Presence of a "CAGA box" in the APP gene unique to amyloid plaque-forming species and absent in all APLP -1/2 genes: implications in Alzheimer’s disease BRYAN MALONEY † , YUAN-WEN GE † , NIGEL GREIG ‡ and DEBOMOY K. LAHIRI † ,§ ,1 Departments of † Psychiatry and of § Medical and Molecular Genetics, Institute of Psychiatric Research, Indiana University School of Medicine, Indianapolis, Indiana, USA; and ‡ Laboratory of Neurosciences, National Institute on Aging, NIH, Baltimore, Maryland, USA 1 Correspondence: Indiana University School of Medicine, Institute of Psychiatric Research, 791 Union Dr., Indianapolis, IN 46202, USA. E-mail: dlahiri@iupui.edu <h3>SPECIFIC AIMS</h3> The amyloid-ß precursor protein (APP) is the source of toxic amyloid-ß peptide (Aß), which is associated with Alzheimer’s disease (AD). A "CAGA" sequence within the 5'-untranslated region (5'-UTR) of the APP gene is predicted to be the loop of a stem loop structure in a portion of the 5'-UTR that has been implicated to participate in gene regulation. We investigate whether this CAGA box is unique to the APP genes of humans and other species that naturally form pathologic amyloid brain plaque or if it is common to all mammals or even to all species’ APP and
/lp/fed-of-american-socs-for-experimental-biology/presence-of-a-caga-box-in-the-app-gene-unique-to-amyloid-plaque-0h7c2ilImy