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Research Article

Pulse-chase analysis of procollagen biosynthesis by azidohomoalanine labeling

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Pages 403-410 | Received 20 Jun 2014, Accepted 19 Aug 2014, Published online: 22 Sep 2014

References

  • Shapiro JR, Byers PH, Glorieux FH, Sponseller PD, eds. Osteogenesis imperfecta: a translational approach to brittle bone disease. Amsterdam: Academic Press; 2014
  • Arnold WV, Fertala A. Skeletal diseases caused by mutations that affect collagen structure and function. Int J Biochem Cell B 2013;45:1556–67
  • Bateman JF, Boot-Handford RP, Lamande SR. Genetic diseases of connective tissues: cellular and extracellular effects of ECM mutations. Nat Rev Genet 2009;10:173–83
  • De Paepe A, Malfait F. The Ehlers-Danlos syndrome, a disorder with many faces. Clin Genet 2012;82:1–11
  • Byers PH, Murray ML. Ehlers-Danlos syndrome: a showcase of conditions that lead to understanding matrix biology. Matrix Biol 2014;33:10–15
  • Wynn TA. Cellular and molecular mechanisms of fibrosis. J Pathol 2008;214:199–210
  • Kalluri R, Zeisberg M. Fibroblasts in cancer. Nat Rev Cancer 2006;6:392–401
  • Makareeva E, Han SJ, Vera JC, Sackett DL, Holmbeck K, Phillips CL, Visse R, Nagase H, Leikin S. Carcinomas contain a matrix metalloproteinase-resistant isoform of type I collagen exerting selective support to invasion. Cancer Res 2010;70:4366–74
  • Jansens A, Braakman I. Pulse-chase labeling techniques for the analysis of protein maturation and degradation. Methods Mol Biol 2003;232:133–45
  • Pollard J. Radioisotopic labeling of proteins for polyacrylamide gel electrophoresis. In: Walker J, ed. The protein protocols handbook. New York: Humana Press; 1996:121–6
  • Bonifacino JS. Metabolic labeling with amino acids. Curr Protoc Mol Biol 2001;44:VI:10.8.1–10.8.8
  • Coligan JE, Gates FT, Kimball ES, Maloy WL. Radiochemical sequence-analysis of biosynthetically labeled proteins. Methods Enzymol 1983;91:413–34
  • Bateman JF, Mascara T, Chan D, Cole WG. Abnormal type-I collagen-metabolism by cultured fibroblasts in lethal perinatal osteogenesis imperfecta. Biochem J 1984;217:103–15
  • Barsh GS, Byers PH. Reduced secretion of structurally abnormal type-i procollagen in a form of osteogenesis imperfecta. Proc Natl Acad Sci U S A 1981;78:5142–6
  • Ong SE, Mann M. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat Protoc 2006;1:2650–60
  • Van Hoof D, Pinkse MWH, Oostwaard DWV, Mummery CL, Heck AJR, Krijgsveld J. An experimental correction for arginine-to-proline conversion artifacts in SILAC-based quantitative proteomics. Nat Methods 2007;4:677–8
  • Boersema PJ, Raijmakers R, Lemeer S, Mohammed S, Heck AJR. Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat Protoc 2009;4:484–94
  • Mann M. Functional and quantitative proteomics using SILAC. Nat Rev Mol Cell Bio 2006;7:952–8
  • Johnson JA, Lu YY, Van Deventer JA, Tirrell DA. Residue-specific incorporation of non-canonical amino acids into proteins: recent developments and applications. Curr Opin Chem Biol 2010;14:774–80
  • Dieterich D, Lee J, Link A, Graumann J, Tirrell D, Schuman E. Labeling, detection and identification of newly synthesized proteomes with bioorthogonal non-canonical amino-acid tagging. Nat Protoc 2007;2:532–40
  • Dieterich DC, Link AJ, Graumann J, Tirrell DA, Schuman EM. Selective identification of newly synthesized proteins in mammalian cells using bioorthogonal noncanonical amino acid tagging (BONCAT). Proc Natl Acad Sci USA 2006;103:9482–7
  • Prescher J, Bertozzi C. Chemistry in living systems. Nat Chem Biol 2005;1:13–21
  • Baskin JM, Prescher JA, Laughlin ST, Agard NJ, Chang PV, Miller IA, Lo A, Codelli JA, Bertozzi CR. Copper-free click chemistry for dynamic in vivo imaging. Proc Natl Acad Sci USA 2007;104:16793–7
  • Griffin RJ. The medicinal chemistry of the azido group. Prog Med Chem 1994;31:121–232
  • Dieterich D, Hodas J, Gouzer G, Shadrin I, Ngo J, Triller A, Tirrell DA, Schuman EM. In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons. Nat Neurosci 2010;13:897–905
  • Taskent-Sezgin H, Chung J, Banerjee P, Nagarajan S, Dyer R, Carrico I, Raleigh DP. Azidohomoalanine: a conformationally sensitive IR probe of protein folding, protein structure, and electrostatics. Angew Chem 2010;49:7473–5
