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STAT 1α/1β, STAT 3 and STAT 5: Expression and Association with c-MET and EGF-Receptor in Long-Term Cultures of Human Hepatocytes
- Source :
- Biochemical and Biophysical Research Communications. 265:376-381
- Publication Year :
- 1999
- Publisher :
- Elsevier BV, 1999.
-
Abstract
- Long-term cultures of human hepatocytes were maintained serum-free in a chemically defined medium in the presence of HGF and EGF for up to 30 days. STAT 1alpha/1beta, STAT 3, and STAT 5 were present and tyrosine phosphorylated throughout the culture period in the cytosol as well as the nucleus. We show by co-immunoprecipitation that a portion of the cellular pools of STAT 1alpha/1beta and STAT 5 is physically associated with c-MET and EGF-receptor. Co-immunoprecipitation of STAT 3 with STAT 5 did occur in the cytosol but not in the nucleus, suggesting dimerization of the two STAT family members. The observed differences of protein amounts and tyrosine phosphorylation between cytosol and nucleus, the association of STAT proteins with EGF-receptor and c-MET and with each other may all be involved in regulating the activity of the STAT transcription factors. It is intriguing to speculate that STAT 5 may have a modulating role in the regulation of STAT 3 activity.
- Subjects :
- STAT3 Transcription Factor
Biophysics
Biology
Biochemistry
Culture Media, Serum-Free
stat
Mice
chemistry.chemical_compound
Cytosol
STAT5 Transcription Factor
Animals
Humans
Protein inhibitor of activated STAT
SOCS3
Phosphorylation
Tyrosine
Molecular Biology
STAT4
Cells, Cultured
Cell Nucleus
Tyrosine phosphorylation
Cell Biology
Proto-Oncogene Proteins c-met
Milk Proteins
Molecular biology
DNA-Binding Proteins
ErbB Receptors
STAT1 Transcription Factor
Liver
chemistry
Trans-Activators
STAT protein
Cattle
Rabbits
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 265
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....59dfcbdb53dfbccd47a52402edec6af1