A1 Refereed original research article in a scientific journal
Developmental expression of Pim kinases suggests functions also outside of the hematopoietic system
Authors: Eichmann A, Yuan L, Breant C, Alitalo K, Koskinen PJ
Publisher: STOCKTON PRESS
Publication year: 2000
Journal: Oncogene
Journal name in source: ONCOGENE
Journal acronym: ONCOGENE
Volume: 19
Issue: 9
First page : 1215
Last page: 1224
Number of pages: 10
ISSN: 0950-9232
DOI: https://doi.org/10.1038/sj.onc.1203355
Abstract
We have cloned a novel quail cDNA with strong homology to the pint family of proto-oncogenes. The deduced amino acid (aa) sequence of the cDNA, named qpim, is more closely related to Xenopus Pim and to the recently identified rat Pim-3 than to human or rodent Pim-1 or Pim-2. The protein encoded by the qpim cDNA can autophosphorylate itself and share substrates with murine Pim-l, suggesting functional redundancy to other Pim family serine/threonine kinases. We have compared the expression of qpim in avian embryos to mouse pim-1, -2 and -3 by in situ hybridization. qpim shows a highly dynamic expression pattern, particularly at early developmental stages. Surprisingly, its expression pattern is not identical to any of the murine pint genes, which show complementary and/or partially overlapping expression sites both in- and outside of the hematopoietic system. Altogether, our results suggest novel functions for Pim family kinases during embryonic development, in particular in epithelia and in the central nervous system.
We have cloned a novel quail cDNA with strong homology to the pint family of proto-oncogenes. The deduced amino acid (aa) sequence of the cDNA, named qpim, is more closely related to Xenopus Pim and to the recently identified rat Pim-3 than to human or rodent Pim-1 or Pim-2. The protein encoded by the qpim cDNA can autophosphorylate itself and share substrates with murine Pim-l, suggesting functional redundancy to other Pim family serine/threonine kinases. We have compared the expression of qpim in avian embryos to mouse pim-1, -2 and -3 by in situ hybridization. qpim shows a highly dynamic expression pattern, particularly at early developmental stages. Surprisingly, its expression pattern is not identical to any of the murine pint genes, which show complementary and/or partially overlapping expression sites both in- and outside of the hematopoietic system. Altogether, our results suggest novel functions for Pim family kinases during embryonic development, in particular in epithelia and in the central nervous system.
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