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Effect of tumor necrosis factor‐α converting enzyme (TACE) and metalloprotease inhibitor on amyloid precursor protein metabolism in human neurons by Megan Blacker; Mark C. Noe; Thomas J. Carty; Cynthia G. Goodyer; Andréa C. LeBlanc is a Neuroscience article available to read on EtoBox.
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## Abstract Tumor necrosis factor‐α (TNF‐α) is implicated in inflammatory processes and much effort is being directed at inhibiting the release of TNF‐α for treatment of inflammatory conditions. In this context, the drug CP‐661,631 has been developed to inhibit the TNF‐α converting enzyme (TACE). However, TACE is also implicated in amyloid precursor protein secretion. Amyloid precursor protein (APP) undergoes constitutive and regulated secretion by α‐secretase endoproteolytic cleavage within the amyloid β peptide (Aβ) domain. Alternative cleavage at the N‐ and C‐terminus of the Aβ domain by β‐ and γ‐secretases results in the production of Aβ. In many cellular and __in vivo__ animal models, increased secretion of APP results in a concomitant decrease in the production of Aβ suggesting that the two pathways are intricately linked. However, in human primary neuron cultures, increased APP secretion is not associated with a decrease in total Aβ production. To determine if the use of CP‐661,631 may enhance amyloidogenic processing in human brain, we have assessed the effect of CP‐661,631 on APP metabolism in primary cultures of human neurons. Our results show that CP‐661,631 effectively
Who reads Effect of tumor necrosis factor‐α converting enzyme (TACE) and metalloprotease inhibitor on amyloid precursor protein metabolism in human neurons?
It is typically read by researchers, students, and practitioners in Neuroscience.
- Author
- Megan Blacker; Mark C. Noe; Thomas J. Carty; Cynthia G. Goodyer; Andréa C. LeBlanc
- Publisher
- John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0022-3042)
- Published
- 2002
- Language
- EN
- Field
- Neuroscience (Life Sciences)