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J Biol Chem, Vol. 274, Issue 29, 20165-20170, July 16, 1999
From the Department of Cell Biology, The University of Alabama at
Birmingham, Birmingham, Alabama 35294-0005
The capacitative Ca2+ entry
pathway in J774 macrophages is rapidly inhibited by the amino sugar
glucosamine. This pathway is also inhibited by treatments such as
2-deoxy-D-glucose (2dGlc) or glucose deprivation that
inhibit glycolysis and lead to significant decreases in cellular ATP
and other trinucleotides. We sought to determine whether glucosamine's
effect on capacitative Ca2+ entry was also due to ATP
depletion, as has been suggested recently for its link to insulin
resistance. In contrast to brief treatments with 2dGlc, there was no
significant decrease in ATP following exposure to glucosamine. In
addition, the 2dGlc-mediated inhibition of capacitative
Ca2+ influx was reversed by staurosporine, a microbial
alkaloid that inhibits a broad range of protein kinases. Staurosporine
was also able to reverse the inhibition of capacitative
Ca2+ entry seen following other treatments that decreased
cellular ATP levels, including cytochalasin B and iodoacetic acid.
Other inhibitors of protein kinase C, including bisindolylmaleimide, K252a, H-7, and calphostin C, were unable to mimic this effect of
staurosporine. However, the inhibition of capacitative Ca2+
influx in the presence of glucosamine was not reversed by
staurosporine. These data indicate that the inhibitory action on
capacitative Ca2+ entry of glucosamine is distinct
from that caused by ATP depletion.
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