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Bradykinin activates ADP‐ribosyl cyclase in neuroblastoma cells: Intracellular concentration decrease in NAD and increase in cyclic ADP‐ribose
Author(s) -
Higashida Haruhiro,
Salmina Alla,
Hashii Minako,
Yokoyama Shigeru,
Zhang Jia-Sheng,
Noda Mami,
Zhong Zen-Guo,
Jin Duo
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.07.084
Subject(s) - nad+ kinase , intracellular , second messenger system , cyclase , chemistry , bradykinin , cyclic adp ribose , receptor , biochemistry , enzyme , biology , microbiology and biotechnology , cd38 , stem cell , cd34
ADP‐ribosyl cyclase activity in the crude membrane fraction of neuroblastoma × glioma NGPM1‐27 hybrid cells was measured by monitoring [ 3 H] cyclic ADP‐ribose (cADPR) formation from [ 3 H] NAD + . Bradykinin (BK) at 100 nM increased ADP‐ribosyl cyclase activity by about 2.5‐fold. Application of 300 nM BK to living NGPM1‐27 cells decreased NAD + to 78% of the prestimulation level at 30 s. In contrast, intracellular cADPR concentrations were increased by 2–3‐fold during the period from 30 to 120 s after the same treatment. Our results suggest that cADPR is one of the second messengers downstream of B 2 BK receptors.