Pref-1 Interacts with Fibronectin To Inhibit Adipocyte Differentiation

REFERENCES

• Antras, J., F. Hilliou, G. Redziniak, and J. Pairault. 1989. Decreased biosynthesis of actin and cellular fibronectin during adipose conversion of 3T3-F442A cells. Reorganization of the cytoarchitecture and extracellular matrix fibronectin. Biol. Cell 66:247–254.
   PubMed Web of Science ®Google Scholar
• Baladrón, V., M. J. Ruiz-Hidalgo, M. L. Nueda, M. J. Diaz-Guerra, J. J. Garcia-Ramirez, E. Bonvini, E. Gubina, and J. Laborda. 2005. dlk acts as a negative regulator of Notch1 activation through interactions with specific EGF-like repeats. Exp. Cell Res. 303:343–359.
   PubMedGoogle Scholar
• Bray, S. J., S. Takada, E. Harrison, S. C. Shen, and A. C. Ferguson-Smith. 2008. The atypical mammalian ligand Delta-like homologue 1 (Dlk1) can regulate Notch signalling in Drosophila. BMC Dev. Biol. 8:11.
   PubMedGoogle Scholar
• Fukai, F., T. Iso, K. Sekiguchi, N. Miyatake, A. Tsugita, and T. Katayama. 1993. An amino-terminal fibronectin fragment stimulates the differentiation of ST-13 preadipocytes. Biochemistry 32:5746–5751.
   PubMedGoogle Scholar
• Garcés, C., M. J. Ruiz-Hidalgo, J. Font de Mora, C. Park, L. Miele, J. Goldstein, E. Bonvini, A. Porras, and J. Laborda. 1997. Notch-1 controls the expression of fatty acid-activated transcription factors and is required for adipogenesis. J. Biol. Chem. 272:29729–29734.
   PubMedGoogle Scholar
• George, E. L., E. N. Georges-Labouesse, R. S. Patel-King, H. Rayburn, and R. O. Hynes. 1993. Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development 119:1079–1091.
   PubMed Web of Science ®Google Scholar
• Howe, A. K., A. E. Aplin, and R. L. Juliano. 2002. Anchorage-dependent ERK signaling-mechanisms and consequences. Curr. Opin. Genet. Dev. 12:30–35.
   PubMed Web of Science ®Google Scholar
• Hynes, R. O. 2009. The extracellular matrix: not just pretty fibrils. Science 326:1216–1219.
   PubMed Web of Science ®Google Scholar
• Hynes, R. O. 2002. Integrins: bidirectional, allosteric signaling machines. Cell 110:673–687.
   PubMed Web of Science ®Google Scholar
• Jensen, C. H., B. Teisner, P. Hojrup, H. B. Rasmussen, O. D. Madsen, B. Nielsen, and K. Skjodt. 1993. Studies on the isolation, structural analysis and tissue localization of fetal antigen 1 and its relation to a human adrenal-specific cDNA, pG2. Hum. Reprod. 8:635–641.
   PubMedGoogle Scholar
• Kamiya, S., R. Kato, M. Wakabayashi, T. Tohyama, I. Enami, M. Ueki, H. Yajima, T. Ishii, H. Nakamura, T. Katayama, J. Takagi, and F. Fukai. 2002. Fibronectin peptides derived from two distinct regions stimulate adipocyte differentiation by preventing fibronectin matrix assembly. Biochemistry 41:3270–3277.
   PubMedGoogle Scholar
• Kim, K. A., J. H. Kim, Y. Wang, and H. S. Sul. 2007. Pref-1 (preadipocyte factor 1) activates the MEK/extracellular signal-regulated kinase pathway to inhibit adipocyte differentiation. Mol. Cell. Biol. 27:2294–2308.
   PubMed Web of Science ®Google Scholar
• Komatsu, H., M. Y. Chao, J. Larkins-Ford, M. E. Corkins, G. A. Somers, T. Tucey, H. M. Dionne, J. Q. White, K. Wani, M. Boxem, and A. C. Hart. 2008. OSM-11 facilitates LIN-12 Notch signaling during Caenorhabditis elegans vulval development. PLoS Biol. 6:e196.
   PubMed Web of Science ®Google Scholar
• Kopan, R., and M. X. Ilagan. 2009. The canonical Notch signaling pathway: unfolding the activation mechanism. Cell 137:216–233.
   PubMed Web of Science ®Google Scholar
• Lee, K., J. A. Villena, Y. S. Moon, K. H. Kim, S. Lee, C. Kang, and H. S. Sul. 2003. Inhibition of adipogenesis and development of glucose intolerance by soluble preadipocyte factor-1 (Pref-1). J. Clin. Investig. 111:453–461.
   PubMedGoogle Scholar
• Liu, J., S. M. DeYoung, M. Zhang, A. Cheng, and A. R. Saltiel. 2005. Changes in integrin expression during adipocyte differentiation. Cell Metab. 2:165–177.
   PubMed Web of Science ®Google Scholar
• Mei, B., L. Zhao, L. Chen, and H. S. Sul. 2002. Only the large soluble form of preadipocyte factor-1 (Pref-1), but not the small soluble and membrane forms, inhibits adipocyte differentiation: role of alternative splicing. Biochem. J. 364:137–144.
   PubMedGoogle Scholar
• Moon, Y. S., C. M. Smas, K. Lee, J. A. Villena, K. H. Kim, E. J. Yun, and H. S. Sul. 2002. Mice lacking paternally expressed Pref-1/Dlk1 display growth retardation and accelerated adiposity. Mol. Cell. Biol. 22:5585–5592.
