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Antise oligonucleotide inhibition of amyloid precursor protein expressed in bacteria
Author(s) -
Kumar Vijaya Buddhiraju,
Franko Mark,
Banks William A,
Morley John E
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a107-a
Subject(s) - amyloid precursor protein , complementary dna , oligonucleotide , transfection , expression vector , bacteria , microbiology and biotechnology , plasmid , biology , amyloid precursor protein secretase , vector (molecular biology) , chemistry , gene , biochemistry , alzheimer's disease , recombinant dna , disease , medicine , genetics , pathology
Amyloid Precursor Protein (APP) is known to be involved in contributing to the beta fragment that is implicated in Alzheimer’s disease (AD). Reducing the expression of APP is one the therapeutic approaches to alleviate AD. We have previously shown that antisense oligodeoxynucleotides (ODNs) to APP mRNA effectively reduce its expression and improve the memory in mice that serve as animal models for AD. For this investigation, we have cloned APP cDNA into a bacterial expression vector, pBAD, and transfected into bacteria. The protein expression could be induced with arabinose and detected by antibody to the tagged V5 peptide. Here we show that the antisense oligonucleotides effectively reduce the expression of APP in bacterial cells by using prokaryotic expression. As the monitoring of the effectiveness of an ODN is faster and simpler compared to eukaryotic expression, such bacterial expression systems may prove to be an improved method of testing pharmaceutical agents aimed to treat AD.