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Journal of Cell Science, Vol 112, Issue 6 905-915, Copyright © 1999 by Company of Biologists
JOURNAL ARTICLES |
KA Grako, T Ochiya, D Barritt, A Nishiyama and WB Stallcup
The Burnham Institute, La Jolla Cancer Research Center, La Jolla, CA 92037, USA.
A line of null mice has been produced which fails to express the transmembrane chondroitin sulfate proteoglycan NG2. Homozygous NG2 null mice do not exhibit gross phenotypic differences from wild-type mice, suggesting that detailed analyses are required to detect subtle alterations caused by the absence of NG2. Accordingly, dissociated cultures of aortic smooth muscle cells from null mice were compared to parallel cultures from wild-type mice for their ability to proliferate and migrate in response to specific growth factors. Both null and wild-type smooth muscle cells exhibited identical abilities to proliferate and migrate in response to PDGF-BB. In contrast, only the wild-type cells responded to PDGF-AA in both types of assays. NG2 null cells failed to proliferate or migrate in response to PDGF-AA, implying a defect in the signaling cascade normally initiated by activation of the PDGF (alpha)-receptor. In agreement with this idea, activation of the extracellular signal-regulated kinase (ERK) in response to PDGF-AA treatment occured only in wild-type cells. Failure to observe autophosphorylation of the PDGF (alpha)-receptor in PDGF-AA-treated null cells indicates that the absence of NG2 causes a defect in signal transduction at the level of (alpha)-receptor activation.
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 I. T. Makagiansar, S. Williams, K. Dahlin-Huppe, J.-i. Fukushi, T. Mustelin, and W. B. Stallcup Phosphorylation of NG2 Proteoglycan by Protein Kinase C-{alpha} Regulates Polarized Membrane Distribution and Cell Motility J. Biol. Chem., December 31, 2004; 279(53): 55262 - 55270. [Abstract] [Full Text] [PDF]
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 J. Legg, U. B. Jensen, S. Broad, I. Leigh, and F. M. Watt Role of melanoma chondroitin sulphate proteoglycan in patterning stem cells in human interfollicular epidermis Development, December 15, 2003; 130(24): 6049 - 6063. [Abstract] [Full Text] [PDF]
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 W. B. Stallcup and K. Dahlin-Huppe Chondroitin sulfate and cytoplasmic domain-dependent membrane targeting of the NG2 proteoglycan promotes retraction fiber formation and cell polarization J. Cell Sci., March 8, 2002; 114(12): 2315 - 2325. [Abstract] [Full Text] [PDF]
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X. Fang, M. A. Burg, D. Barritt, K. Dahlin-Huppe, A. Nishiyama, and W. B. Stallcup Cytoskeletal Reorganization Induced by Engagement of the NG2 Proteoglycan Leads to Cell Spreading and Migration Mol. Biol. Cell, October 1, 1999; 10(10): 3373 - 3387. [Abstract] [Full Text]
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L. Goretzki, M. A. Burg, K. A. Grako, and W. B. Stallcup High-affinity Binding of Basic Fibroblast Growth Factor and Platelet-derived Growth Factor-AA to the Core Protein of the NG2 Proteoglycan J. Biol. Chem., June 11, 1999; 274(24): 16831 - 16837. [Abstract] [Full Text] [PDF]
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 M. A. Burg, R. Pasqualini, W. Arap, E. Ruoslahti, and W. B. Stallcup NG2 Proteoglycan-binding Peptides Target Tumor Neovasculature Cancer Res., June 1, 1999; 59(12): 2869 - 2874. [Abstract] [Full Text] [PDF]
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L. Goretzki, C. R. Lombardo, and W. B. Stallcup Binding of the NG2 Proteoglycan to Kringle Domains Modulates the Functional Properties of Angiostatin and Plasmin(ogen) J. Biol. Chem., September 8, 2000; 275(37): 28625 - 28633. [Abstract] [Full Text] [PDF]
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