Oyama M, Kubota K
Laboratory of Biology, Himeji Institute of Technology, Hyogo, Japan.
Biochim Biophys Acta. 1991 Mar 19;1092(1):85-8. doi: 10.1016/0167-4889(91)90180-6.
Binding of cAMP to cell surface receptors evokes the transient activation of of adenylate cyclase in Dictyostelium discoideum. Dithiothreitol is also known as an activator of this enzyme. We found that the dithiothreitol-induced activation was specifically enhanced by extracellular polyamines or divalent cations. Furthermore, EDTA, a chelating agent of divalent cations, completely inhibited the dithiothreitol-induced activation of adenylate cyclase while EDTA did not inhibit the cAMP-induced activation. The inhibition was nullified by addition of polyamines or divalent cations. These results suggest that extracellular polyamines and divalent cations play a specific role in the dithiothreitol-induced activation of adenylate cyclase.
环磷酸腺苷(cAMP)与细胞表面受体的结合会引发盘基网柄菌中腺苷酸环化酶的瞬时激活。二硫苏糖醇也被认为是这种酶的激活剂。我们发现,细胞外多胺或二价阳离子可特异性增强二硫苏糖醇诱导的激活作用。此外,二价阳离子螯合剂乙二胺四乙酸(EDTA)完全抑制了二硫苏糖醇诱导的腺苷酸环化酶激活,而EDTA并不抑制cAMP诱导的激活。添加多胺或二价阳离子可消除这种抑制作用。这些结果表明,细胞外多胺和二价阳离子在二硫苏糖醇诱导的腺苷酸环化酶激活中发挥着特定作用。