| Transition between proliferation and differentiation for lens epithelial cells is regulated by Src family kinases. | |
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MedLine Citation:
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PMID: 12203728 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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As in many cell types, lens cells must withdraw from the cell cycle before they initiate their differentiation. The involvement of Src family kinases (SFKs) in this key initiating event in cell differentiation was examined in lens epithelial cell cultures. SFK activity was suppressed with the specific inhibitor PP1. This induced expression of the cyclin-dependent kinase (CDK) inhibitors p27 and p57 and suppressed lens epithelial cell proliferation. Therefore, inhibition of SFK activity created conditions permissive for undifferentiated lens epithelial cells to withdraw from the cell cycle. Growth of the lens epithelial cell cultures in the presence of PP1 induced expression of filensin and CP49, lens differentiation-specific intermediate filament proteins, providing evidence that suppression of SFK activity also promoted the initiation of lens cell differentiation. The mechanism by which PP1 signaled cell cycle withdrawal and commitment to differentiation was shown to involve induction of N-cadherin cell-cell junction assembly and reorganization of the actin cytoskeleton from stress fibers to cortical filaments. This result was supported by the compaction of the epithelial monolayer in response to PP1, a morphogenetic change that we have previously shown to be dependent on N-cadherin function and a hallmark of the commencement of the lens differentiation program in culture. The results presented in this study suggest that the decision of lens epithelial cells to withdraw from the cell cycle and initiate differentiation requires inhibition of SFKs and the formation of N-cadherin cell-cell junctions. |
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Authors:
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Janice L Walker; Liping Zhang; A Sue Menko |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Developmental dynamics : an official publication of the American Association of Anatomists Volume: 224 ISSN: 1058-8388 ISO Abbreviation: Dev. Dyn. Publication Date: 2002 Aug |
Date Detail:
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Created Date: 2002-08-30 Completed Date: 2003-04-07 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 9201927 Medline TA: Dev Dyn Country: United States |
Other Details:
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Languages: eng Pagination: 361-72 Citation Subset: IM |
Copyright Information:
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Copyright 2002 Wiley-Liss, Inc. |
Affiliation:
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Department of Pathology, Anatomy, and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Actins
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metabolism Animals Cadherins / metabolism Cell Cycle / physiology Cell Cycle Proteins / metabolism Cell Differentiation / physiology* Cell Division / physiology* Cells, Cultured Chick Embryo Cyclin-Dependent Kinase Inhibitor p27 Cyclin-Dependent Kinase Inhibitor p57 Enzyme Inhibitors / metabolism Epithelial Cells / cytology, physiology* Eye Proteins / metabolism Integrin alpha6 / metabolism Intermediate Filament Proteins / metabolism Lens, Crystalline / cytology*, physiology Nuclear Proteins / metabolism Oncogene Protein pp60(v-src) / metabolism Pyrazoles / metabolism Pyrimidines / metabolism Quail / embryology Tumor Suppressor Proteins / metabolism src-Family Kinases / antagonists & inhibitors, metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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EY10577/EY/NEI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/4-amino-5-(4-methylphenyl)-7-(tert-butyl)pyrazolo(3,4-d)pyrimidine; 0/Actins; 0/Cadherins; 0/Cell Cycle Proteins; 0/Cyclin-Dependent Kinase Inhibitor p57; 0/Enzyme Inhibitors; 0/Eye Proteins; 0/Integrin alpha6; 0/Intermediate Filament Proteins; 0/Nuclear Proteins; 0/Pyrazoles; 0/Pyrimidines; 0/Tumor Suppressor Proteins; 0/filensin; 147604-94-2/Cyclin-Dependent Kinase Inhibitor p27; EC 2.7.10.2/Oncogene Protein pp60(v-src); EC 2.7.10.2/src-Family Kinases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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