Tenascin-C: Its functions as an integrin ligand |
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| Affiliation: | 1. Department of Cell Biology and Human Anatomy, University of California at Davis, 1 Shields Avenue, Davis, CA 95616, USA;2. Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058 Basel, Switzerland;3. Faculty of Science, University of Basel, Klingelbergstrasse 50, CH-4056 Basel, Switzerland;1. Department of Chemistry ‘U. Schiff’, University of Florence, Via della Lastruccia 13, I-50019 Sesto Fiorentino, Italy;2. Department of Biomedical, Experimental and Clinical Sciences “Mario Serio”, University of Florence, Viale Morgagni 50, I-50134 Florence, Italy;3. Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Chiba 278-8510, Japan;4. Department of Drug Informatics, Faculty of Pharmaceutical Sciences, Josai International University, 1 Gumyo, Togane-shi, Chiba 283-8555, Japan;5. Department of Applied Chemistry, Faculty of Science, Tokyo University of Science, Tokyo 162-8601, Japan;6. Department of Chemistry, Kurume University School of Medicine, Kurume 830-0011, Japan;12. Department of Internal Medicine, Kagawa University, Kagawa 761-0793, Japan;1. GlaxoSmithKline Medicines Research Centre, Gunnels Wood Road, Stevenage SG1 2NY, UK;2. University of Nottingham School of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK;1. Key Laboratory of Smart Drug Delivery, Ministry of Education, School of Pharmacy, Fudan University, Lane 826, Zhangheng Road, Shanghai 201203, PR China;2. Department of Pharmacology, Institute of Medical Sciences, Shanghai Jiaotong University School of Medicine, 280 South Chongqing Road, Shanghai 200025, PR China;1. State Key Laboratory of Organ Failure Research, National Clinical Research Center of Kidney Disease, Division of Nephrology, Nanfang Hospital, Southern Medical University, Guangzhou, China;2. Guangzhou Regenerative Medicine and Health Guangdong Laboratory, Guangzhou, China;3. Department of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA |
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| Abstract: | This review summarizes the experimental evidence of tenascin-C/integrin interactions, emphasizing the identification of integrin binding sites and the effects of specific interactions on cell behavior. At least four integrins appear to bind to the third fibronectin-type 3 domain of tenascin-C: α9β1, αVβ3, α8β1 and αVβ6. The α9β1 integrin recognizes a highly conserved IDG motif in this domain, while the others recognize an RGD motif. There is also significant evidence that the collagen receptor α2β1 can bind to tenascin-C, but the interacting site is unknown. Tenascin-C interactions with α9β1 and αVβ3 can promote cell proliferation and interactions with αVβ3 can also inhibit apoptosis. Interactions with α7β1 integrin, which may bind to the alternatively spliced domain of tenascin-C, and α9β1 integrin are able to influence the differentiation of mesenchymal stem cells into the neuronal lineage. This illustrates the potential for using our knowledge of tenascins and their integrin receptors in stem cell-based therapies. |
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| Keywords: | Tenascin Integrin Extracellular matrix RGD IDG |
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