Inhibition of protein kinase A fails to alter mast cell adenosine responsiveness.
Inhibition of protein kinase A fails to alter mast cell adenosine responsiveness.
复制标题
蛋白激酶 A 的抑制不能改变肥大细胞腺苷反应性。
DOI：
10.1007/bf02005755
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发表时间：
1994
期刊：
影响因子：
--
通讯作者：
Walker,LL
中科院分区：
文献类型：
--
作者：
Marquardt,DL;Walker,LL
Adenosine activates adenylate cyclase and phospholipase C in mast cells and potentiates stimulated mediator release. To determine whether activation of adenylate cyclase is necessary for the effects of adenosine on the mast cell secretory process, a specific inhibitor of cAMP-dependent protein kinase, KT5720, was used. Antigen and adenosine each induced a rapid increase in mast cell cAMP-dependent protein kinase activity within 30 s. Preincubation with KT5720 (100 nM–10 μM) suppressed cAMP-dependent protein kinase activity and inhibited antigen-stimulated β-hexosaminidase and leukotriene C4releases. Adenosine retained its ability to potentiate β-hexosaminidase release in antigen- and A23187-stimulated cells even in the presence of complete cAMP-dependent protein kinase inhibition. Mast cells rendered unresponsive to adenosine-related signals by preincubation with adenosine analogs maintained this hyporesponsiveness after incubation with KT5720. It appears that the abilities of adenosine to augment mast cell degranulation and induced receptor hyporesponsiveness are independent of changes in cAMP.
