| Girding for migratory cues: roles of the Akt substrate Girdin in cancer progression and angiogenesis. | |
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MedLine Citation:
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PMID: 20132219 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Cell migration is a fundamental aspect of a multitude of physiological and pathological processes, including embryonic development, inflammation, angiogenesis, and cancer progression. A variety of proteins are essential for cell migration, but context-specific signaling pathways and promigratory proteins must now be identified for our understanding of cancer biology to continue to advance. In this review, we focus on the emerging roles of Girdin (also designated KIAA1212, APE, GIV, and HkRP1), a novel component of the phosphatidylinositol 3-kinase (PI3-K)/Akt signaling pathway that is a core-signaling transduction pathway in cancer progression. Girdin is expressed in some types of cancer cells and immature endothelial cells, and is therefore at the crossroads of multiple intracellular processes, including reorganization of the actin cytoskeleton, endocytosis, and modulation of Akt activity, which ultimately lead to cancer invasion and angiogenesis. It also acts as a nonreceptor guanine nucleotide exchange factor (GEF) for Galphai proteins. A significant observation is that Girdin, although vital for cancer progression and postnatal vascular remodelling, is dispensable for cell migratory events during embryonic development. These findings suggest that Girdin and its interacting proteins are potential pharmaceutical targets for cancer therapies and pathological anigiogenesis, including tumor angiogenesis. |
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Authors:
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Liang Weng; Atsushi Enomoto; Maki Ishida-Takagishi; Naoya Asai; Masahide Takahashi |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review Date: 2010-02-02 |
Journal Detail:
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Title: Cancer science Volume: 101 ISSN: 1349-7006 ISO Abbreviation: Cancer Sci. Publication Date: 2010 Apr |
Date Detail:
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Created Date: 2010-08-13 Completed Date: 2010-09-29 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101168776 Medline TA: Cancer Sci Country: England |
Other Details:
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Languages: eng Pagination: 836-42 Citation Subset: IM |
Affiliation:
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Department of Pathology, Nagoya University Graduate School of Medicine, Showa-ku, Nagoya, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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1-Phosphatidylinositol 3-Kinase
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metabolism Animals Cell Movement* / physiology Disease Progression* Endothelial Cells / metabolism Female Humans Neoplasms / blood supply*, metabolism* Neoplastic Processes Neovascularization, Pathologic* Pregnancy Proto-Oncogene Proteins c-akt / metabolism* Signal Transduction |
| Chemical | |
Reg. No./Substance:
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EC 2.7.1.137/1-Phosphatidylinositol 3-Kinase; EC 2.7.11.1/Proto-Oncogene Proteins c-akt |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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