Cionin, a protochordean hybrid of cholecystokinin and gastrin: biological activity in mammalian systems.
Cionin, a protochordean hybrid of cholecystokinin and gastrin: biological activity in mammalian systems.
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Cionin，胆囊收缩素和胃泌素的原索混合物：哺乳动物系统中的生物活性。
DOI：
10.1152/ajpgi.1991.260.6.g977
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
Rehfeld,JF
中科院分区：
文献类型：
--
作者：
Schjoldager,B;Park,J;Johnsen,AH;Yamada,T;Rehfeld,JF
原脊索八肽cionin在结构上是哺乳动物胆囊收缩素（CCK）和胃泌素的杂合体，因此可能是它们的共同祖先。为了确定cionin的行为是否像CCK或胃泌素，我们研究了其对犬胃底生长抑素细胞和猪和牛胆囊肌肉的影响。Cionin释放生长抑素的效力（ED 500.15 nM）和功效（细胞含量的14.8%）与CCK-8（ED 500.12 nM，功效16.7%）相似。CCK-8和cionin的功效而非效力不同于硫酸化胃泌素（0.12 nM，9.7%）、非硫酸化胃泌素（0.20 nM，9.4%）和非硫酸化CCK-8（0.30 nM，10.4%）。CCK和胃泌素以浓度依赖性方式刺激猪胆囊肌条收缩，功效无差异，但效力具有特征差异。CCK-8和cionin显示出相似的效力，ED502.0和2.6 nM;两者均与硫酸化胃泌素的ED 50（0.4 μM）和非硫酸化胃泌素的ED 50（2.3 μM）显著不同。CCK放射性配体与猪和牛胆囊肌层的膜富集制剂结合具有特异性和高亲和力。平衡数据显示CCK和胃泌素肽的结合最适合于单个位点。CCK-8和cionin显示出相似的亲和力[Kd分别为0.5 nM（猪）、0.5 nM（牛，CCK）和Kd 0.8和0.9 nM（cionin）]。这些与Kd 0.6和1.5 μM（硫酸化胃泌素）以及0.7和0.2 μM（非硫酸化胃泌素）也有显著差异。结果表明，在哺乳动物中，cionin的作用类似于CCK，而不是胃泌素。胆囊运动;生长抑素;受体
The protochordean octapeptide cionin is structurally a hybrid of mammalian cholecystokinin (CCK) and gastrin, and thus their possible common ancestor. To determine whether cionin behaves like CCK or gastrin, we examined its effect on canine fundic somatostatin cells and on porcine and bovine gallbladder muscles. Cionin released somatostatin with a potency (ED500.15 nM) and efficacy (14.8% of cell content) similar to that of CCK-8 (ED500.12 nM, efficacy 16.7%). The efficacies but not the potencies of CCK-8 and cionin differed from those of sulfated gastrin (0.12 nM, 9.7%), nonsulfated gastrin (0.20 nM, 9.4%), and nonsulfated CCK-8 (0.30 nM, 10.4%). CCK and gastrin stimulated contractions of porcine gallbladder muscle strips in a concentration-dependent manner with no differences in efficacy but with characteristic differences in potency. CCK-8 and cionin displayed similar potencies of ED502.0 and 2.6 nM; both were significantly different from the ED50 of 0.4 μM for sulfated gastrin and 2.3 μM for nonsulfated gastrin. CCK radioligand binding to membrane-enriched preparations of porcine and bovine gallbladder muscularis was specific and of high affinity. The equilibrium data revealed that binding of CCK and gastrin peptides best fit a single site. CCK-8 and cionin displayed similar affinities [Kd0.5 nM (porcine), 0.5 nM (bovine, CCK) vs. Kd0.8 and 0.9 nM (cionin), respectively]. These differed again significantly from Kd 0.6 and 1.5 μM (sulfated gastrin) and 0.7 and 0.2 μM (nonsulfated gastrin). The results show that cionin behaves like CCK rather than gastrin in mammals.gallbladder motility; somatostatin; receptorsSubmitted on August 10, 1990Accepted on December 19, 1990