Unwinding fibril formation of medin, the peptide of the most common form of human amyloid

Biochemical and Biophysical Research Communications

Volumn 361, Issue 4, 2007, Pages 822-828

  Larsson, Annika ^a   Söderberg, Linda ^b   Westermark, Gunilla T ^c   Sletten, Knut ^d   Engström, Ulla ^e   Tjernberg, Lars O ^b   Näslund, Jan ^b   Westermark, Per ^a  

^a UPPSALA UNIVERSITY   (Sweden)

^b KAROLINSKA INSTITUTE   (Sweden)

^c LINKÖPING UNIVERSITY   (Sweden)

^d UNIVERSITY OF OSLO   (Norway)

^e LUDWIG INSTITUTE FOR CANCER RESEARCH   (Sweden)

Author keywords

Amyloid; Fibril formation; Lactadherin; Medin

Indexed keywords

AMYLOID; CONGO RED; MEDIN PEPTIDE; PEPTIDE DERIVATIVE; PHENYLALANINE; THIOFLAVINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING ASSAY; CARBOXY TERMINAL SEQUENCE; ELECTRON MICROSCOPY; FLUORESCENCE; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEOMICS;

ALGORITHMS; AMINO ACID SEQUENCE; AMYLOID; ANTIGENS, SURFACE; HUMANS; MILK PROTEINS; MOLECULAR SEQUENCE DATA; PEPTIDES;

EID: 34547897456     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.06.187     Document Type: Article

References (25)

1. Merlini G., and Bellotti V. Molecular mechanisms of amyloidosis. N. Engl. J. Med. 349 (2003) 583-596
2. Westermark P. Aspects on human amyloid forms and their fibril polypeptides. FEBS J. 272 (2005) 5942-5949
3. Gillmore J.D., and Hawkins P.N. Drug insight: emerging therapies for amyloidosis. Nat. Clin. Pract. Nephrol. 2 (2006) 263-270
4. Häggqvist B., Näslund J., Sletten K., Westermark G.T., Mucchiano G., Tjernberg L.O., Nordstedt C., Engström U., and Westermark P. Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid. Proc. Natl. Acad. Sci. USA 96 (1999) 8669-8674
5. Peng S., Glennert J., and Westermark P. Medin-amyloid: a recently characterized age-associated arterial amyloid form affects mainly arteries in the upper part of the body. Amyloid 12 (2005) 96-102
6. Mucchiano G., Cornwell III G.G., and Westermark P. Senile aortic amyloid. Evidence for two distinct forms of localized deposits. Am. J. Pathol. 140 (1992) 871-877
7. Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., and Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416 (2002) 507-511
8. Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., and Glabe C.G. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300 (2003) 486-489
9. Chiti F., Stefani M., Taddei N., Ramponi G., and Dobson C.M. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424 (2003) 805-808
10. Tjernberg L., Hosia W., Bark N., Thyberg J., and Johansson J. Charge attraction and beta propensity are necessary for amyloid fibril formation from tetrapeptides. J. Biol. Chem. 277 (2002) 43243-43246
11. Kallberg Y., Gustafsson M., Persson B., Thyberg J., and Johansson J. Prediction of amyloid fibril-forming proteins. J. Biol. Chem. 276 (2001) 12945-12950
12. Gazit E. A possible role for pi-stacking in the self-assembly of amyloid fibrils. FASEB J. 16 (2002) 77-83
13. Bemporad F., Taddei N., Stefani M., and Chiti F. Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase. Protein Sci. 15 (2006) 862-870
14. Reches M., and Gazit E. Amyloidogenic hexapeptide fragment of medin: homology to functional islet amyloid polypeptide fragments. Amyloid 11 (2004) 81-89
15. Gazit E., Della Bruna P., Pieraccini S., and Colombo G. The molecular dynamics of assembly of the ubiquitous aortic medial amyloidal medin fragment. J. Mol. Graph. Model. 25 (2007) 903-911
16. Westermark G.T., Johnson K.H., and Westermark P. Staining methods for identification of amyloid in tissue. Methods Enzymol. 309 (1999) 3-25
17. Frank R. The SPOT-synthesis technique. Synthetic peptide arrays on membrane supports-principles and applications. J. Immunol. Methods 267 (2002) 13-26
18. Fernandez-Escamilla A.M., Rousseau F., Schymkowitz J., and Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 22 (2004) 1302-1306
19. Levine III H. Thioflavin T interaction with amyloid β-sheet structures. Amyloid 2 (1995) 1-6
20. Jarrett J.T., and Lansbury Jr. P.T. Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry 31 (1992) 12345-12352
21. Krebs M.R., Morozova-Roche L.A., Daniel K., Robinson C.V., and Dobson C.M. Observation of sequence specificity in the seeding of protein amyloid fibrils. Protein Sci. 13 (2004) 1933-1938
22. Hurshman A.R., White J.T., Powers E.T., and Kelly J.W. Transthyretin aggregation under partially denaturing conditions is a downhill polymerization. Biochemistry 43 (2004) 7365-7381
23. O'Nuallain B., Williams A.D., Westermark P., and Wetzel R. Seeding specificity in amyloid growth induced by heterologous fibrils. J. Biol. Chem. 279 (2004) 17490-17499
24. Larsson A., Peng S., Persson H., Rosenbloom J., Abrams W.R., Wassberg E., Thelin S., Sletten K., Gerwins P., and Westermark P. Lactadherin binds to elastin-a starting point for medin amyloid formation?. Amyloid 13 (2006) 78-85
25. Couto J.R., Taylor M.R., Godwin S.G., Ceriani R.L., and Peterson J.A. Cloning and sequence analysis of human breast epithelial antigen BA46 reveals an RGD cell adhesion sequence presented on an epidermal growth factor-like domain. DNA Cell Biol. 15 (1996) 281-286