In:
Science, American Association for the Advancement of Science (AAAS), Vol. 283, No. 5410 ( 1999-03-26), p. 2085-2089
Abstract:
Spatially resolved fluorescence resonance energy transfer (FRET) measured by fluorescence lifetime imaging microscopy (FLIM), provides a method for tracing the catalytic activity of fluorescently tagged proteins inside live cell cultures and enables determination of the functional state of proteins in fixed cells and tissues. Here, a dynamic marker of protein kinase Cα (PKCα) activation is identified and exploited. Activation of PKCα is detected through the binding of fluorescently tagged phosphorylation site–specific antibodies; the consequent FRET is measured through the donor fluorophore on PKCα by FLIM. This approach enabled the imaging of PKCα activation in live and fixed cultured cells and was also applied to pathological samples.
Type of Medium:
Online Resource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.283.5410.2085
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
1999
detail.hit.zdb_id:
128410-1
detail.hit.zdb_id:
2066996-3
detail.hit.zdb_id:
2060783-0
SSG:
11
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