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J Biol Chem, Vol. 274, Issue 11, 6827-6830, March 12, 1999
From the Department of Pharmacology & Physiology, University of
Rochester Medical Center, Rochester, New York 14642
Using stably expressed fluorescent indicator
proteins, we have determined for the first time the relationship
between the free Ca2+ and Ca2+-calmodulin
concentrations in intact cells. A similar relationship is obtained when
the free Ca2+ concentration is externally buffered or when
it is transiently increased in response to a
Ca2+-mobilizing agonist. Below a free Ca2+
concentration of 0.2 µM, no Ca2+-calmodulin
is detectable. A global maximum free Ca2+-calmodulin
concentration of ~ 45 nM is produced when the free Ca2+ concentration exceeds 3 µM, and a
half-maximal concentration is produced at a free Ca2+
concentration of 1 µM. Data for fractional saturation of
the indicators suggest that the total concentration of
calmodulin-binding proteins is ~ 2-fold higher than the total
calmodulin concentration. We conclude that high-affinity calmodulin
targets (Kd 
10 nM) are efficiently
activated throughout the cell, but efficient activation of low-affinity
targets (Kd 
100 nM) occurs only
where free Ca2+-calmodulin concentrations can be locally enhanced.
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