Protein tyrosine phosphatase-1C is rapidly phosphorylated in tyrosine in macrophages in response to colony stimulating factor-1

Yee Guide Yeung, Karen L. Berg, Fiona J. Pixley, Ruth Hogue Angeletti, E. Richard Stanley

Research output: Contribution to journalArticle

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Abstract

An ∼64-kDa cytoplasmic protein is rapidly phosphorylated in tyrosine in the response of macrophages to colony stimulating factor-1. To identify this protein, BAC1.2F5 macrophages were incubated with or without colony stimulating factor-1, the phosphotyrosine-containing portion of their cytosolic fractions subjected to size exclusion chromatography, and the 45-70-kDa fraction further fractionated by reverse phase high pressure liquid chromatography (RP-HPLC). Tryptic peptides of pooled RP-HPLC fractions from stimulated cells (containing the ∼64-kDa protein and an ∼54-kDa protein) and from unstimulated cells (containing the ∼54-kDa protein alone), were sequenced directly. All seven readable sequences of 8 sequenceable peptides present uniquely in the stimulated fraction were present in the sequence of the src homology 2 domain-containing protein tyrosine phosphatase-1C (PTP-1C). The identity of the ∼64-kDa protein was confirmed by Western blotting with an antibody raised to a PTP-1C peptide. The rapid, growth factor-induced tyrosine phosphorylation of PTP-1C suggests that it may be involved in very early events in growth factor signal transduction.

Original languageEnglish (US)
Pages (from-to)23447-23450
Number of pages4
JournalJournal of Biological Chemistry
Volume267
Issue number33
StatePublished - Nov 25 1992

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Non-Receptor Type 6 Protein Tyrosine Phosphatase
Macrophage Colony-Stimulating Factor
Macrophages
Tyrosine
High pressure liquid chromatography
Proteins
Reverse-Phase Chromatography
Peptides
Intercellular Signaling Peptides and Proteins
SH2 Domain-Containing Protein Tyrosine Phosphatases
High Pressure Liquid Chromatography
Signal transduction
Phosphotyrosine
Phosphorylation
Size exclusion chromatography
Sequence Homology
Gel Chromatography
Signal Transduction
Western Blotting
Antibodies

ASJC Scopus subject areas

  • Biochemistry

Cite this

Yeung, Y. G., Berg, K. L., Pixley, F. J., Angeletti, R. H., & Stanley, E. R. (1992). Protein tyrosine phosphatase-1C is rapidly phosphorylated in tyrosine in macrophages in response to colony stimulating factor-1. Journal of Biological Chemistry, 267(33), 23447-23450.

Protein tyrosine phosphatase-1C is rapidly phosphorylated in tyrosine in macrophages in response to colony stimulating factor-1. / Yeung, Yee Guide; Berg, Karen L.; Pixley, Fiona J.; Angeletti, Ruth Hogue; Stanley, E. Richard.

In: Journal of Biological Chemistry, Vol. 267, No. 33, 25.11.1992, p. 23447-23450.

Research output: Contribution to journalArticle

Yeung, YG, Berg, KL, Pixley, FJ, Angeletti, RH & Stanley, ER 1992, 'Protein tyrosine phosphatase-1C is rapidly phosphorylated in tyrosine in macrophages in response to colony stimulating factor-1', Journal of Biological Chemistry, vol. 267, no. 33, pp. 23447-23450.
Yeung, Yee Guide ; Berg, Karen L. ; Pixley, Fiona J. ; Angeletti, Ruth Hogue ; Stanley, E. Richard. / Protein tyrosine phosphatase-1C is rapidly phosphorylated in tyrosine in macrophages in response to colony stimulating factor-1. In: Journal of Biological Chemistry. 1992 ; Vol. 267, No. 33. pp. 23447-23450.
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AU - Stanley, E. Richard

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N2 - An ∼64-kDa cytoplasmic protein is rapidly phosphorylated in tyrosine in the response of macrophages to colony stimulating factor-1. To identify this protein, BAC1.2F5 macrophages were incubated with or without colony stimulating factor-1, the phosphotyrosine-containing portion of their cytosolic fractions subjected to size exclusion chromatography, and the 45-70-kDa fraction further fractionated by reverse phase high pressure liquid chromatography (RP-HPLC). Tryptic peptides of pooled RP-HPLC fractions from stimulated cells (containing the ∼64-kDa protein and an ∼54-kDa protein) and from unstimulated cells (containing the ∼54-kDa protein alone), were sequenced directly. All seven readable sequences of 8 sequenceable peptides present uniquely in the stimulated fraction were present in the sequence of the src homology 2 domain-containing protein tyrosine phosphatase-1C (PTP-1C). The identity of the ∼64-kDa protein was confirmed by Western blotting with an antibody raised to a PTP-1C peptide. The rapid, growth factor-induced tyrosine phosphorylation of PTP-1C suggests that it may be involved in very early events in growth factor signal transduction.

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