Abstract
Interleukin 3 (IL-3) regulates the proliferation and differentiation of hematopoietic cells. Although the IL-3 receptor chains lack kinase catalytic domains, IL-3 induces tyrosine phosphorylation of cellular proteins. To investigate the potential role of the JAK family of protein-tyrosine kinases in IL-3 signal transduction, we have obtained full-length cDNA clones for murine Jak1 and Jak2 protein-tyrosine kinases and prepared antiserum against the predicted proteins. Using antisera against Jak2, we demonstrate that IL-3 stimulation results in the rapid and specific tyrosine phosphorylation of Jak2 and activates its in vitro kinase activity.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Bone Marrow / enzymology
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Cell Line
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Cells, Cultured
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Cloning, Molecular
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DNA / genetics
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DNA / metabolism
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Interleukin-3 / pharmacology*
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Janus Kinase 2
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Mice
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Molecular Sequence Data
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Monocytes / enzymology
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Oligodeoxyribonucleotides
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Polymerase Chain Reaction / methods
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Protein Biosynthesis
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Protein-Tyrosine Kinases / genetics
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Protein-Tyrosine Kinases / isolation & purification
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Protein-Tyrosine Kinases / metabolism*
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Proto-Oncogene Proteins*
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RNA, Messenger / isolation & purification
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RNA, Messenger / metabolism
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Signal Transduction / drug effects
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Signal Transduction / physiology*
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Transcription, Genetic
Substances
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Interleukin-3
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Oligodeoxyribonucleotides
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Proto-Oncogene Proteins
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RNA, Messenger
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DNA
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Protein-Tyrosine Kinases
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Jak2 protein, mouse
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Janus Kinase 2