Activity-dependent neurotrophic factor, ADNF, determines the structure characteristicsof Colivelin, a fusion protein of ADNF9 and Humanin analog

Journal of Peptide Science

Volumn 14, Issue 5, 2008, Pages 631-636

  Arakawa, Tsutomu ^a   Niikura, Takako ^b,d   Arisaka, Fumio ^c   Kita, Yoshiko ^b  

^a ALLIANCE PROTEIN LABORATORIES   (United States)

^b KEIO UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^c TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^d GEORGETOWN UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

ADNF; Circular dichroism; Colivelin; Fusion peptide; Humanin; Sedimentation analysis

Indexed keywords

ACTIVITY DEPENDENT NEUROTROPHIC FACTOR; ACTIVITY DEPENDENT NEUROTROPHIC FACTOR 9 HUMANIN FUSION PROTEIN; COLIVELIN; HYBRID PROTEIN; MONOMER; NEUROTROPHIC FACTOR; PHOSPHATE BUFFERED SALINE; WATER;

AMINO ACID COMPOSITION; ARTICLE; CIRCULAR DICHROISM; NEUROPROTECTION; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SEDIMENTATION RATE; STRUCTURE ANALYSIS; ULTRACENTRIFUGATION;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; DRUG STABILITY; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MULTIPROTEIN COMPLEXES; NERVE TISSUE PROTEINS; OLIGOPEPTIDES; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; ULTRACENTRIFUGATION;

EID: 44349146630     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.959     Document Type: Article

References (18)

1. Niikura T, Maruyama N, Hashimoto Y, Ito Y, Yamagishi Y, Matsuoka M, Takeuchi Y, Aiso S, Nishimoto I. V6421 APP-inducible neuronal cells: a model system for investigating Alzheimer's disorders. Biochem. Biophys. Res. Commun. 2000; 274: 445-454.
2. Hashimoto Y, Ito Y, Niikura T, Shao Z, Hata M, Oyama F, Nishimoto I. Mechanisms of neuroprotection by a novel rescue factor Humanin from Swedish mutant amyloid precursor protein. Biochem. Biophys. Res. Commun. 2001; 283: 460-468.
3. Hashimoto Y, Niikura T, Tajima H, Yasukawa T, Sudo H, Ito Y, Kita Y, Kawasumi M, Kouyama K, Doyu M, Sobue G, Koide T, Tsuji S, Lang J, Kurokawa K, Nishimoto I. A rescue factor abolishing neuronal cell death by a wide spectrum of familial Alzheimer's disease genes and Aβ. Proc. Natl. Acad. Sci. U.S.A. 2001; 98: 6336-6341.
4. Yamagishi Y, Hashimoto Y, Niikura T, Nishimoto I. Identification of essential amino acids in Humanin, a neuroprotective factor against Alzheimer's disease-relevant insults. Peptides 2003; 24: 585-595.
5. Terashita K, Hashimoto Y, Niikura T, Tajima H, Yamagishi Y, Ishizaka M, Kawasumi M, Chiba T, Kanekura K, Yamada M, Nawa M, Kita Y, Nishimoto I. Two serine residues distinctly regulate the rescue function of Humanin, an inhibiting factor of Alzheimer's disease-related neurotoxicity: functional potentiation by isomerization and dimerization. J. Neurochem. 2003; 85: 1521-1538.
6. Hashimoto Y, Niikura T, Ito Y, Sudo H, Hata M, Arakawa E, Abe Y, Kita Y, Nishimoto I. Detailed characterization of neuroprotection by a rescue factor Humanin against various Alzheimer's disease-relevant insults. J. Neurosci. 2001; 21: 9235-9245.
7. Jung SS, van Nostrand WE. Humanin rescues human cerebrovascular smooth muscle cells from Aβ-induced toxicity. J. Neurochem. 2003; 84: 266-272.
8. Niikuta T, Tajima H, Kita Y. Neuronal cell death in Alzheimer's disease and a Neuroprotective factor. humanin. Curr. Neuropharmacol. 2006; 4: 139-147.
9. Chiba T, Yamada M, Hashimoto Y, Sato M, Sasabe J, Kita Y, Terashita K, Aiso S, Nishimoto I, Matsuoka M. Development of a femtomolar-acting humanin derivative named Colivelin by attaching activity-dependent neurotrophic factor to its N terminus: characterization of Colivelin-mediated neuroprotection against Alzheimer's disease-related insults in vitro and in vivo. J. Neurosci. 2005; 25: 10252-10261.
10. Brenneman DE, Gozes I. A femtomolar-acting neuroprotective peptide. J Clin. Invest. 1996; 97: 2299-2307.
11. Brenneman DE, Hauser J, Neale E, Rubinraut S, Fridkin M, Davidson A, Gozes I. Activity-dependent neurotrophic factor: Structure-activity relationships of femtomolar-acting peptides. J. Biol. Chem. 1998; 285: 619-627.
12. Chiba T, Hashimoto Y, Tajima H, Yamada M, Koto R, Niikura T, Terashita K, Schulman H, Aiso S, Kita Y, Matsuoka M, Nishimoto I. Neuroprotective effect of activity-dependent neurotrophic factor, ADNF, against toxicity by familial amyotrophic lateral sclerosis-linked mutant SOD1 in vitro and in vivo. J. Neurosci. Res. 2004; 78: 542-552.
13. Arakawa T, Niikura T, Tajima H, Kita Y. The secondary structure analysis of a potent Ser14Gly analog of antiAlzheimer peptide, Humanin, by circular dichroism. J. Pept. Sci. 2006; 12: 639-642.
14. Arakawa T, Niikura T, Tajima T, Arisaka F, Kita Y. Structure analysis of activity dependent Neurotrophic factor 9 by circular dichroism and sedimentation equilibrium. J. Mol. Neurosci. 2007; 33: 262-267.
15. Laue TM, Shah BD, Ridgeway TM, Pelletier SL. Computer-aided interpretation of analytical sedimentation data for proteins. In Analytical Ultracentrifugation in Biochemistry and Polymer Science, Harding SE, Rowe AJ, Horton JC (eds). Royal Society of Chemistry: Cambridge, 1992; 90-125.
16. Schuck P. Size-distribution analysis of macromolecules by sedimentation velocity untracentrifugation and Lamm equation modeling. Biophys. J. 2000; 78: 1606-1619.
17. Howarth M, Chinnapen DJ, Gerrow K, Dorrestein PC, Grandy MR, Kelleher NL, El-Husseini A, Ting AY. A monovalent streptavidin with a single femtomo]ar biotin binding site. Nat. Methods 2006; 3: 267-273.
18. DeChancie J, Houk KN. The origins of femtomolar protein-ligand binding: hydrogen-bond cooperativity and desolvation energetics in the biotin-(strept)avidin binding site. J. Am. Chem, Soc. 2007; 129: 5419-5429.