메뉴 건너뛰기




Volumn 81, Issue 1, 2012, Pages 25-32

Recombinant expression, purification and dimerization of the neurotrophic growth factor Artemin for in vitro and in vivo use

Author keywords

Disulphide bond; Growth factor; Neurological disease; Neurotrophic factor; Protein dimerization; Protein purification

Indexed keywords

ARTN PROTEIN, HUMAN; DITHIOTHREITOL; HYBRID PROTEIN; NERVE GROWTH FACTOR; NERVE PROTEIN; SUMO 1 PROTEIN;

EID: 80053443991     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.08.028     Document Type: Article
Times cited : (4)

References (40)
  • 1
    • 0036581222 scopus 로고    scopus 로고
    • The GDNF family: Signalling, biological functions and therapeutic value
    • DOI 10.1038/nrn812
    • M.S. Airaksinen, and M. Saarma The GDNF family: signalling, biological functions and therapeutic value Nat. Rev. Neurosci. 3 2002 383 394 (Pubitemid 135706635)
    • (2002) Nature Reviews Neuroscience , vol.3 , Issue.5 , pp. 383-394
    • Airaksinen, M.S.1    Saarma, M.2
  • 2
    • 33846501598 scopus 로고    scopus 로고
    • GDNF family receptor complexes are emerging drug targets
    • DOI 10.1016/j.tips.2006.12.005, PII S0165614706002884
    • M. Bespalov, and M. Saarma GDNF family receptor complexes are emerging drug targets Trends Pharmacol. Sci. 28 2007 68 74 (Pubitemid 46161837)
    • (2007) Trends in Pharmacological Sciences , vol.28 , Issue.2 , pp. 68-74
    • Bespalov, M.M.1    Saarma, M.2
  • 3
    • 0032408664 scopus 로고    scopus 로고
    • Artemin, a novel member of the GDNF ligand family, supports peripheral and central neurons and signals through the GFRα3-RET receptor complex
    • DOI 10.1016/S0896-6273(00)80649-2
    • R.H. Baloh, M.G. Tansey, P.A. Lampe, T.J. Fahrner, H. Enomoto, K.S. Simburger, M.L. Leitner, T. Araki, E.M. Johnson Jr., and J. Milbrandt Artemin, a novel member of the GDNF ligand family, supports peripheral and central neurons and signals through the GFRalpha3-RET receptor complex Neuron 21 1998 1291 1302 (Pubitemid 29022532)
    • (1998) Neuron , vol.21 , Issue.6 , pp. 1291-1302
    • Baloh, R.H.1    Tansey, M.G.2    Lampe, P.A.3    Fahrner, T.J.4    Enomoto, H.5    Simburger, K.S.6    Leitner, M.L.7    Araki, T.8    Johnson Jr., E.M.9    Milbrandt, J.10
  • 8
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • J. Schlessinger Cell signaling by receptor tyrosine kinases Cell 103 2000 193 200
    • (2000) Cell , vol.103 , pp. 193-200
    • Schlessinger, J.1
  • 10
    • 33750264993 scopus 로고    scopus 로고
    • Quantitative analysis of the activation mechanism of the multicomponent growth-factor receptor Ret
    • DOI 10.1038/nchembio823, PII NCHEMBIO823
    • S. Schlee, P. Carmillo, and A. Whitty Quantitative analysis of the activation mechanism of the multicomponent growth-factor receptor Ret Nat. Chem. Biol. 2 2006 636 644 (Pubitemid 44610348)
    • (2006) Nature Chemical Biology , vol.2 , Issue.11 , pp. 636-644
    • Schlee, S.1    Carmillo, P.2    Whitty, A.3
  • 11
    • 49749153447 scopus 로고    scopus 로고
    • The role of GDNF family ligand signalling in the differentiation of sympathetic and dorsal root ganglion neurons
    • U. Ernsberger The role of GDNF family ligand signalling in the differentiation of sympathetic and dorsal root ganglion neurons Cell Tissue Res. 333 2008 353 371
    • (2008) Cell Tissue Res. , vol.333 , pp. 353-371
    • Ernsberger, U.1
  • 12
    • 0032488668 scopus 로고    scopus 로고
    • Identification and characterization of GFRα-3, a novel co-receptor belonging to the glial cell line-derived neurotrophic receptor family
    • DOI 10.1074/jbc.273.6.3502
    • C.A. Worby, Q.C. Vega, H.H. Chao, A.F. Seasholtz, R.C. Thompson, and J.E. Dixon Identification and characterization of GFRalpha-3, a novel co-receptor belonging to the glial cell line-derived neurotrophic receptor family J. Biol. Chem. 273 1998 3502 3508 (Pubitemid 28109772)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.6 , pp. 3502-3508
    • Worby, C.A.1    Vega, Q.C.2    Chao, H.H.-J.3    Seasholtz, A.F.4    Thompson, R.C.5    Dixon, J.E.6
  • 14
    • 0031594917 scopus 로고    scopus 로고
