Calbindin D28K (formerly known as vitamin D-dependent calcium binding
protein and referred to here as calbindin) is found in a wide variety
of tissues, but only in certain cells within those tissues. Apart from
its ability to bind calcium, nothing is known about its function in t
hese cells. To investigate its role we have transfected the chick calb
indin cDNA into mouse NIH3T3 fibroblasts and established a new cell li
ne where calbindin is permanently expressed. Immunofluorescence studie
s show that calbindin is distributed throughout the cytoplasm, and tre
atment of the cells with cycloheximide shows that it has a relatively
long half-life within the cell. Measurements of intracellular calcium
concentration using Fura-2 suggest that the presence of calbindin with
in the cells does not affect the increase in intracellular calcium lev
els which occurs in response to serum stimulation or the rate at which
these return to the basal level, but that it may act as a buffer for
the entry of extracellular calcium.