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. 2002 Apr 12;1574(3):383-6.
doi: 10.1016/s0167-4781(01)00357-8.

Identification and characterization of an isoform of murine Mpl

Diana F Sabath  1 , Cathy Lofton-Day, Nancy Lin, Si Lok, Kenneth Kaushansky, Virginia C Broudy
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Identification and characterization of an isoform of murine Mpl

Diana F Sabath et al. Biochim Biophys Acta. .

Abstract

A new isoform of the full-length murine thrombopoietin (Tpo) receptor was isolated from a murine spleen cDNA library. This isoform, c-mpl-II, differs from full-length c-mpl (c-mpl-I) by virtue of deletion of 180 nucleotides that encode 60 amino acids located in the extracellular domain of Mpl. Normal murine megakaryocytes were found to express both c-mpl-I and c-mpl-II transcripts. BaF3 cells transfected with c-mpl-I expressed a 95 kDa protein that was displayed on the cell surface and bound 125I-Tpo. BaF3 cells transfected with c-mpl-II expressed a 70 kDa protein. However, these cells were not able to bind 125I-Tpo and surface display of Mpl-II could not be detected. In summary, c-mpl-II is an isoform of murine Mpl expressed by megakaryocytes that lacks a 60 amino acid region required for surface expression of the protein.

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