Identification of fibronectin type I domains as amyloid-binding modules on tissue-type plasminogen activator and three homologs

References

• Syrovets T, Tippler B, Rieks M, Simmet T. Plasmin is a potent and specific chemoattractant for human peripheral monocytes acting via a cyclic guanosine monophosphate-dependent pathway. Blood 1997; 89: 4574–4583
   PubMed Web of Science ®Google Scholar
• Syrovets T, Jendrach M, Rohwedder A, Schule A, Simmet T. Plasmin-induced expression of cytokines and tissue factor in human monocytes involves AP-1 and IKKbeta-mediated NF-kappaB activation. Blood 2001; 97: 3941–3950
   PubMed Web of Science ®Google Scholar
• Baricos W H, Cortez S L, el-Dahr S S, Schnaper H W. ECM degradation by cultured human mesangial cells is mediated by a PA/plasmin/MMP-2 cascade. Kidney Int 1995; 47: 1039–1047
   PubMed Web of Science ®Google Scholar
• Ling C, Zou T, Hsiao Y, Tao X, Chen Z L, Strickland S, Song H. Disruption of tissue plasminogen activator gene reduces macrophage migration. Biochem Biophys Res Commun 2006; 349: 906–912
   Google Scholar
• Brodsky S, Chen J, Lee A, Akassoglou K, Norman J, Goligorsky M S. Plasmin-dependent and -independent effects of plasminogen activators and inhibitor-1 on ex vivo angiogenesis. Am J Physiol Heart Circ Physiol 2001; 281: H1784–H1792
   Google Scholar
• Syrovets T, Simmet T. Novel aspects and new roles for the serine protease plasmin. Cell Mol Life Sci 2004; 61: 873–885
   PubMed Web of Science ®Google Scholar
• Galantai R, Modos K, Fidy J, Kolev K, Machovich R. Structural basis of the cofactor function of denatured albumin in plasminogen activation by tissue-type plasminogen activator. Biochem Biophys Res Commun 2006; 341: 736–741
   PubMedGoogle Scholar
• Bobbink I W, Tekelenburg W L, Sixma J J, de Boer H C, Banga J D, de Groot P G. Glycated proteins modulate tissue-plasminogen activator-catalyzed plasminogen activation. Biochem Biophys Res Commun 1997; 240: 595–601
   Google Scholar
• Machovich R, Owen W G. Denatured proteins as cofactors for plasminogen activation. Arch Biochem Biophys 1997; 344: 343–349
   PubMed Web of Science ®Google Scholar
• Haddeland U, Bennick A, Brosstad F. Stimulating effect on tissue-type plasminogen activator – a new and sensitive indicator of denatured fibrinogen. Thromb Res 1995; 77: 329–336
   Google Scholar
• Haddeland U, Sletten K, Bennick A, Nieuwenhuizen W, Brosstad F. Aggregated, conformationally changed fibrinogen exposes the stimulating sites for t-PA-catalysed plasminogen activation. Thromb Haemost 1996; 75: 326–331
   Google Scholar
• Reijerkerk A, Mosnier L O, Kranenburg O, Bouma B N, Carmeliet P, Drixler T, Meijers J C, Voest E E, Gebbink M F. Amyloid endostatin induces endothelial cell detachment by stimulation of the plasminogen activation system. Mol Cancer Res 2003; 1: 561–568
   Google Scholar
• Kranenburg O, Bouma B, Kroon-Batenburg L M, Reijerkerk A, Wu Y P, Voest E E, Gebbink M F. Tissue-type plasminogen activator is a multiligand cross-beta structure receptor. Curr Biol 2002; 12: 1833–1839
   PubMed Web of Science ®Google Scholar
• Maas C, Hermeling S, Bouma B, Jiskoot W, Gebbink M F. A role for protein misfolding in immunogenicity of biopharmaceuticals. J Biol Chem 2007; 282: 2229–2236
   PubMed Web of Science ®Google Scholar
• Herczenik E, Bouma B, Korporaal S J, Strangi R, Zeng Q, Gros P, Van E M, Van Berkel T J, Gebbink M F, Akkerman J W. Activation of human platelets by misfolded proteins. Arterioscler Thromb Vasc Biol 2007; 27: 1657–1665
   PubMed Web of Science ®Google Scholar
• Ursini F, Davies K J, Maiorino M, Parasassi T, Sevanian A. Atherosclerosis: another protein misfolding disease?. Trends Mol Med 2002; 8: 370–374
   PubMed Web of Science ®Google Scholar
• Lee J Y, Kweon H S, Cho E, Lee J Y, Byun H R, Kim D H, Kim Y H, Han P L, Koh J Y. Upregulation of tPA/plasminogen proteolytic system in the periphery of amyloid deposits in the Tg2576 mouse model of Alzheimer's disease. Neurosci Lett 2007; 423: 82–87
