Cellular Models – Transgenic mouse – Pre-clinical studies

  • Chafekar SM, Zwart R, Veerhuis R, Vanderstichele H, Baas F, Scheper W. Increased Aß1-42 production sensitizes neuroblastoma cells for ER stress toxicity. Curr Alzheimer Res 2008; 5: 469-474.
  • Cupers P, Bentahir M, Craessaerts K, Orlans I, Vanderstichele H, Saftig P, De Strooper B, Annaert W. The discrepancy between presenilin subcellular localization and γ-secretase processing of  amyloid precursor protein. J Cell biol 2001; 154: 731-740.
  • Hemmer K, Fransen L, Vanderstichele H, Vanmechelen E, Heuschling P. An in vitro model for the study of microglia-induced neurodegeneration: involvement of  nitric oxide and tumor necrosis factor-alpha. Neurochem Int 2001; 38: 557-565.
  • Dewachter I, Van Dorpe J, Smeijers L, Gilis M, Kuipéri C, Laenen I, Caluwaerts N, Moechars D, Checler F, Vanderstichele H, Van Leuven F. Aging increased amyloid peptide and caused amyloid plaques in brain of old APP/V717I transgenic mice by a different mechanism than mutant Presenilin1. J Neuroscience 2000; 20: 6452-6458.
  • Kumar-Singh S, De Jonghe C, Cruts M, Kleinert R, Wang R, Mercken M, De Strooper B, Vanderstichele H, Löfgren A, Vanderhoeven I, Backhovens H , Vanmechelen E, Kroisel PM, Van Broeckhoven C. Nonfibrillar diffuse amyloid deposition due to a ß 42 secretase site mutation points to an essential role for N-truncated Aß42 in Alzheimer’s disease.  Hum Mol Genet 2000; 9: 2589-2598.
  • Van Dorpe J, Smeijers L, Dewachter I, Nuyens D, Spittaels K, Van den Haute C, Mercken M, Moechars D, Laenen I, Kuiperi C, Bruynseels K, Tesseur I, Loos R, Vanderstichele H, Checler F, Sciot R, Van Leuven F.  Prominent cerebral amyloid angiopathy in transgenic mice overexpressing the London mutant of human APP in neurons. Am J Pathol. 2000; 157: 1283-1298.
  • Herreman A, Hartmann D, Annaert W, Saftig P, Craessaerts K, Serneels L, Umans L, Schrijvers V, Checler F, Vanderstichele H, Baekelandt V, Dressel R, Cupers P, Huylebroeck D, Zwijsen A, Van Leuven F, De Stooper B. Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of  presenilin 1 deficiency. Proc  Natl Acad Sci (USA) 1999; 96: 11872-11877.
  • De Jonghe C, Cruts M, Rogaeva EA, Tysoe C, Singleton A, Vanderstichele H, Meschino W, Dermaut B, Vanderhoeven I, Backhovens H, Vanmechelen E, Morris CM, Hardy J, Rubinsztein DC, St.George-Hyslop PH, Van Broeckhoven C. Aberrant splicing in the presenilin-1 intron 4 mutation causes presenile Alzheimer’s Disease by increased Aß42 secretion. Hum Mol Genet 1999; 8: 1529-1540.
  • De Jonghe C, Cras P, Vanderstichele H, Cruts M, Vanderhoeven I, Smouts I,  Vanmechelen E, Martin J-J, Hendriks L, Van Broeckhoven C.  Evidence that Aß42 plasma levels in presenilin-1 mutation carriers do not allow for prediction of their clinical phenotype. Neurobiol Dis 1999; 6: 280-287.
  • Dermaut B, Cruts M, Slooter AJC, Van Gestel S, De Jonghe C, Vanderstichele H, Vanmechelen E, Breteler MM, Hofman A, van Duijn CM, Van Broeckhoven C. The Glu318Gly substitution in presenilin 1 is not causally related to Alzheimer disease. Am J Hum Gen 1999; 64: 290-292.
  • De Jonghe C, Tysoe C, Cruts M, Vanderhoeven I, Vanderstichele H, Vanmechelen E, Van Broeckhoven C, Rubinsztein DC, Hendriks L. A presenilin-1 truncating mutation causing Alzheimer’s disease. In: ‘Alzheimer’s disease and related disorders’, edited by K.Iqbal, DF Swaab, B. Winblad, HM Wisniewski, John Wiley and Sons Ltd, Chichester, 1999: 81-86.
  • Dermaut B, Cruts M, Slooter AJC, Van Gestel S, De Jonghe C, Backhovens H, Vanderstichele H, Vanmechelen E, Breteler MMB, Hofman A, Hendriks L, Van Duijn CM, Van Broeckhoven C. Glu318Gly in presenilin-1 is a neutral mutation in relation to dementia: The Rotterdam Study. In: ’Alzheimer’s disease and related disorders’, edited by K.Iqbal, DF Swaab, B. Winblad, HM Wisniewski, John Wiley and Sons Ltd, Chichester, 1999: 87-92.
  • Saftig P, Craessaerts K, Vanderstichele H, Guhde G, Annaert W, von Figura K, Van Leuven F, De Strooper B. The two major familial Alzheimer’s disease gene products: Presenilin 1 and Amyloid Precursor Protein interact functionally. Neuroscience News 1998; 1:35-38.
  • De Strooper B, Saftig P, Craessaerts K, Vanderstichele H, Guhde G, Annaert W, Von Figura K, Van Leuven F. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 1998; 391: 387-390.

 

Neurodegeneration ⇑