The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-Kd tyrosine phosphorylated protein
Abstract
Although the erythropoietin receptor (EpR) lacks a tyrosine kinase consensus sequence within its proline-rich intracellular domain, addition of its ligand to Ep-responsive cells stimulates the rapid and transient tyrosine phosphorylation of a number of cellular proteins. The characterization of these phosphorylatable substrates, which include 5 major phosphoproteins with molecular masses of approximately 145, 130, 97, 72, and 56 Kd is an essential step in understanding the signal transduction pathways used by Ep. Recently, we and others have shown that the major 72-Kd tyrosine phosphorylated protein is the EpR itself. We now report, using both murine DA-3 and human MO7E cell lines engineered to express high levels of biologically responsive EpRs (and designated DA-ER and MO7-ER, respectively), that the major 56-Kd tyrosine phosphorylated protein is the recently identified SH2-containing protein, p52shc. Interestingly, in Ep-stimulated cells, anti-Shc antibodies coprecipitate the major 145-Kd tyrosine phosphorylated protein in both DA-ER and MO7-ER cells. Tyrosine phosphorylation of both proteins is detectable within 30 seconds of incubation with Ep at 37 degrees C, reaches a maximum between 2 and 5 minutes, and declines by 30 minutes. In addition, tyrosine phosphorylated Shc appears capable of associating with the activated EpR, but this could only be shown in MO7-ER cells. Lastly, as has been shown previously with the tyrosine kinase containing receptors for epidermal growth…
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“SHIP1 was originally observed in hematopoietic cells after a variety of cytokines and growth factors induced the tyrosine phosphorylation of this 145-kDa protein [98–104].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [101]
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Metadata
- Authors
- Damen, J., Liu, L., Cutler, R., & Krystal, G.
- Affiliations
- Terry Fox Laboratory, B.C. Cancer Agency, Vancouver, Canada.
- BC Cancer Agency (CA)
- ORCID
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 1993-10-15
- Volume
- 82
- Issue
- 8
- Pages
- 2296-2303
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W50290146
- Cited by
- 193
- References
- 36
- Citations by year
- 2026: 1 · 2023: 3 · 2022: 1 · 2018: 1 · 2017: 2 · 2012: 4
- FWCI
- 13.78
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Blood (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
- Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- erythropoietin, erythropoietin receptor, Shc, Grb2, tyrosine phosphorylation, signal transduction, Ras activation, receptor tyrosine kinase, MO7e cells
- MeSH terms
- Src Homology 2 Domain-Containing, Transforming Protein 1, Animals, Cell Line, Erythropoietin, Cricetinae, Humans, Molecular Weight, Phosphoproteins, Phosphorylation, Proteins, Tyrosine, Oncogene Proteins, Receptors, Erythropoietin, Adaptor Proteins, Vesicular Transport, Adaptor Proteins, Signal Transducing, Mice, Shc Signaling Adaptor Proteins
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