   PubMed Web of Science ®Google Scholar
• Nichols, A. M., Y. Pan, A. Herreman, B. K. Hadland, B. De Strooper, R. Kopan, and S. S. Huppert. 2004. Notch pathway is dispensable for adipocyte specification. Genesis 40:40–44.
   PubMed Web of Science ®Google Scholar
• Pullikuth, A. K., and A. D. Catling. 2007. Scaffold mediated regulation of MAPK signaling and cytoskeletal dynamics: a perspective. Cell Signal. 19:1621–1632.
   PubMed Web of Science ®Google Scholar
• Rahman, S., Y. Patel, J. Murray, K. V. Patel, R. Sumathipala, M. Sobel, and E. S. Wijelath. 2005. Novel hepatocyte growth factor (HGF) binding domains on fibronectin and vitronectin coordinate a distinct and amplified Met-integrin induced signalling pathway in endothelial cells. BMC Cell Biol. 6:8.
   PubMedGoogle Scholar
• Ross, D. A., P. K. Rao, and T. Kadesch. 2004. Dual roles for the Notch target gene Hes-1 in the differentiation of 3T3-L1 preadipocytes. Mol. Cell. Biol. 24:3505–3513.
   PubMedGoogle Scholar
• Sander, E. E., J. P. ten Klooster, S. van Delft, R. A. van der Kammen, and J. G. Collard. 1999. Rac downregulates Rho activity: reciprocal balance between both GTPases determines cellular morphology and migratory behavior. J. Cell Biol. 147:1009–1022.
   PubMed Web of Science ®Google Scholar
• Selvarajan, S., L. R. Lund, T. Takeuchi, C. S. Craik, and Z. Werb. 2001. A plasma kallikrein-dependent plasminogen cascade required for adipocyte differentiation. Nat. Cell Biol. 3:267–275.
   PubMed Web of Science ®Google Scholar
• Smas, C. M., L. Chen, and H. S. Sul. 1997. Cleavage of membrane-associated pref-1 generates a soluble inhibitor of adipocyte differentiation. Mol. Cell. Biol. 17:977–988.
   PubMed Web of Science ®Google Scholar
• Smas, C. M., L. Chen, L. Zhao, M. J. Latasa, and H. S. Sul. 1999. Transcriptional repression of pref-1 by glucocorticoids promotes 3T3-L1 adipocyte differentiation. J. Biol. Chem. 274:12632–12641.
   PubMed Web of Science ®Google Scholar
• Smas, C. M., D. Green, and H. S. Sul. 1994. Structural characterization and alternate splicing of the gene encoding the preadipocyte EGF-like protein pref-1. Biochemistry 33:9257–9265.
   PubMedGoogle Scholar
• Smas, C. M., D. Kachinskas, C. M. Liu, X. Xie, L. K. Dircks, and H. S. Sul. 1998. Transcriptional control of the pref-1 gene in 3T3-L1 adipocyte differentiation. Sequence requirement for differentiation-dependent suppression. J. Biol. Chem. 273:31751–31758.
   PubMed Web of Science ®Google Scholar
• Smas, C. M., and H. S. Sul. 1997. Molecular mechanisms of adipocyte differentiation and inhibitory action of pref-1. Crit. Rev. Eukaryot. Gene Expr. 7:281–298.
   PubMedGoogle Scholar
• Smas, C. M., and H. S. Sul. 1993. Pref-1, a protein containing EGF-like repeats, inhibits adipocyte differentiation. Cell 73:725–734.
   PubMed Web of Science ®Google Scholar
• Spiegelman, B. M., and C. A. Ginty. 1983. Fibronectin modulation of cell shape and lipogenic gene expression in 3T3-adipocytes. Cell 35:657–666.
   PubMed Web of Science ®Google Scholar
• Sul, H. S. 2009. Minireview: Pref-1: role in adipogenesis and mesenchymal cell fate. Mol. Endocrinol. 23:1717–1725.
   PubMedGoogle Scholar
• Villena, J. A., C. S. Choi, Y. Wang, S. Kim, Y. J. Hwang, Y. B. Kim, G. Cline, G. I. Shulman, and H. S. Sul. 2008. Resistance to high-fat diet-induced obesity but exacerbated insulin resistance in mice overexpressing preadipocyte factor-1 (Pref-1): a new model of partial lipodystrophy. Diabetes 57:3258–3266.
   PubMed Web of Science ®Google Scholar
• Wang, Y., and H. S. Sul. 2006. Ectodomain shedding of preadipocyte factor 1 (Pref-1) by tumor necrosis factor alpha converting enzyme (TACE) and inhibition of adipocyte differentiation. Mol. Cell. Biol. 26:5421–5435.
   PubMed Web of Science ®Google Scholar
• Wang, Y., and H. S. Sul. 2009. Pref-1 regulates mesenchymal cell commitment and differentiation through Sox9. Cell Metab. 9:287–302.
   PubMed Web of Science ®Google Scholar
• White, E. S., F. E. Baralle, and A. F. Muro. 2008. New insights into form and function of fibronectin splice variants. J. Pathol. 216:1–14.
   PubMed Web of Science ®Google Scholar
• Wijelath, E. S., S. Rahman, M. Namekata, J. Murray, T. Nishimura, Z. Mostafavi-Pour, Y. Patel, Y. Suda, M. J. Humphries, and M. Sobel. 2006. Heparin-II domain of fibronectin is a vascular endothelial growth factor-binding domain: enhancement of VEGF biological activity by a singular growth factor/matrix protein synergism. Circ. Res. 99:853–860.
   PubMed Web of Science ®Google Scholar
• Zhong, C., M. Chrzanowska-Wodnicka, J. Brown, A. Shaub, A. M. Belkin, and K. Burridge. 1998. Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol. 141:539–551.
   PubMed Web of Science ®Google Scholar