    • GFRalpha-3, a protein related to GFRalpha-1, is expressed in developing peripheral neurons and ensheathing cells
    • J. Widenfalk, A. Tomac, E. Lindqvist, B. Hoffer, and L. Olson GFRalpha-3, a protein related to GFRalpha-1, is expressed in developing peripheral neurons and ensheathing cells Eur. J. Neurosci. 10 1998 1508 1517
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 1508-1517
    • Widenfalk, J.1    Tomac, A.2    Lindqvist, E.3    Hoffer, B.4    Olson, L.5
  • 18
    • 67649862000 scopus 로고    scopus 로고
    • HSV-mediated transfer of artemin overcomes myelin inhibition to improve outcome after spinal cord injury
    • Z. Zhou, X. Peng, D.J. Fink, and M. Mata HSV-mediated transfer of artemin overcomes myelin inhibition to improve outcome after spinal cord injury Mol. Ther. 17 2009 1173 1179
    • (2009) Mol. Ther. , vol.17 , pp. 1173-1179
    • Zhou, Z.1    Peng, X.2    Fink, D.J.3    Mata, M.4
  • 19
    • 33749557162 scopus 로고    scopus 로고
    • Protection by GDNF and other trophic factors against the dopamine-depleting effects of neurotoxic doses of methamphetamine
    • DOI 10.1196/annals.1369.024, Cellular and Molecular Mechanisms of Drugs of Abuse and Neurotoxicity: Cocaine, GHB, and Substituted Amphetamines
    • W.A. Cass, L.E. Peters, M.E. Harned, and K.B. Seroogy Protection by GDNF and other trophic factors against the dopamine-depleting effects of neurotoxic doses of methamphetamine Ann. NY Acad. Sci. 1074 2006 272 281 (Pubitemid 44532830)
    • (2006) Annals of the New York Academy of Sciences , vol.1074 , pp. 272-281
    • Cass, W.A.1    Peters, L.E.2    Harned, M.E.3    Seroogy, K.B.4
  • 21
    • 0142106351 scopus 로고    scopus 로고
    • Novel functions and signalling pathways for GDNF
    • DOI 10.1242/jcs.00786
    • H. Sariola, and M. Saarma Novel functions and signalling pathways for GDNF J. Cell Sci. 116 2003 3855 3862 (Pubitemid 37279301)
    • (2003) Journal of Cell Science , vol.116 , Issue.19 , pp. 3855-3862
    • Sariola, H.1    Saarma, M.2
  • 22
    • 0034947940 scopus 로고    scopus 로고
    • Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase
    • M. Geiser, R. Cbe, D. Drewello, and R. Schmitz Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase BioTechniques 31 2001 88 92 (Pubitemid 32645915)
    • (2001) BioTechniques , vol.31 , Issue.1 , pp. 88-92
    • Geiser, M.1    Cebe, R.2    Drewello, D.3    Schmitz, R.4
  • 23
    • 81955167980 scopus 로고    scopus 로고
    • Exceptional stability of Artemin neurotrophic factor dimers: Effects of temperature, pH, buffer and storage conditions on protein integrity and activity
    • 10.1007/s12010-011-9354-4
    • W. Bruinzeel, and S. Masure Exceptional stability of Artemin neurotrophic factor dimers: Effects of temperature, pH, buffer and storage conditions on protein integrity and activity Appl. Biochem. Biotechnol. 2011 10.1007/s12010-011-9354-4
    • (2011) Appl. Biochem. Biotechnol.
    • Bruinzeel, W.1    Masure, S.2
  • 24
    • 0025281866 scopus 로고
    • Study of strong to ultratight protein interactions using differential scanning calorimetry
    • DOI 10.1021/bi00481a024
    • J.F. Brandts, and L.N. Lin Study of strong to ultratight protein interactions using differential scanning calorimetry Biochemistry 29 1990 6927 6940 (Pubitemid 20225495)
    • (1990) Biochemistry , vol.29 , Issue.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.-N.2
  • 25
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using thermofluor
    • DOI 10.1021/bi048135v
    • D. Matulis, J.K. Kranz, F.R. Salemme, and M.J. Todd Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor Biochemistry 44 2005 5258 5266 (Pubitemid 40471238)
    • (2005) Biochemistry , vol.44 , Issue.13 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 27
    • 29344475982 scopus 로고    scopus 로고
    • Comparison of SUMO fusion technology with traditional gene fusion systems: Enhanced expression and solubility with SUMO
    • DOI 10.1110/ps.051812706
    • J.G. Marblestone, S.C. Edavettal, Y. Lim, P. Lim, X. Zuo, and T.R. Butt Comparison of SUMO fusion technology with traditional gene fusion systems: enhanced expression and solubility with SUMO Protein Sci. 15 2006 182 189 (Pubitemid 43004245)
