ISSN: 2161-0460

Journal of Alzheimers Disease & Parkinsonism
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Research Article

Abnormal Protein Profiles in Hippocampus of Mouse Models of Down Syndrome: Similarities with Alzheimer's Disease

Aaron Block1, A. Ranjitha Dhanasekaran1, Md. Mahiuddin Ahmed1 and Katheleen J Gardiner1,2*

1 Department of Pediatrics, Linda Crnic Institute for Down Syndrome, University of Colorado Denver, Colorado, USA

2 Department of Biochemistry and Molecular Genetics, Human Medical Genetics and Genomics, and Neuroscience Programs, University of Colorado Denver, Colorado, USA

Corresponding Author:
Katheleen Gardiner
Department of Pediatrics
Linda Crnic Institute for Down Syndrome
Human Medical Genetics and Genomics
Neuroscience Programs, University of Colorado Denver
Mail Stop 8608, 12700 E 19th Avenue
Aurora, Colorado 80045, USA
Tel: 303-724-0572
Fax: 303-720-5741
E-mail: katheleen.gardiner@ucdenver.edu

Received date: December 20, 2013; Accepted date: January 22, 2014; Published date: February 03, 2014

Citation: Block A, Dhanasekaran AR, Ahmed MM, Gardiner KJ (2014) Abnormal Protein Profiles in Hippocampus of Mouse Models of Down Syndrome: Similarities with Alzheimer’s Disease. J Alzheimers Dis Parkinsonism 4:138. doi:10.4172/2161-0460.1000138

Copyright: © 2014 Block A, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Down syndrome (DS) is caused by an extra copy of the long arm of human chromosome 21 (HSA21) and the increased expression, due to dosage, of HSA21 encoded genes. In addition to intellectual disability, all individuals with DS develop the neuropathology of Alzheimer’s Disease (AD) by age 30-40. The amyloid precursor protein gene, APP, that is mutated or duplicated in some familial AD (FAD), is encoded by HSA21, over expressed in DS, and a candidate for causing AD in DS. However, only half of those with DS will develop the AD-like dementia by age 50-60, suggesting that additional HSA21 genes may modulate the effects of APP triplication, and/or protect the DS brain from early onset progression to dementia in spite of neuropathology. In sporadic AD and mouse models of FAD, abnormal levels of a diverse set of proteins, including receptors, scaffold proteins, kinases, phosphatases and cytokines, have been documented, but nothing is known about their possible roles in AD in DS. Here, we compare expression of 26 AD-related proteins in hippocampus of four mouse models of DS, the Ts65Dn, Tc1, Dp (10)1Yey and Dp (17)1Yey, that together provided trisomy of partially overlapping subsets of all HSA21 genes or mouse orthologs. In the Dp(10)1Yey, that is trisomic for HSA21 orthologs mapping to mouse chromosome 10, twelve of 26 AD-related proteins were elevated, while in the Tc1, Dp(17)1Yey and the popular Ts65Dn, six, four and two differed from littermate controls. These data suggest that genes mapping to the HSA21 orthologous regions of mouse chromosomes 10 and 17 contribute to protein perturbations in the DS brain, and possibly AD in DS. Considering the different phenotypic features of the four DS mouse models further suggests that some protein abnormalities may be compensatory and protective for brain function and/or that learning and memory deficits may be age-dependent.

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