   PubMedGoogle Scholar
• Melchor J P, Pawlak R, Strickland S. The tissue plasminogen activator-plasminogen proteolytic cascade accelerates amyloid-beta (Abeta) degradation and inhibits Abeta-induced neurodegeneration. J Neurosci 2003; 23: 8867–8871
   PubMed Web of Science ®Google Scholar
• Periz G, Fortini M E. Proteolysis in Alzheimer's disease. Can plasmin tip the balance?. EMBO Rep 2000; 1: 477–478
   Google Scholar
• Siao C J, Tsirka S E. Tissue plasminogen activator mediates microglial activation via its finger domain through annexin II. J Neurosci 2002; 22: 3352–3358
   PubMed Web of Science ®Google Scholar
• Tucker H M, Kihiko-Ehmann M, Wright S, Rydel R E, Estus S. Tissue plasminogen activator requires plasminogen to modulate amyloid-beta neurotoxicity and deposition. J Neurochem 2000; 75: 2172–2177
   PubMedGoogle Scholar
• Tucker H M, Kihiko M, Caldwell J N, Wright S, Kawarabayashi T, Price D, Walker D, Scheff S, McGillis J P, Rydel R E, Estus S. The plasmin system is induced by and degrades amyloid-beta aggregates. J Neurosci 2000; 20: 3937–3946
   PubMedGoogle Scholar
• Xanthopoulos K, Paspaltsis I, Apostolidou V, Petrakis S, Siao C J, Kalpatsanidis A, Grigoriadis N, Tsaftaris A, Tsirka S E, Sklaviadis T. Tissue plasminogen activator in brain tissues infected with transmissible spongiform encephalopathies. Neurobiol Dis 2005; 20: 519–527
   PubMed Web of Science ®Google Scholar
• Jaroniec C P, MacPhee C E, Astrof N S, Dobson C M, Griffin R G. Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril. Proc Natl Acad Sci U S A 2002; 99: 16748–16753
   PubMed Web of Science ®Google Scholar
• Yamada M, Kadoya Y, Kasai S, Kato K, Mochizuki M, Nishi N, Watanabe N, Kleinman H K, Yamada Y, Nomizu M. Ile-Lys-Val-Ala-Val (IKVAV)-containing laminin alpha1 chain peptides form amyloid-like fibrils. FEBS Lett 2002; 530: 48–52
   Google Scholar
• Schielen J G, Adams H P, Voskuilen M, Tesser G J, Nieuwenhuizen W. Structural requirements of position A alpha-157 in fibrinogen for the fibrin-induced rate enhancement of the activation of plasminogen by tissue-type plasminogen activator. Biochem J 1991; 276: 655–659
   Google Scholar
• Johannessen M, Diness V, Pingel K, Petersen L C, Rao D, Lioubin P, O'Hara P, Mulvihill E. Fibrin affinity and clearance of t-PA deletion and substitution analogues. Thromb Haemost 1990; 63: 54–59
   Google Scholar
• Gebbink M F, Zondag G C, Koningstein G M, Feiken E, Wubbolts R W, Moolenaar W H. Cell surface expression of receptor protein tyrosine phosphatase RPTP mu is regulated by cell-cell contact. J Cell Biol 1995; 131: 251–260
   PubMed Web of Science ®Google Scholar
• van Zonneveld A J, Veerman H, Pannekoek H. On the interaction of the finger and the kringle-2 domain of tissue-type plasminogen activator with fibrin. Inhibition of kringle-2 binding to fibrin by epsilon-amino caproic acid. J Biol Chem 1986; 261: 14214–14218
   PubMed Web of Science ®Google Scholar
• Rostagno A, Williams M J, Baron M, Campbell I D, Gold L I. Further characterization of the NH2-terminal fibrin-binding site on fibronectin. J Biol Chem 1994; 269: 31938–31945
   Google Scholar
• Rostagno A A, Schwarzbauer J E, Gold L I. Comparison of the fibrin-binding activities in the N- and C-termini of fibronectin. Biochem J 1999; 338: 375–386
   Google Scholar
• Schnolzer M, Alewood P, Jones A, Alewood D, Kent S B. In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences. Int J Pept Protein Res 1992; 40: 180–193
   PubMedGoogle Scholar
• Dawson P E, Muir T W, Clark-Lewis I, Kent S B. Synthesis of proteins by native chemical ligation. Science 1994; 266: 776–779
   PubMed Web of Science ®Google Scholar
• Hackeng T M, Griffin J H, Dawson P E. Protein synthesis by native chemical ligation: expanded scope by using straightforward methodology. Proc Natl Acad Sci USA 1999; 96: 10068–10073
   Google Scholar
