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

• Autorzy: Stachowiak K. , Rodziewicz-Motowidlo S. , Sosnowska R. , Kasprzykowski F. , Lankiewicz L. , Grubb A. , Grzonka Z.
• Języki publikacji: EN

Abstrakty

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.

Słowa kluczowe

EN

cystatin C; human cystatin C; dimerization; antisense peptide; gel electrophoresis; molecular dynamics

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2004
• Tom: 51
• Numer: 1
• Opis fizyczny: p.153-160,fig.,ref.

Twórcy

autor

Stachowiak K.

• University of Gdansk, Sobieskiego 18, 80-952 Gdansk, Poland

autor

Rodziewicz-Motowidlo S.

autor

Sosnowska R.

autor

Kasprzykowski F.

autor

Lankiewicz L.

autor

Grubb A.

autor

Grzonka Z.

Bibliografia

• Abrahamson M. (1996) Scand J Clin Lab Invest Suppl.; 226: 47-56.
• Abrahamson M, Dalbege H, Olafsson I, Carlsen S, Grubb A. (1988) FEBSLett; 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 US 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, Lankiewicz L, Wiczk W, Wieczerzak E, Ciarkowski J, Drabik P, Janowski R, Kozak M, Jaskolski 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, Jaskolski M. (2001) Nat Struct Biol.; 8: 316-20.
• Jaskolski 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) JMolBiol.; 291: 1079-89.
• Koradi R, Billeter M, Wutrich K. (1996) JMol Graph.; 14: 51-5, 29-32.
• Kyte J, Doolittle RF. (1982) JMol Biol.; 157: 105-32.
• Martin JR, Craven CJ, Jerala R, Kroon-Zitko L, Zerovnik E, Turk V, Waltho JP. (1995) JMol 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, Karpinska 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.