  • Dover R, Jayaram Y, Patel K, Chinery R. p53 expression in cultured cells following radioisotope labelling. J Cell Sci 1994;107:1181–4
  • Yeargin J, Haas M. Elevated levels of wild-type P53 induced by radiolabeling of cells leads to apoptosis or sustained growth arrest. Curr Biol 1995;5:423–31
  • Hu VW, Heikka DS. Radiolabeling revisited: metabolic labeling with (35)S-methionine inhibits cell cycle progression, proliferation, and survival. FASEB J 2000;14:448–54
  • Hu VW, Heikka DS, Dieffenbach PB, Ha L. Metabolic radiolabeling: experimental tool or Trojan horse? (35)S-methionine induces DNA fragmentation and p53-dependent ROS production. FASEB J 2001;15:1562–8
  • Marko NF, Dieffenbach PB, Yan G, Ceryak S, Howell RW, Mccaffrey TA, Hu VW. Does metabolic radiolabeling stimulate the stress response? Gene expression profiling reveals differential cellular responses to internal beta vs. external gamma radiation. FASEB J 2003;17:1470–86
  • Solary E, Bertrand R, Jenkins J, Pommier Y. Radiolabeling of DNA can induce its fragmentation in Hl-60 human promyelocytic leukemic-cells. Exp Cell Res 1992;203:495–8
  • Yanokura M, Takase K, Yamamoto K, Teraoka H. Cell death and cell-cycle arrest induced by incorporation of [H-3]thymidine into human haemopoietic cell lines. Int J Radiat Biol 2000;76:295–303
  • Raghunath M, Bruckner P, Steinmann B. Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta. J Mol Biol 1994;236:940–9
  • Makareeva E, Aviles NA, Leikin S. Chaperoning osteogenesis: new protein-folding disease paradigms. Trends Cell Biol 2011;21:168–76
  • Makareeva E, Cabral WA, Marini JC, Leikin S. Molecular mechanism of alpha 1(I)-osteogenesis imperfecta/ehlers-danlos syndrome – unfolding of an N-anchor domain at the N-terminal end of the type I collagen triple helix. J Biol Chem 2006;281:6463–70
  • Schmittgen TD, Livak KJ. Analyzing real-time PCR data by the comparative C-T method. Nat Protoc 2008;3:1101–8
  • Marini JC, Forlino A, Cabral WA, Barnes AM, San Antonio JD, Milgrom S, Hyland JC, Körkkö J, Prockop DJ, De Paepe A, Coucke P, Symoens S, Glorieux FH, Roughley PJ, Lund AM, Kuurila-Svahn K, Hartikka H, Cohn DH, Krakow D, Mottes M, Schwarze U, Chen D, Yang K, Kuslich C, Troendle J, Dalgleish R, Byers PH. Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans. Hum Mutat 2007;28:209–21
  • Bruckner P, Eikenberry EF. Formation of the triple helix of type I procollagen in cellulo. Temperature-dependent kinetics support a model based on cis in equilibrium trans isomerization of peptide bonds. Eur J Biochem 1984;140:391–5
  • Cabral WA, Chang W, Barnes AM, Weis M, Scott MA, Leikin S, Makareeva E, Kuznetsova NV, Rosenbaum KN, Tifft CJ, Bulas DI, Kozma C, Smith PA, Eyre DR, Marini JC. Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta. Nat Genet 2007;39:359–65
  • Forlino A, Kuznetsova NV, Marini JC, Leikin S. Selective retention and degradation of molecules with a single mutant alpha1(I) chain in the Brtl IV mouse model of OI. Matrix Biol 2007;26:604–14
  • Lander H. An essential role for free radicals and derived species in signal transduction. FASEB J 1997;11:118–24
  • Chau JF, Jia D, Wang Z, Liu Z, Hu Y, Zhang X, Jia H, Lai KP, Leong WF, Au BJ, Mishina Y, Chen YG, Biondi C, Robertson E, Xie D, Liu H, He L, Wang X, Yu Q, Li B. A crucial role for bone morphogenetic protein-Smad1 signalling in the DNA damage response. Nat Commun 2012;3:836
  • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 2002;1:376–86
  • Kiick K, Saxon E, Tirrell D, Bertozzi C. Incorporation of azides into recombinant proteins for chemoselective modification by the staudinger ligation. Proc Natl Acad Sci USA 2002;99:19–24
  • Bateman JF, Chan D, Mascara T, Rogers JG, Cole WG. Collagen defects in lethal perinatal osteogenesis imperfecta. Biochem J 1986;240:699–708
  • Vogel BE, Minor RR, Freund M, Prockop DJ. A point mutation in a type I procollagen gene converts glycine 748 of the alpha 1 chain to cysteine and destabilizes the triple helix in a lethal variant of osteogenesis imperfecta. J Biol Chem 1987;262:14737–44
  • Ishida Y, Yamamoto A, Kitamura A, Lamande SR, Yoshimori T, Bateman JF, Kubota H, Nagata K. Autophagic elimination of misfolded procollagen aggregates in the endoplasmic reticulum as a means of cell protection. Mol Biol Cell 2009;20:2744–54

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