ArticleProceedings of the National Academy of Sciences of the United States of America1994
Activation of JAK2 tyrosine kinase by prolactin receptors in Nb2 cells and mouse mammary gland explants.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 226 citations in OpenAlex.
- Multiple Endocrine Disruption by the MET/ALK Inhibitor Crizotinib in Patients With Non-small Cell Lung Cancer.American journal of clinical oncology · 2015Trial
- Irisin modulates the transcriptomic profile of porcine anterior pituitary cells isolated from gilts on days 15-16 of pregnancy.Scientific reports · 2026Article
- Article
- The brain as a source and a target of prolactin in mammals.Neural regeneration research · 2022Review
- Prolactin and its significance in the placenta.Hormones (Athens, Greece) · 2022Review
- Secretion and Function of Pituitary Prolactin in Evolutionary Perspective.Frontiers in neuroscience · 2020Review
- Advances in Nutritional Epigenetics-A Fresh Perspective for an Old Idea. Lessons Learned, Limitations, and Future Directions.Epigenetics insights · 2020Article
- Growth hormone (GH) receptor (GHR)-specific inhibition of GH-Induced signaling by soluble IGF-1 receptor (sol IGF-1R).Molecular and cellular endocrinology · 2019Article
- Subdomain 2, Not the Transmembrane Domain, Determines the Dimerization Partner of Growth Hormone Receptor and Prolactin Receptor.Endocrinology · 2017Article
- Jak2-Stat5a/b Signaling Induces Epithelial-to-Mesenchymal Transition and Stem-Like Cell Properties in Prostate Cancer.The American journal of pathology · 2015Article
- Tyrosyl phosphorylated serine-threonine kinase PAK1 is a novel regulator of prolactin-dependent breast cancer cell motility and invasion.Advances in experimental medicine and biology · 2015Review
- c-Abl activates janus kinase 2 in normal hematopoietic cells.The Journal of biological chemistry · 2014Article
- Tyrosyl phosphorylated PAK1 regulates breast cancer cell motility in response to prolactin through filamin A.Molecular endocrinology (Baltimore, Md.) · 2013Article
- The role of prolactin receptor in GH signaling in breast cancer cells.Molecular endocrinology (Baltimore, Md.) · 2013Article
- Autocrine prolactin: an emerging market for homegrown (prolactin) despite the imports.Genes & development · 2012Article
- Molecular mechanisms of prolactin and its receptor.Endocrine reviews · 2012Review
- Adapter protein SH2B1beta binds filamin A to regulate prolactin-dependent cytoskeletal reorganization and cell motility.Molecular endocrinology (Baltimore, Md.) · 2011Article
- Differential biological activity of disease-associated JAK2 mutants.FEBS letters · 2011Article
- Growth hormone signaling in human T47D breast cancer cells: potential role for a growth hormone receptor-prolactin receptor complex.Molecular endocrinology (Baltimore, Md.) · 2011Article
- Adapter protein SH2B1beta cross-links actin filaments and regulates actin cytoskeleton.Molecular endocrinology (Baltimore, Md.) · 2009Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
One of the earliest cellular responses to prolactin (PRL) binding in Nb2 cells, a rat pre-T lymphoma cell line, is an increase in tyrosine phosphorylation of cellular proteins. In this work, immunologic techniques have been used to demonstrate that in Nb2 cells and in mouse mammary gland explants, JAK2, a non-receptor tyrosine kinase, is activated following stimulation with PRL. PRL stimulated tyrosine phosphorylation of JAK2 at times as early as 30 sec and concentrations of PRL as low as 0.5 ng/ml (2.5 pM) in Nb2 cells and 100 ng/ml (5 nM) in mammary gland explants. When JAK2 was immunoprecipitated from solubilized Nb2 cells or mammary gland explants and incubated with [gamma-32P]ATP, 32P was incorporated into a protein migrating with an apparent molecular weight appropriate for JAK2 only when cells had been incubated with PRL, indicating that JAK2 tyrosine kinase activity is exquisitely sensitive to PRL. In Nb2 cells, JAK2 was found to associate with PRL receptor irrespective of whether or not the cells had been incubated with PRL. These results provide strong evidence that JAK2 is constitutively associated with the PRL receptor and that it is activated and tyrosine phosphorylated upon PRL binding to the PRL receptor. These results are consistent with JAK2 serving as an early, perhaps initial, signaling molecule for PRL.
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