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J. Biol. Chem., Vol. 283, Issue 28, 99935, July 11, 2008

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CD147 Doesn't Follow the Secretase Crowd

A pathological hallmark in the development of Alzheimer disease is the accumulation of β-amyloid peptides (Aβ) in the brain, a result of sequential cleavage of transmembrane amyloid precursor proteins (APPs). A major APP cleaver is -secretase, a multisubunit enzyme complex. Previous reports have suggested that a glycoprotein called CD147 is a subunit of -secretase and that CD147 levels inversely correlate with levels of Aβ, but in this Paper of the Week, Kulandaivelu Vetrivel and colleagues demonstrate that this is not the case. They observed that the cellular and brain tissue localization of CD147 did not correlate with other core components of -secretase. Although CD147 depletion could increase Aβ levels in intact fibroblasts, it did not affect -secretase cleavage of APP in an in vitro assay. Rather, they found that the cell medium from CD147-overexpressing cells could degrade Aβ peptides more rapidly than normal medium, pointing to an extracellular location for this glycoprotein. As CD147 is known to participate in matrix metalloprotease (MMP) production, this study may point to a new pathway of Aβ regulation, whereby secreted CD147 triggers amyloid degradation through MMPs.

Immunohistochemical staining of the cortex and CA1 regions of mouse hippocampus show that CD147 and nicastrin (core secretase subunit) do not have similar localization.

FOOTNOTES

See referenced article, J. Biol. Chem. 2008, 283, 19489-19498

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This Article Full Text (PDF) Author Profile Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Related Collections Papers Of The Week Social Bookmarking                      What's this?