19 expression was restricted to immature neurons and oligodendrocyte precursors. In contrast to the other cell types examined, the neuronal and glial precursors that express p19 were shown, using BrdU labeling, to be postmitotic both in primary culture and in vivo. The data demonstrate widespread, stage-specific expression of p19 and suggest that the protein exerts a general, lineage-independent function during induction of differentiation of mammalian cells. In view of the available evidence on the stimulation of serine phosphorylation of p19 by several growth factors, our working hypothesis is that phosphorylation of p19 may be involved in the mechanism by which growth factors control cell differentiation.

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