Westlind-Danielsson A, Andell S, Abens J, Bartfai T
Department of Biochemistry, Arrhenius Laboratory, Stockholm, Sweden.
Acta Physiol Scand. 1988 Mar;132(3):425-30. doi: 10.1111/j.1748-1716.1988.tb08347.x.
The equilibrium binding of [3H]propionyl neuropeptide Y ([ 3H]pNPY) to receptors in a crude synaptic membrane preparation from the rat striatum was influenced by GTP, which caused an apparent loss of high-affinity binding sites for [3H]pNPY. In the presence of GTP (10(-5) M), NPY and peptide YY (PYY) inhibited basal and forskolin-stimulated adenylate cyclase activity in a concentration-dependent manner in a cell-free preparation from rat striatum. The IC50 values for NPY and PYY were 1 X 10(-8) M and 1.4 x 10(-8) M respectively. The inhibitory action of NPY (10(-6) M) or of PYY (10(-6) M) was additive to that of acetylcholine (10(-4) M). The two peptides together also showed additivity (P less than 0.05) in inhibiting adenylate cyclase.
[3H]丙酰神经肽Y（[3H]pNPY）与大鼠纹状体粗制突触膜制剂中受体的平衡结合受到GTP的影响，GTP导致[3H]pNPY的高亲和力结合位点明显丧失。在GTP（10^(-5) M）存在的情况下，神经肽Y（NPY）和肽YY（PYY）在大鼠纹状体无细胞制剂中以浓度依赖的方式抑制基础和福斯高林刺激的腺苷酸环化酶活性。NPY和PYY的IC50值分别为1×10^(-8) M和1.4×10^(-8) M。NPY（10^(-6) M）或PYY（10^(-6) M）的抑制作用与乙酰胆碱（10^(-4) M）的抑制作用具有相加性。这两种肽共同作用时在抑制腺苷酸环化酶方面也表现出相加性（P＜0.05）。
