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Assessment of aldehyde dehydrogenase in viable cells
RJ Jones, JP Barber, MS Vala, MI Collector, SH Kaufmann, SM Ludeman, OM Colvin and J Hilton
Johns Hopkins Oncology Center, Johns Hopkins Medical Institutions,
Baltimore, MD 21287-8967, USA.
Cytosolic aldehyde dehydrogenase (ALDH), an enzyme responsible for
oxidizing intracellular aldehydes, has an important role in ethanol,
vitamin A, and cyclophosphamide metabolism. High expression of this enzyme
in primitive stem cells from multiple tissues, including bone marrow and
intestine, appears to be an important mechanism by which these cells are
resistant to cyclophosphamide. However, although hematopoietic stem cells
(HSC) express high levels of cytosolic ALDH, isolating viable HSC by their
ALDH expression has not been possible because ALDH is an intracellular
protein. We found that a fluorescent aldehyde, dansyl aminoacetaldehyde
(DAAA), could be used in flow cytometry experiments to isolate viable mouse
and human cells based on their ALDH content. The level of dansyl
fluorescence exhibited by cells after incubation with DAAA paralleled
cytosolic ALDH levels determined by Western blotting and the sensitivity of
the cells to cyclophosphamide. Moreover, DAAA appeared to be a more
sensitive means of assessing cytosolic ALDH levels than Western blotting.
Bone marrow progenitors treated with DAAA proliferated normally.
Furthermore, marrow cells expressing high levels of dansyl fluorescence
after incubation with DAAA were enriched for hematopoietic progenitors. The
ability to isolate viable cells that express high levels of cytosolic ALDH
could be an important component of methodology for identifying and
purifying HSC and for studying cyclophosphamide-resistant tumor cell
populations.
Volume 85,
Issue 10,
pp. 2742-2746,
05/15/1995
Copyright © 1995 by The American Society of Hematology
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