    • (2006) Protein Science , vol.15 , Issue.1 , pp. 182-189
    • Marblestone, J.G.1    Edavettal, S.C.2    Lim, Y.3    Lim, P.4    Zuo, X.5    Butt, T.R.6
  • 28
    • 0027285510 scopus 로고
    • GDNF: A glial cell line-derived neurotrophic factor for midbrain dopaminergic neurons
    • L.F. Lin, D.H. Doherty, J.D. Lile, S. Bektesh, and F. Collins GDNF: a glial cell line-derived neurotrophic factor for midbrain dopaminergic neurons Science 260 1993 1072 1073
    • (1993) Science , vol.260 , pp. 1072-1073
    • Lin, L.F.1    Doherty, D.H.2    Lile, J.D.3    Bektesh, S.4    Collins, F.5
  • 30
  • 33
    • 33744789162 scopus 로고    scopus 로고
    • Structure of Artemin Complexed with Its Receptor GFRα3: Convergent Recognition of Glial Cell Line-Derived Neurotrophic Factors
    • DOI 10.1016/j.str.2006.05.010, PII S0969212606002279
    • X. Wang, R.H. Baloh, J. Milbrandt, and K.C. Garcia Structure of artemin complexed with its receptor GFRalpha3: convergent recognition of glial cell line-derived neurotrophic factors Structure 14 2006 1083 1092 (Pubitemid 43831668)
    • (2006) Structure , vol.14 , Issue.6 , pp. 1083-1092
    • Wang, X.1    Baloh, R.H.2    Milbrandt, J.3    Garcia, K.C.4
  • 35
    • 0030475462 scopus 로고    scopus 로고
    • Glial cell line-derived neurotrophic factor: Selective reduction of the intermolecular disulfide linkage and characterization of its disulfide structure
    • DOI 10.1021/bi9605550
    • M. Haniu, J. Hui, Y. Young, J. Le, V. Katta, R. Lee, G. Shimamoto, and M.F. Rohde Glial cell line-derived neurotrophic factor: selective reduction of the intermolecular disulfide linkage and characterization of its disulfide structure Biochemistry 35 1996 16799 16805 (Pubitemid 27020526)
    • (1996) Biochemistry , vol.35 , Issue.51 , pp. 16799-16805
    • Haniu, M.1    Hui, J.2    Young, Y.3    Le, J.4    Katta, V.5    Lee, R.6    Shimamoto, G.7    Rohde, M.F.8
  • 36
    • 0030989670 scopus 로고    scopus 로고
    • X-ray structure of glial cell-derived neurotrophic factor at 1.9 A resolution and implications for receptor binding
    • DOI 10.1038/nsb0697-435
    • C. Eigenbrot, and N. Gerber X-ray structure of glial cell-derived neurotrophic factor at 1.9 resolution and implications for receptor binding Nat. Struct. Biol. 4 1997 435 438 (Pubitemid 27263594)
    • (1997) Nature Structural Biology , vol.4 , Issue.6 , pp. 435-438
    • Eigenbrot, C.1    Gerber, N.2
  • 37
    • 0036187342 scopus 로고    scopus 로고
    • Effect of the intermolecular disulfide bond on the conformation and stability of glial cell line-derived neurotrophic factor
    • T. Li, H. Yamane, T. Arakawa, L.O. Narhi, and J. Philo Effect of the intermolecular disulfide bond on the conformation and stability of glial cell line-derived neurotrophic factor Protein Eng. 15 2002 59 64 (Pubitemid 34184343)
    • (2002) Protein Engineering , vol.15 , Issue.1 , pp. 59-64
    • Li, T.1    Yamane, H.2    Arakawa, T.3    Narhi, L.O.4    Philo, J.5
  • 39
    • 0037044749 scopus 로고    scopus 로고
    • The cystine knot promotes folding and not thermodynamic stability in vascular endothelial growth factor
    • DOI 10.1074/jbc.M206438200
    • Y.A. Muller, C. Heiring, R. Misselwitz, K. Welfle, and H. Welfle The cystine knot promotes folding and not thermodynamic stability in vascular endothelial growth factor J. Biol. Chem. 277 2002 43410 43416 (Pubitemid 35285729)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 43410-43416
    • Muller, Y.A.1    Heiring, C.2    Misselwitz, R.3    Welfle, K.4    Welfle, H.5
  • 40
    • 15244362275 scopus 로고    scopus 로고
    • Extraordinarily stable disulfide-linked homodimer of human growth hormone
    • DOI 10.1110/ps.041048805
    • A.L. Grigorian, J.J. Bustamante, P. Hernandez, A.O. Martinez, and L.S. Haro Extraordinarily stable disulfide-linked homodimer of human growth hormone Prot. Sci. 14 2005 902 913 (Pubitemid 40389359)
    • (2005) Protein Science , vol.14 , Issue.4 , pp. 902-913
    • Grigorian, A.L.1    Bustamante, J.J.2    Hernandez, P.3    Martinez, A.O.4    Haro, L.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.