Phosphorylation of Extracellular Matrix Tenascin-X Detected by Differential Mass Tagging Followed by NanoLC-MALDI-TOF/TOF-MS/MS Using ProteinPilot Software

REFERENCES

• Hunter, T. (2000). Signaling-2000 and beyond. Cell 100:113–127.
   PubMed Web of Science ®Google Scholar
• Blume-Jensen, P., and Hunter, T. (2001). Oncogenic kinase signalling. Nature 411:355–365.
   PubMed Web of Science ®Google Scholar
• Imada, S., Sugiyama, Y., and Imada, M. (1988). Fibronectin phosphorylation by ecto-protein kinase. Exp. Cell Res. 179:554–564.
   PubMed Web of Science ®Google Scholar
• Revert, F., Penadés, J.R., Plana, M., Bernal, D., Johansson, C., Itarte, E., Cervera, J., Wieslander, J., Quinones, S., and Saus, J. (1995). Phosphorylation of the Goodpasture antigen by type A protein kinases. J. Biol. Chem. 270:13254–13261.
   PubMed Web of Science ®Google Scholar
• Seger, D., Gechtman, Z., and Shaltiel, S. (1998). Phosphorylation of vitronectin by casein kinase II. Identification of the sites and their promotion of cell adhesion and spreading. J. Biol. Chem. 273:24805–24813.
   PubMed Web of Science ®Google Scholar
• Koliakos, G., Trachana, V., Gaitatzi, M., and Dimitriadou, A. (2001). Phosphorylation of laminin-1 by protein kinase C. Mol. Cells 11:179–185.
   PubMed Web of Science ®Google Scholar
• Trachana, V., Christophorides, E., Kouzi-Koliakos, K., and Koliakos, G. (2005). Laminin-1 is phosphorylated by ecto-protein kinases of monocytes. Int. J. Biochem. Cell Biol. 37:478–492.
   PubMed Web of Science ®Google Scholar
• Stepanova, V., Jerke, U., Sagach, V., Lindschau, C., Dietz, R., Haller, H., and Dumler, I. (2002). Urokinase-dependent human vascular smooth muscle cell adhesion requires selective vitronectin phosphorylation by ectoprotein kinase CK2. J. Biol. Chem. 277:10265–10272.
   PubMed Web of Science ®Google Scholar
• Reinders, J., and Sickmann, A. (2005). State-of-the-art in phosphoproteomics. Proteomics 5:4052–4061.
   PubMed Web of Science ®Google Scholar
• Eyrich, B., Sickmann, A., and Zahedi, R.P. (2011). Catch me if you can: Mass spectrometry-based phosphoproteomics and quantification strategies. Proteomics 11:554–570.
   PubMed Web of Science ®Google Scholar
• Stensballe, A., Andersen, S., and Jensen, O.N. (2001). Characterization of phosphoproteins from electrophoretic gels by nanoscale Fe(III) affinity chromatography with off-line mass spectrometry analysis. Proteomics 1:207–222.
   PubMed Web of Science ®Google Scholar
• Ross, P.L., Huang, Y.N., Marchese, J.N., Williamson, B., Parker, K., Hattan, S., Khainovski, N., Pillai, S., Dey, S., Daniels, S., Purkayastha, S., Juhasz, P., Martin, S., Bartlet-Jones, M., He, F., Jacobson, A., and Pappin, D.J. (2004). Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell Proteomics 3:1154–1169.
   PubMed Web of Science ®Google Scholar
• Shirran, S.L., and Botting, C.H. (2010). A comparison of the accuracy of iTRAQ quantification by nLC-ESI MSMS and nLC-MALDI MSMS methods. J. Proteomics 73:1391–1403.
   PubMed Web of Science ®Google Scholar
• Shilov, I.V., Seymour, S.L., Patel, A.A., Loboda, A., Tang, W.H., Keating, S.P., Hunter, C.L., Nuwaysir, L.M., and Schaeffer, D.A. (2007). The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol. Cell Proteomics 6:1638–1655.
   PubMed Web of Science ®Google Scholar
• Chiquet-Ehrismann, R. (2004). Tenascins. Int. J. Biochem. Cell Biol. 36:986–990.
   PubMed Web of Science ®Google Scholar
• Morel, Y., Bristow, J., Gitelman, S.E., and Miller, W.L. (1989). Transcript encoded on the opposite strand of the human steroid 21-hydroxylase/complement component C4 gene locus. Proc. Natl. Acad. Sci. U.S.A. 86:6582–6586.
   PubMedGoogle Scholar
• Matsumoto, K., Arai, M., Ishihara, N., Ando, A., Inoko, H., and Ikemura, T. (1992). Cluster of fibronectin type III repeats found in the human major histocompatibility complex class III region shows the highest homology with the repeats in an extracellular matrix protein, tenascin. Genomics 12:485–491.