• Bobbink I W, de Boer H C, Tekelenburg W L, Banga J D, de Groot P G. Effect of extracellular matrix glycation on endothelial cell adhesion and spreading: involvement of vitronectin. Diabetes 1997; 46: 87–93
   Google Scholar
• Renne T, Pozgajova M, Gruner S, Schuh K, Pauer H U, Burfeind P, Gailani D, Nieswandt B. Defective thrombus formation in mice lacking coagulation factor XII. J Exp Med 2005; 202: 271–281
   PubMed Web of Science ®Google Scholar
• Renne T, Nieswandt B, Gailani D. The intrinsic pathway of coagulation is essential for thrombus stability in mice. Blood Cells Mol Dis 2006; 36: 148–151
   PubMed Web of Science ®Google Scholar
• Miyazawa K, Shimomura T, Kitamura N. Activation of hepatocyte growth factor in the injured tissues is mediated by hepatocyte growth factor activator. J Biol Chem 1996; 271: 3615–3618
   PubMedGoogle Scholar
• Itoh H, Naganuma S, Takeda N, Miyata S, Uchinokura S, Fukushima T, Uchiyama S, Tanaka H, Nagaike K, Shimomura T, Miyazawa K, Yamada G, Kitamura N, Koono M, Kataoka H. Regeneration of injured intestinal mucosa is impaired in hepatocyte growth factor activator-deficient mice. Gastroenterology 2004; 127: 1423–1435
   PubMedGoogle Scholar
• Matsubara Y, Ichinose M, Yahagi N, Tsukada S, Oka M, Miki K, Kimura S, Omata M, Shiokawa K, Kitamura N, Kaneko Y, Fukamachi H. Hepatocyte growth factor activator: a possible regulator of morphogenesis during fetal development of the rat gastrointestinal tract. Biochem Biophys Res Commun 1998; 253: 477–484
   Google Scholar
• Maas C, Govers-Riemslag J WP, Bouma B, Schiks B, Hazenberg B PC, Lokhorst H M, Hammarstrõm P, ten Cate H, de Groot P G, Bouma B N, Gebbink M FBG. Factor XII is activated by misfolded proteins, which leads to kallikrein formation without initiating coagulation. J Clin Invest 2008, in press
   Google Scholar
• Shibayama Y, Joseph K, Nakazawa Y, Ghebreihiwet B, Peerschke E I, Kaplan A P. Zinc-dependent activation of the plasma kinin-forming cascade by aggregated beta amyloid protein. Clin Immunol 1999; 90: 89–99
   PubMed Web of Science ®Google Scholar
• Bouma B, Kroon-Batenburg L M, Wu Y P, Brunjes B, Posthuma G, Kranenburg O, de Groot P G, Voest E E, Gebbink M F. Glycation induces formation of amyloid cross-beta structure in albumin. J Biol Chem 2003; 278: 41810–41819
   PubMed Web of Science ®Google Scholar
• Mao Y, Ootaka T, Saito T, Sato H, Sato T, Ito S. The involvement of advanced glycation endproducts (AGEs) in renal injury of diabetic glomerulosclerosis: association with phenotypic change in renal cells and infiltration of immune cells. Clin Exp Nephrol 2003; 7: 201–209
   Google Scholar
• Hudry-Clergeon G, Freyssinet J M, Torbet J, Marx J. Orientation of fibrin in strong magnetic fields. Ann N Y Acad Sci 1983; 408: 380–387
   Google Scholar
• Downing A K, Driscoll P C, Harvey T S, Dudgeon T J, Smith B O, Baron M, Campbell I D. Solution structure of the fibrin binding finger domain of tissue-type plasminogen activator determined by 1H nuclear magnetic resonance. J Mol Biol 1992; 225: 821–833
   PubMed Web of Science ®Google Scholar
• Ledesma M D, Da Silva J S, Crassaerts K, Delacourte A, De S B, Dotti C G. Brain plasmin enhances APP alpha-cleavage and Abeta degradation and is reduced in Alzheimer's disease brains. EMBO Rep 2000; 1: 530–535
   PubMedGoogle Scholar
• Paul J, Strickland S, Melchor J P. Fibrin deposition accelerates neurovascular damage and neuroinflammation in mouse models of Alzheimer's disease. J Exp Med 2007; 204: 1999–2008
   PubMed Web of Science ®Google Scholar
• Van Nostrand W E, Melchor J, Wagner M, Davis J. Cerebrovascular smooth muscle cell surface fibrillar A beta. Alteration of the proteolytic environment in the cerebral vessel wall. Ann N Y Acad Sci 2000; 903: 89–96
   Google Scholar
• Medina M G, Ledesma M D, Dominguez J E, Medina M, Zafra D, Alameda F, Dotti C G, Navarro P. Tissue plasminogen activator mediates amyloid-induced neurotoxicity via Erk1/2 activation. EMBO J 2005; 24: 1706–1716
   PubMedGoogle Scholar
