Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl

PL EN


Preferences help
enabled [disable] Abstract
Number of results
2004 | 51 | 1 | 153-160

Article title

Effect of antisense peptide binding on the dimerization of human cystatin C - gel electrophoresis and molecular modeling studies.

Content

Title variants

Languages of publication

EN

Abstracts

EN
Human cystatin C (HCC) shows a tendency to dimerize. This process is particularly easy in the case of the L68Q HCC mutant and might lead to formation of amyloid deposits in brain arteries of young adults. Our purpose was to find ligands of monomeric HCC that can prevent its dimerization. Eleven antisense peptide ligands of monomeric HCC were designed and synthesized. The influence of these ligands on HCC dimerization was studied using gel electrophoresis and molecular modeling methods. The results suggest that all the designed peptides interact with monomeric HCC facilitating its dimerization rather than preventing it.

Year

Volume

51

Issue

1

Pages

153-160

Physical description

Dates

published
2004
received
2003-10-31
revised
2004-03-02
accepted
2004-03-09

Contributors

  • Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland
  • Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland
  • Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland
  • Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland
  • Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland
author
  • Department of Clinical Chemistry, University Hospital, Lund, Sweden
  • Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland

References

  • Abrahamson M. (1996) Scand J Clin Lab Invest Suppl.; 226: 47-56.
  • Abrahamson M, Dalbege H, Olafsson I, Carlsen S, Grubb A. (1988) FEBS Lett.; 236: 14-8.
  • Baranyi L, Campbell W, Ohshima K, Fujimoto S, Boros M, Okada H. (1995) Nat Med.; 1: 894-901.
  • Blalock JE. (1990) Trends Biotechnol.; 8: 140-4.
  • Blalock JE. (1995)Nat Med.; 1: 876-8.
  • Blalock JE. (1999) Cell Mol Life Sci.; 55: 513-8.
  • Bode W, Engh R, Musil D, Thiele U, Huber R, Karshikov A, Brzin J, Kos J, Turk V. (1988) EMBO J.; 7: 2593-9.
  • Case DA, Pearlman DA, Caldwell JW, Cheatham III TE, Ross WS, Simmerling D, Darden T, Merz KM, Stanton RV, Cheng A, Vincent JJ, Crowley M, Ferguson DM, Radmer R, Seibel GL, Singh UC, Wiener P, Kollman PA. (1997) Amber 5.0. University of California, San Fransisco
  • Dieckmann T, Mitschang L, Hofmann M, Kos J, Turk V, Auerswald EA, Jaenicke R, Oschkinat H. (1993) J Mol Biol.; 234: 1048-59.
  • Ekiel I, Abrahamson M. (1996) J Biol Chem.; 271: 1314-21.
  • Ekiel I, Abrahamson M, Fulton DB, Lindahl P, Storer AC, Levadoux W, Lafrance M, Labelle S, Pomerleau Y, Groleau D, LeSauter L, Gehring K. (1997) J Mol Biol.; 271: 266-77.
  • Engh RA, Dieckmann T, Bode W, Auerswald EA, Turk V, Huber R, Oschkinat H. (1993) J Mol Biol.; 234: 1060-9.
  • Essman U, Perera L, Berkowitz ML, Darden TA, Lee H, Pedersen L. (1995) J Chem Phys.; 103: 8577-93.
  • Gerhatz B, Ekiel I, Abrahamson M. (1998) Biochemistry.; 37: 17309-17.
  • Ghiso J, Jensson O, Frangione B. (1986) Proc Natl Acad Sci U S A.; 83: 2974-8.
  • Ghiso J, Saball E, Leoni J, Rostagno A, Frangione B. (1990) Proc Natl Acad Sci USA.; 87: 1288-91.
  • Grubb AO. (2000) Adv Clin Chem.; 35: 63-99.
  • Grzonka Z, Jankowska E, Kasprzykowski F, Kasprzykowska R, Łankiewicz L, Wiczk W, Wieczerzak E, Ciarkowski J, Drabik P, Janowski R, Kozak M, Jaskólski M, Grubb AO. (2001) Acta Biochim Polon.; 48: 1-20.
  • Heal JR, Bino S, Ray KP, Christie G, Miller AD, Raynes JG. (1999) Mol Immunol.; 36: 1141-8.
  • Heal JR, Bino S, Roberts GW, Raynes JG, Miller AD. (2002) Chembiochem.; 3: 76-85.
  • Janowski R, Kozak M, Jankowska E, Grzonka Z, Grubb AO, Abrahamson M, Jaskólski M. (2001) Nat Struct Biol.; 8: 316-20.
  • Jaskólski M. (2001) Acta Biochim Polon. 48: 807-27.
  • Jensson O, Gudmundsson G, Arnason A, Blondal H, Petursdottir I, Thorsteinsson L, Grubb AO, Lofberg H, Cohen D, Frangione B. (1987) Acta Neurol Scand.; 76: 102-14.
  • Jeppsson JO, Laurel CB, Franzen B. (1979) Clin Chem.; 25: 629-38.
  • Jerela R, Zerovnik E. (1999) J Mol Biol.; 291: 1079-89.
  • Koradi R, Billeter M, Wütrich K. (1996) J Mol Graph.; 14: 51-5, 29-32.
  • Kyte J, Doolittle RF. (1982) J Mol Biol.; 157: 105-32.
  • Martin JR, Craven CJ, Jerala R, Kroon-Zitko L, Zerovnik E, Turk V, Waltho JP. (1995) J Mol Biol.; 246: 331-43.
  • McGee AW, Dakoji SR, Olsen O, Bredt DS, Lim WA, Prehoda KE. (2001) Mol Cell.; 8: 1291-301.
  • Mekler LB. (1969) Biofizika.; 14: 581-4.
  • Olafsson I, Grubb AO. (2000) Amyloid.; 7: 70-9.
  • Saint-Jean AP, Phillips KR, Creighton DJ, Stone MJ. (1998) Biochemistry.; 37: 10345-53.
  • Sautebin L, Rombola L, Di Rosa M, Caliendo G, Perissutti E, Grieco P, Severino B, Santagada V. (2000) Eur J Med Chem.; 35: 727-32.
  • Schymkowitz JW, Rousseau F, Wilkinson HR, Friedler A, Itzhaki LS. (2001) Nat Struct Biol.; 8: 888-92.
  • Staniforth RA, Giannini S, Higgins LD, Conroy MJ, Hounslow AM, Jerala R, Craven CJ, Waltho JP. (2001) EMBO J.; 20: 4774-81.
  • Stachowiak K, Tokmina M, Karpińska A, Sosnowska R, Wiczk W. (2004) Acta Biochim Polon.; 51: (in press).
  • Stubbs MT, Laber B, Bode W, Huber R, Jerala R, Lenarcic B, Turk V. (1990) EMBO J.; 9: 1939-47.
  • SYBYL ver. 6.6 2000 Tripos, Inc.
  • Zhao R, Yu X, Liu H, Zhai L, Xiong S, Su T, Liu S. (2001) J Chrom A.; 913: 421-28.

Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.bwnjournal-article-abpv51i1p153kz
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.