Abstract
We describe a novel cytoplasmic tyrosine kinase, termed BPK (B cell progenitor kinase), which is expressed in all stages of the B lineage and in myeloid cells. BPK has classic SH1, SH2, and SH3 domains, but lacks myristylation signals and a regulatory phosphorylation site corresponding to tyrosine 527 of c-src. BPK has a long, basic amino-terminal region upstream of the SH3 domain. BPK was evaluated as a candidate for human X-linked agammaglobulinemia (XLA), an inherited immunodeficiency characterized by a severe deficit of B and plasma cells and profound hypogammaglobulinemia. BPK mapped to within 100 kb of a probe defining the polymorphism most closely linked to XLA at DXS178. Reduction in or the absence of BPK mRNA, protein expression, and kinase activity was observed in XLA pre-B and B cell lines. BPK is likely the XLA gene and functions in pathways critical to B cell expansion.
Lingua originale | English |
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pagine (da-a) | 279-290 |
Numero di pagine | 12 |
Rivista | Cell |
Volume | 72 |
DOI | |
Stato di pubblicazione | Pubblicato - 1993 |
Keywords
- Agammaglobulinemia
- Amino Acid Sequence
- Animals
- B-Lymphocytes
- Blotting, Northern
- Blotting, Southern
- Cell Line
- Chromosome Mapping
- Cloning, Molecular
- Cosmids
- Cytoplasm
- DNA
- Heterozygote Detection
- Humans
- Hybrid Cells
- Mice
- Molecular Sequence Data
- Protein-Tyrosine Kinases
- RNA, Messenger
- Sequence Homology, Amino Acid
- Transcription, Genetic
- Tumor Cells, Cultured
- X Chromosome