• Yasuhara O, Walker D G, McGeer P L. Hageman factor and its binding sites are present in senile plaques of Alzheimer's disease. Brain Res 1994; 654: 234–240
   Google Scholar
• Bergamaschini L, Parnetti L, Pareyson D, Canziani S, Cugno M, Agostoni A. Activation of the contact system in cerebrospinal fluid of patients with Alzheimer disease. Alzheimer Disease & Associated Disorders 1998; 12: 102–108
   PubMed Web of Science ®Google Scholar
• Bergamaschini L, Donarini C, Gobbo G, Parnetti L, Gallai V. Activation of complement and contact system in Alzheimer's disease. Mech Ageing Develop 2001; 122: 1971–1983
   Google Scholar
• Miklossy J, Taddei K, Martins R, Escher G, Kraftsik R, Pillevuit O, Lepori D, Campiche M. Alzheimer disease: curly fibers and tangles in organs other than brain. J Neuropathol Exp Neurol 1999; 58: 803–814
   PubMed Web of Science ®Google Scholar
• van Duinen S G, Maat-Schieman M L, Bruijn J A, Haan J, Roos R A. Cortical tissue of patients with hereditary cerebral hemorrhage with amyloidosis (Dutch) contains various extracellular matrix deposits. Lab Invest 1995; 73: 183–189
   PubMed Web of Science ®Google Scholar
• Yamada T, Tsujioka Y, Taguchi J, Takahashi M, Tsuboi Y, Shimomura T. White matter astrocytes produce hepatocyte growth factor activator inhibitor in human brain tissues. Exp Neurol 1998; 153: 60–64
   Google Scholar
• Shikano M, Kushimoto H, Hasegawa H, Tomita M, Hasegawa M, Murakami K, Kawashima S. Usefulness of serum hepatocyte growth factor for the diagnosis of amyloidosis. Intern Med 2000; 39: 715–719
   PubMed Web of Science ®Google Scholar
• Williams M J, Phan I, Baron M, Driscoll P C, Campbell I D. Secondary structure of a pair of fibronectin type 1 modules by two-dimensional nuclear magnetic resonance. Biochemistry 1993; 32: 7388–7395
   Google Scholar
• Limper A H, Quade B J, LaChance R M, Birkenmeier T M, Rangwala T S, McDonald J A. Cell surface molecules that bind fibronectin's matrix assembly domain. J Biol Chem 1991; 266: 9697–9702
   Google Scholar
• Hocking D C, Sottile J, Keown-Longo P J. Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin. J Biol Chem 1994; 269: 19183–19187
   PubMed Web of Science ®Google Scholar
• Ohashi T, Erickson H P. Domain unfolding plays a role in superfibronectin formation. J Biol Chem 2005; 280: 39143–39151
   Google Scholar
• Ingham K C, Brew S A, Huff S, Litvinovich S V. Cryptic self-association sites in type III modules of fibronectin. J Biol Chem 1997; 272: 1718–1724
   Google Scholar
• Litvinovich S V, Brew S A, Aota S, Akiyama S K, Haudenschild C, Ingham K C. Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module. J Mol Biol 1998; 280: 245–258
   PubMed Web of Science ®Google Scholar
• Schlunegger M P, Bennett M J, Eisenberg D. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv Protein Chem 1997; 50: 61–122
   PubMedGoogle Scholar
• Bennett M J, Schlunegger M P, Eisenberg D. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci 1995; 4: 2455–2468
   PubMed Web of Science ®Google Scholar
• Schwarz-Linek U, Pilka E S, Pickford A R, Kim J H, Hook M, Campbell I D, Potts J R. High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules. J Biol Chem 2004; 279: 39017–39025
   PubMed Web of Science ®Google Scholar
• Sagare A, Deane R, Bell R D, Johnson B, Hamm K, Pendu R, Marky A, Lenting P J, Wu Z, Zarcone T, Goate A, Mayo K, Perlmutter D, Coma M, Zhong Z, Zlokovic B V. Clearance of amyloid-beta by circulating lipoprotein receptors. Nat Med 2007; 13: 1029–1031
   PubMed Web of Science ®Google Scholar
• Bu G, Cam J, Zerbinatti C. LRP in amyloid-beta production and metabolism. Ann N Y Acad Sci 2006; 1086: 35–53
   Google Scholar
• Donahue J E, Flaherty S L, Johanson C E, Duncan JA, III, Silverberg G D, Miller M C, Tavares R, Yang W, Wu Q, Sabo E, Hovanesian V, Stopa E G. RAGE, LRP-1, and amyloid-beta protein in Alzheimer's disease. Acta Neuropathol (Berl) 2006; 112: 405–415
   PubMed Web of Science ®Google Scholar