Adenosine analogs inhibit adipocyte adenylate cyclase by a GTP-dependent process: basis for actions of adenosine and methylxanthines on cyclic AMP production and lipolysis.
Adenosine analogs inhibit adipocyte adenylate cyclase by a GTP-dependent process: basis for actions of adenosine and methylxanthines on cyclic AMP production and lipolysis.
复制标题
腺苷类似物通过 GTP 依赖性过程抑制脂肪细胞腺苷酸环化酶：腺苷和甲基黄嘌呤对环 AMP 产生和脂肪分解作用的基础。
DOI：
--
复制
发表时间：
1978
影响因子：
11.1
通讯作者：
M. Rodbell
中科院分区：
文献类型：
--
作者：
C. Londos;D. Cooper;W. Schlegel;M. Rodbell
大鼠脂肪细胞纯化膜中的腺苷酸环化酶被低浓度的嘌呤修饰的腺苷类似物抑制，特别是那些在N6位修饰的腺苷类似物。这种抑制作用被甲基黄嘌呤竞争性拮抗，但不被其他环核苷酸磷酸二酯酶抑制剂拮抗，并且它依赖于测定介质中GTP的“抑制”浓度。核糖修饰的腺苷类似物通过既不依赖于GTP浓度也不被甲基黄嘌呤拮抗的过程抑制腺苷酸环化酶。这些结果解释了腺苷和甲基黄嘌呤对脂肪细胞代谢的有效作用，并证明了GTP在介导作用于细胞表面受体的试剂的抑制中的重要性。
Adenylate cyclase in purified membranes from rat adipocytes is inhibited by low concentrations of purine-modified adenosine analogs, particularly those modified in the N6 position. Such inhibition is antagonized competitively by methylxanthines, but not by other cyclic nucleotide phosphodiesterase inhibitors, and it is dependent on "inhibitory" concentrations of GTP in the assay medium. Ribose-modified adenosine analogs inhibit adenylate cyclase through a process that is neither dependent upon the GTP concentration nor antagonized by methylxanthines. These results explain the potent effects of adenosine and methylxanthines on fat cell metabolism and demonstrate the importance of GTP in mediating inhibition by agents that act at cell surface receptors.