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J. Biol. Chem., Vol. 267, Issue 28, 19840-19845, Oct, 1992
JT Deeney, K Tornheim, HM Korchak, M Prentki and BE Corkey
Cytosolic free Ca2+ rises in pancreatic beta-cells in response to glucose
stimulation and is part of the coupling to insulin secretion. This study
evaluates a possible role for cytosolic long chain acyl-CoA esters in
modulating Ca2+ handling by clonal beta-cells (HIT). Intact cells incubated
with 20 microM free palmitic acid exhibited a 40% decrease in basal
cytosolic free Ca2+. In contrast, acyl-CoA esters, up to a chain length of
16, but not the corresponding fatty acids, significantly lowered the Ca2+
set point maintained by cells permeabilized with saponin. The maximum
response to the various acyl- CoA esters increased with increasing chain
length, with no differences in the half-maximally effective concentration
of 0.5 microM. Long chain acyl-CoA esters caused a 40-50% increase in
45Ca2+ influx into a non- mitochondrial pool in the permeabilized HIT
cells, consistent with a stimulatory effect on the endoplasmic reticulum
Ca(2+)-ATPase activity, but did not affect inositol
1,4,5-trisphosphate-induced Ca(2+)-efflux. Thapsigargin, an inhibitor of
endoplasmic reticulum Ca(2+)-ATPase activity, blocked the decrease in the
Ca2+ set point caused by acyl-CoA esters. The ability of acyl-CoA esters to
lower the Ca2+ set point depended on the ATP/ADP ratio (or free ADP); the
Ca2+ set point was lowered by 36 +/- 3.6% at an ATP/ADP ratio of 90 and by
14 +/- 1.9% at an ATP/ADP ratio of 7. Depletion of cellular protein kinase
C did not prevent the acyl-CoA-induced lowering of the Ca2+ set point.
These findings suggest that the increases in long chain acyl-CoA esters may
play a role in restoring cytosolic free Ca2+ through activation of
Ca(2+)-ATPases.
Acyl-CoA esters modulate intracellular Ca2+ handling by permeabilized clonal pancreatic beta-cells
Evans Department of Medicine, Boston University School of Medicine, Massachusetts 02118.
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