Pten Modulates Gdnf/Ret Mediated Chemotaxis and Branching Morphogenesis in the Developing Kidney.
From: Department of Pathology, University of Michigan, MSRB1, BSRB 2049, 109 Zina Pitcher Dr., Ann Arbor, MI 48109, USA.
Developmental biology
- Publish Date: Jul 2007
- ISSN: 0012-1606
- Volume: 307
- Issue: 2
- Pages: 290-9
- Medium: Print
- Language: English
- Citation (JAMA): Kim Doyeob, Dressler Gregory R, et al. Pten Modulates Gdnf/Ret Mediated Chemotaxis and Branching Morphogenesis in the Developing Kidney.. Dev. Biol. Jul 2007;307:290-9
Abstract
The RET receptor tyrosine kinase is activated by GDNF and controls outgrowth and invasion of the ureteric bud epithelia in the developing kidney. In renal epithelial cells and in enteric neuronal precursor cells, activation of RET results in chemotaxis as Ret expressing cells invade the surrounding GDNF expressing tissue. One potential downstream signaling pathway governing RET mediated chemotaxis may require phosphatidylinositol 3-kinase (PI3K), which generates PI(3,4,5) triphosphate. The PTEN tumor suppressor gene encodes a protein and lipid phosphatase that regulates cell growth, apoptosis and many other cellular processes. PTEN helps regulate cellular chemotaxis by antagonizing the PI3K signaling pathway through dephosphorylation of phosphotidylinositol triphosphates. In this report, we show that PTEN suppresses RET mediated cell migration and chemotaxis in cell culture assays, that RET activation results in asymmetric localization of inositol triphosphates and that loss of PTEN affects the pattern of branching morphogenesis in developing mouse kidneys. These data suggest a critical role for the PI3K/PTEN axis in shaping the pattern of epithelial branches in response to RET activation.
Mesh Headings (Keywords): 1-Phosphatidylinositol 3-Kinase, Animals, Cell Line, Cell Movement, Chemotaxis, Dogs, Glial Cell Line-Derived Neurotrophic Factor, Green Fluorescent Proteins, Kidney, Mice, Mice, Transgenic, Morphogenesis, Mutation, PTEN Phosphohydrolase, Phosphatidylinositol Phosphates, Proto-Oncogene Proteins c-ret, Recombinant Proteins, Signal Transduction
Check for Full Text / PubMed Unique Identifier (PMID): 17540362
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.