Rozengurt E
Department of Medicine, Division of Digestive Diseases, School of Medicine and Molecular Biology Institute, University of California, Los Angeles, California 90095, USA.
Am J Physiol. 1998 Aug;275(2):G177-82. doi: 10.1152/ajpgi.1998.275.2.G177.
Gastrointestinal (GI) peptides (also referred to as neuropeptides or regulatory peptides), including the mammalian bombesin-like peptides gastrin and CCK, elicit the synthesis of classic second messengers (e.g., Ca2+, diacylglycerol, and cAMP) and the consequent stimulation of serine/threonine protein kinase cascades. An emerging theme in signal transduction is that these agonists also induce rapid and coordinate tyrosine phosphorylation of a set of focal adhesion proteins, including the nonreceptor tyrosine kinase p125fak and the adaptor proteins p130cas and paxillin. GI peptide-mediated induction of tyrosine phosphorylation of these focal adhesion proteins is critically dependent on the integrity of the actin cytoskeleton and on functional Rho. The purpose of this article is to review recent advances in unraveling this novel tyrosine kinase pathway(s), because it appears to play a fundamental role in the mediation of important biological effects induced by GI peptides, including cell migration and proliferation.
胃肠道（GI）肽（也称为神经肽或调节肽），包括哺乳动物的蛙皮素样肽胃泌素和胆囊收缩素（CCK），可引发经典第二信使（如Ca2+、二酰基甘油和cAMP）的合成，并随之刺激丝氨酸/苏氨酸蛋白激酶级联反应。信号转导中一个新出现的主题是，这些激动剂还能诱导一组粘着斑蛋白的快速且协同的酪氨酸磷酸化，包括非受体酪氨酸激酶p125fak以及衔接蛋白p130cas和桩蛋白。GI肽介导的这些粘着斑蛋白酪氨酸磷酸化的诱导，严重依赖于肌动蛋白细胞骨架的完整性和功能性Rho。本文的目的是综述在揭示这一新型酪氨酸激酶途径方面的最新进展，因为它似乎在介导GI肽诱导的重要生物学效应（包括细胞迁移和增殖）中发挥着基本作用。
