z-logo
Premium
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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom