Complete tyrosine-O-sulphation of gastrin in neonatal rat pancreas
Complete tyrosine-O-sulphation of gastrin in neonatal rat pancreas
复制标题
新生大鼠胰腺中胃泌素的完全酪氨酸-O-硫酸化
作者：
S. Brand;B. Andersen;J. Rehfeld
蛋白质酪氨酸残基的修饰引起了人们极大的兴趣。虽然磷酸化受到了最多的关注1 -3，酪氨酸-O-硫酸化也很常见4，并在激素胃泌素和胆囊收缩素（CCK）中进行了密切研究。CCK调节胰腺酶分泌。它总是硫酸化的5 -9，硫酸化使其胰腺促分泌活性增加100倍10 -13。相比之下，只有一半的胃泌素分子是酪氨酸-O-硫酸化的5 -9，硫酸化不影响胃泌素调节胃酸分泌的能力6。我们现在报告，在新生大鼠胰腺中，这是新生大鼠胃泌素的主要来源14，胃泌素完全硫酸化。此外，出生后第一周内胰腺中胃泌素的消失与肠道中CCK的出现平行。由于硫酸化作用对胃泌素和CCK 10 -13的胰腺促分泌活性是必不可少的，因此新生儿的胰腺胃泌素可能相当于成人的肠CCK。
Modification of tyrosine residues of proteins has attracted great interest. Although phosphorylation has received most attention1–3, tyrosine-O-sulphation is also common4 and has been closely investigated in the hormones gastrin and cholecystokinin (CCK). CCK regulates pancreatic enzyme secretion. It is always sulphated5–9 and sulphation increases its pancreatic secretagogue activity 100-fold10–13. By contrast, only half of gastrin molecules are tyrosine- O-sulphated5–9 and sulphation does not influence the ability of gastrin to regulate gastric acid secretion6. We now report that in neonatal rat pancreas, which is the major source of gastrin in the newborn rat14, gastrin is completely sulphated. Moreover, the disappearance of gastrin from the pancreas during the first weeks after birth parallels the appearance of CCK in the intestine. Since sulphation is essential for pancreatic secretagogue activity of gastrin as well as of CCK10–13, pancreatic gastrin in the neonate may be the equivalent of intestinal CCK in the adult.