Cloning and sequencing of an alternative splicing-derived cDNA variant of the GM-CSF receptor alpha subunit, which encodes a truncated protein
✍ Scribed by Hu, Xiaotang; Zuckerman, Kenneth S.
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 79 KB
- Volume
- 58
- Category
- Article
- ISSN
- 0361-8609
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✦ Synopsis
GM-CSF interacts with the low affinity GM-CSF receptor ␣-subunit, which leads to high affinity association with the ␣-subunit/common -subunit complex and transduction of intracellular signals leading to proliferation, differentiation, and/or activation of hemopoietic cells, predominantly in the neutrophil and monocyte/macrophage lineages. Several alternative splicing-derived variants of the GM-CSF receptor ␣-subunit have been described previously by this and other laboratories. A newly discovered alternativesplicing derived variant was isolated from the peripheral blood mononuclear cells of a patient with juvenile myelomonocytic leukemia. This variant lacks 397 base pairs corresponding to exons 8-11 of the wild type GM-CSF receptor ␣-subunit cDNA and potentially encodes a 233 amino acid protein lacking a membrane-anchoring domain and creating the fourth known potential soluble isoform of the ␣-subunit of the GM-CSF receptor. Am.