Paper
19 February 2007 TIRET microscopy: monitoring protein (amyloid precursor protein and beta-secretase) interaction on the surface of living cells
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Abstract
Total internal reflection fluorescence microscopy (TIRFM) and non-radiative energy transfer (FRET) measurements have been combined in order to examine co-localization of the amyloid precursor protein (APP) and the ?-site APPcleaving enzyme (BACE) in human glioblastoma cells. So far, these proteins have been co-localized within whole cells (depending on the intracellular amount of cholesterol) and in some cases also within their plasma membranes. This supports the present hypothesis of localization within lipid domains on the cell surface and co-internalization via endocytosis.
© (2007) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Christine von Arnim, Michael Wagner, Petra Weber, and Herbert Schneckenburger "TIRET microscopy: monitoring protein (amyloid precursor protein and beta-secretase) interaction on the surface of living cells", Proc. SPIE 6441, Imaging, Manipulation, and Analysis of Biomolecules, Cells, and Tissues V, 64410D (19 February 2007); https://doi.org/10.1117/12.699856
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KEYWORDS
Luminescence

Computer programming

Proteins

Microscopy

Energy transfer

Magnesium

Green fluorescent protein

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