Khan N A, Quemener V, Moulinoux P
Department of Cell Biology, Central Hospital of University (C.H.U.) of Rennes, France.
Life Sci. 1990;46(1):43-7. doi: 10.1016/0024-3205(90)90055-v.
Polyamines (spermidine, spermine and putrescine) inhibited the adenylate cyclase activity in a concentration dependent manner in human erythrocyte plasma membranes. Spermidine (Spd) exhibited more inhibitory effect than spermine (Spm) and putrescine (Put). On the contrary, the addition of amino acids (arginine, glutamine and lysine) did not influence the basal enzyme activity. Other cations (polylysine, polyarginine and polyglutamine) also did not affect the enzyme activity. Addition of all the three polyamines (Spd, Spm and Put) in the reaction mixture exhibited moderate inhibitory effect on the adenylate cyclase activity whether it was basal or activated with sodium fluoride or with forskolin. Since the three polyamines exhibited maximum inhibitory effect at 10 microM concentration which is within physiological limit for mammalian tissues, we suggest that there may be a regulatory function of these molecules on adenylate cyclase activity in human erythrocytes.
多胺（亚精胺、精胺和腐胺）以浓度依赖的方式抑制人红细胞质膜中的腺苷酸环化酶活性。亚精胺（Spd）的抑制作用比精胺（Spm）和腐胺（Put）更强。相反，添加氨基酸（精氨酸、谷氨酰胺和赖氨酸）不会影响基础酶活性。其他阳离子（聚赖氨酸、聚精氨酸和聚谷氨酰胺）也不影响酶活性。在反应混合物中添加所有三种多胺（Spd、Spm和Put），无论其是基础状态还是用氟化钠或福斯高林激活后，都对腺苷酸环化酶活性表现出中度抑制作用。由于这三种多胺在10 microM浓度时表现出最大抑制作用，该浓度处于哺乳动物组织的生理极限范围内，我们认为这些分子可能对人红细胞中的腺苷酸环化酶活性具有调节功能。
