Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-7-13
pubmed:abstractText
We have investigated the interaction of the SH2-containing protein tyrosine phosphatase-1 (SHP-1) and Jak2 in an erythropoietin (Epo)-dependent human leukemia cell line, UT-7/Epo, using reciprocal immunoprecipitation and immunoblotting. The Epo-induced kinetics and dose response on phosphorylated Jak2 in anti-SHP-1 precipitates of UT-7/Epo cell lysates were similar to those in direct anti-Jak2 precipitates, suggesting that Jak2 coprecipitated with SHP-1. Furthermore, immunoblotting with anti-Jak2 and anti-SHP-1 antibodies indicated that SHP-1 appeared to be constitutively associated with non-tyrosine-phosphorylated Jak2 in UT-7/Epo cells in the absence of Epo and without phosphorylation of the Epo receptor (EpoR). Competition studies with C-terminal SHP-1 and Jak2 peptides decreased the amounts of SHP-1 and Jak2 detected in immunoprecipitates supporting the specific coprecipitation of SHP-1 and Jak2. In the presence of a recombinant GST-fusion protein containing both the N-terminal and C-terminal SH2 domains of SHP-1, anti-GST precipitated the fusion protein but not cellular Jak2. These studies suggest that SHP-1 and Jak2 are constitutively associated in UT-7/EPO cells. The association is not dependent upon Epo and is not mediated via SHP-1 SH2 binding. Sequential double immunoprecipitation demonstrated that only a small portion of intracellular Jak2 and SHP-1 molecules are constitutively associated. This partial association pattern may allow a more flexible and diverse regulation of Jak2 and SHP-1 activities. Whether Jak2 and SHP-1 are directly associated with each other or are part of a larger complex needs further investigation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, http://linkedlifedata.com/resource/pubmed/chemical/Erythropoietin, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/JAK2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Janus Kinase 2, http://linkedlifedata.com/resource/pubmed/chemical/PTPN11 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/PTPN6 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1, http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase..., http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase..., http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Erythropoietin, http://linkedlifedata.com/resource/pubmed/chemical/SH2 Domain-Containing Protein...
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1079-9796
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15-24
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10772872-Antibodies, pubmed-meshheading:10772872-Binding, Competitive, pubmed-meshheading:10772872-Dose-Response Relationship, Drug, pubmed-meshheading:10772872-Erythropoietin, pubmed-meshheading:10772872-Humans, pubmed-meshheading:10772872-Immunoblotting, pubmed-meshheading:10772872-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:10772872-Janus Kinase 2, pubmed-meshheading:10772872-Kinetics, pubmed-meshheading:10772872-Peptides, pubmed-meshheading:10772872-Phosphorylation, pubmed-meshheading:10772872-Precipitin Tests, pubmed-meshheading:10772872-Protein Binding, pubmed-meshheading:10772872-Protein Phosphatase 1, pubmed-meshheading:10772872-Protein Tyrosine Phosphatase, Non-Receptor Type 11, pubmed-meshheading:10772872-Protein Tyrosine Phosphatase, Non-Receptor Type 6, pubmed-meshheading:10772872-Protein Tyrosine Phosphatases, pubmed-meshheading:10772872-Protein-Tyrosine Kinases, pubmed-meshheading:10772872-Proto-Oncogene Proteins, pubmed-meshheading:10772872-Receptors, Erythropoietin, pubmed-meshheading:10772872-SH2 Domain-Containing Protein Tyrosine Phosphatases, pubmed-meshheading:10772872-Signal Transduction, pubmed-meshheading:10772872-Tumor Cells, Cultured, pubmed-meshheading:10772872-src Homology Domains
pubmed:year
2000
pubmed:articleTitle
SH2-Containing protein tyrosine phosphatase-1 (SHP-1) association with Jak2 in UT-7/Epo cells.
pubmed:affiliation
Department of Molecular Virology and Host Defense, SmithKline Beecham Pharmaceuticals, Collegeville, Pennsylvania, USA.
pubmed:publicationType
Journal Article