   PubMedGoogle Scholar
• Zweers, M.C., Hakim, A.J., Grahame, R., and Schalkwijk, J. (2004). Joint hypermobility syndromes: the pathophysiologic role of tenascin-X gene defects. Arthritis Rheum. 50:2742–2749.
   PubMed Web of Science ®Google Scholar
• Minamitani, T., Ikuta, T., Saito, Y., Takebe, G., Sato, M., Sawa, H., Nishimura, T., Nakamura, F., Takahashi, K., Ariga, H., and Matsumoto, K. (2004). Modulation of collagen fibrillogenesis by tenascin-X and type VI collagen. Exp. Cell Res. 298:305–315.
   PubMed Web of Science ®Google Scholar
• Veit, G., Hansen, U., Keene, D.R., Bruckner, P., Chiquet-Ehrismann, R., Chiquet, M., and Koch, M. (2006). Collagen XII interacts with avian tenascin-X through its NC3 domain. J. Biol. Chem. 281:27461–27470.
   PubMed Web of Science ®Google Scholar
• Margaron, Y., Bostan, L., Exposito, J.Y., Malbouyres, M., Trunfio-Sfarghiu, A.M., Berthier, Y., and Lethias, C. (2010). Tenascin-X increases the stiffness of collagen gels without affecting fibrillogenesis. Biophys. Chem. 14:87–91.
   Google Scholar
• Zweers, M.C., van Vlijmen-Willems, I.M., van Kuppevelt, T.H., Mecham, R.P., Steijlen, P.M., Bristow, J., and Schalkwijk, J. (2004). Deficiency of tenascin-X causes abnormalities in dermal elastic fiber morphology. J. Invest. Dermatol. 122:885–891.
   PubMed Web of Science ®Google Scholar
• Mao, J.R., Taylor, G., Dean, W.B., Wagner, D.R., Afzal, V., Lotz, J.C., Rubin, E.M., and Bristow, J. (2002). Tenascin-X deficiency mimics Ehlers–Danlos syndrome in mice through alteration of collagen deposition. Nat. Genet. 30:421–425.
   PubMed Web of Science ®Google Scholar
• Matsumoto, K., Takayama, N., Ohnishi, J., Ohnishi, E., Shirayoshi, Y., Nakatsuji, N., and Ariga, H. (2001). Tumour invasion and metastasis are promoted in mice deficient in tenascin-X. Genes. Cells 6:1101–1111.
   Google Scholar
• Kinoshita, T., Ariga, H., and Matsumoto, K. (2007). Distinct glycosylation in interstitial and serum tenascin-X. Biol. Pharm. Bull. 30:354–358.
   PubMed Web of Science ®Google Scholar
• Iyer, V.R., Eisen, M.B., Ross, D.T., Schuler, G., Moore, T., Lee, J.C., Trent, J.M., Staudt, L.M., Hudson Jr, J., Boguski, M.S., Lashkari, D., Shalon, D., Botstein, D., and Brown, P.O. (1999). The transcriptional program in the response of human fibroblasts to serum. Science 283:83–87.
   PubMed Web of Science ®Google Scholar
• Rikova, K., Guo, A., Zeng, Q., Possemato, A., Yu, J., Haack, H., Nardone, J., Lee, K., Reeves, C., Li, Y., Hu, Y., Tan, Z., Stokes, M., Sullivan, L., Mitchell, J., Wetzel, R., Macneill, J., Ren, J.M., and Comb, M.J. (2007). Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell 131:1190–1203.
   PubMed Web of Science ®Google Scholar
• Yu, L.-R., Zhu, Z., Chan, K.C., Issaq, H.J., Dimitrov, D.S., and Veenstra, T.D. (2007). Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J. Proteome Res. 6:4150–4162.
   PubMed Web of Science ®Google Scholar
• Gauci, S., Helbig, A.O., Slijper, M., Krijgsveld, J., Heck, A.J., and Mohammed, S. (2009). Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal. Chem. 81:4493–4501.
   PubMed Web of Science ®Google Scholar
• Ruoslahti, E. (1996). RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 12:697–715.
   PubMed Web of Science ®Google Scholar
• Sun, T., Rodriguez, M., and Kim, L. (2009). Glycogen synthase kinase 3 in the world of cell migration. Dev. Growth Differ. 51:735–742.
   PubMed Web of Science ®Google Scholar
• Gordon, J.L. (1986). Extracellular ATP: Effects, sources and fate. Biochem. J. 15:309–319.
   Google Scholar
• Crane, J.K., and Vezina, C.M. (2005). Externalization of host cell protein kinase C during enteropathogenic Escherichia coli infection. Cell Death Differ. 12:115–127.
   PubMed Web of Science ®Google Scholar