Interleukin 3, granulocyte-macrophage colony-stimulating factor, and transfected erythropoietin receptors mediate tyrosine phosphorylation of a common cytosolic protein (pp100) in FDC-ER cells

Frederick W Quelle; Dawn E Quelle; Don M Wojchowski

doi:10.1016/S0021-9258(18)41891-1

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Interleukin 3, granulocyte-macrophage colony-stimulating factor, and transfected erythropoietin receptors mediate tyrosine phosphorylation of a common cytosolic protein (pp100) in FDC-ER cells

Journal article

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Peer reviewed

Interleukin 3, granulocyte-macrophage colony-stimulating factor, and transfected erythropoietin receptors mediate tyrosine phosphorylation of a common cytosolic protein (pp100) in FDC-ER cells

Frederick W Quelle, Dawn E Quelle and Don M Wojchowski

The Journal of biological chemistry, Vol.267(24), pp.17055-17060

08/25/1992

DOI: 10.1016/S0021-9258(18)41891-1

PMID: 1324920

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Abstract

Receptors for the hematopoietic growth factors erythropoietin, interleukin 3 (IL-3), and granulocyte-macrophage colony-stimulating factor (GM-CSF) are members of a structurally related receptor superfamily. Interestingly, while none of these receptors encode tyrosine kinase activities, induced tyrosine phosphorylation has been observed in various responsive cells stimulated with each factor. Toward defining possible common transduction pathways which are activated by these three cytokines, we have studied induced protein phosphorylation in murine myeloid FDC-P1 cells stably transfected with an erythropoietin receptor cDNA (FDC-ER cells). FDC-ER cells proliferate in response to erythropoietin (Quelle, D. E., and Wojchowski, D. M. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 4801-4805), and presently are shown to rapidly phosphorylate a M(r) 100,000 cytosolic protein (pp100) at tyrosine residues in response to this factor. Phosphorylation of pp100 also is induced in FDC-P1 and FDC-ER cells in response to IL-3 or GM-CSF. Importantly, quantitative analyses showed identical concentration dependencies for factor-induced pp100 phosphorylation and induced cell proliferation. Moreover, a selective loss of proliferative responsiveness to GM-CSF in FDC-ER cells was associated with a reduced capacity of GM-CSF to induce pp100 phosphorylation. Finally, limited differences in tryptic phosphopeptide maps of pp100 as isolated following exposure to erythropoietin, IL-3, or GM-CSF were observed, suggesting that these factors also may preferentially induce phosphorylation of pp100 at distinct sites. These findings are consistent with a role for pp100 as a common cytosolic transducer in the apparently convergent pathways of erythropoietin-, IL-3-, and GM-CSF-induced proliferation of myeloid progenitor cells.

Phosphorylation

Transfection

Erythropoietin - pharmacology

Molecular Weight

Protein-Tyrosine Kinases - metabolism

Phosphoproteins - metabolism

Interleukin-3 - pharmacology

Receptors, Granulocyte-Macrophage Colony-Stimulating Factor - drug effects

Peptide Mapping

Receptors, Cell Surface - drug effects

Vanadates - pharmacology

Cell Membrane - metabolism

Receptors, Cell Surface - physiology

Tyrosine

Cell Line

Granulocyte-Macrophage Colony-Stimulating Factor - pharmacology

Subcellular Fractions - metabolism

Cell Division - drug effects

Animals

Receptors, Granulocyte-Macrophage Colony-Stimulating Factor - physiology

Phosphoproteins - isolation & purification

Cytosol - metabolism

Receptors, Interleukin-3 - drug effects

Mice

Kinetics

Receptors, Erythropoietin

Phosphopeptides - isolation & purification

Receptors, Cell Surface - genetics

Receptors, Interleukin-3 - physiology

Details

Title: Subtitle: Interleukin 3, granulocyte-macrophage colony-stimulating factor, and transfected erythropoietin receptors mediate tyrosine phosphorylation of a common cytosolic protein (pp100) in FDC-ER cells
Creators: Frederick W Quelle - Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802
Dawn E Quelle
Don M Wojchowski
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.267(24), pp.17055-17060
DOI: 10.1016/S0021-9258(18)41891-1
PMID: 1324920
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: United States
Grant note: R29-DK40242 / NIDDK NIH HHS HL44491 / NHLBI NIH HHS
Language: English
Date published: 08/25/1992
Academic Unit: Pathology; Neuroscience and Pharmacology; Internal Medicine
Record Identifier: 9984040485402771

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