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J. Biol. Chem., Vol. 266, Issue 26, 16985-16988, 09, 1991
H Koshiyama, HC Lee and AH Tashjian Jr
In sea urchin eggs an enzymatic metabolite of beta-NAD+, called cyclic
ADP-ribose (cADPR), is as potent and powerful a releaser of sequestered
intracellular Ca2+ as is inositol 1,4,5-trisphosphate (IP3). The enzyme
that synthesizes cADPR is present in several vertebrate animal tissues, but
the Ca(2+)-releasing activity of cADPR has not been described in mammalian
cells. We report here that incubation of beta-NAD+ with cell- free extracts
of several rat tissues (including pituitary gland) generates a product
which releases intracellular Ca2+ stores in permeabilized rat pituitary
GH4C1 cells. This product has the biological characteristics of cADPR (it
acts after depletion of the IP3 stores and after blockade of the IP3
receptor by heparin). The response is mimicked, in a
concentration-dependent manner, by authentic cADPR and is desensitized by
prior incubation with cADPR. We conclude that cADPR is not only synthesized
by certain mammalian cells but also acts in such cells to release
compartmentalized intracellular Ca2+ by a mechanism that differs from that
used by IP3. Therefore, cADPR may serve, in addition to IP3, as a second
messenger for intracellular Ca2+ mobilization in mammalian cells.
Novel mechanism of intracellular calcium release in pituitary cells
Laboratory of Toxicology, Harvard School of Public Health, Boston, Massachusetts.
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