Shori D K, Dormer R L, Goodchild M C, McPherson M A
Department of Medical Biochemistry, University of Wales College of Medicine, Cardiff, U.K.
Acta Univ Carol Med (Praha). 1990;36(1-4):46-8.
Phosphorylation of calmodulin-dependent regulator proteins has been studied in control and CF submandibular glands. Results showed that a 61,000 molecular weight calmodulin-binding protein was less phosphorylated in CF glands than control (p less than 0.001 for difference). The altered calmodulin-binding protein cross-reacted with an antiserum against a known calmodulin-dependent protein phosphatase, calcineurin. An alteration in a protein with calcineurin-like activity in CF epithelial cells would provide a link between defective beta-adrenergic responses and altered Ca2(+)-mediated events in CF and thus might be directly related to the genetic defect.
在对照和囊性纤维化(CF)患者的下颌下腺中,对钙调蛋白依赖性调节蛋白的磷酸化进行了研究。结果显示,在CF患者的腺体中,一种分子量为61,000的钙调蛋白结合蛋白的磷酸化程度低于对照(差异p<0.001)。这种改变的钙调蛋白结合蛋白与一种针对已知钙调蛋白依赖性蛋白磷酸酶——钙调神经磷酸酶的抗血清发生交叉反应。CF上皮细胞中具有钙调神经磷酸酶样活性的蛋白发生改变,这将在CF患者中缺陷的β-肾上腺素能反应和改变的Ca2⁺介导事件之间建立联系,因此可能与遗传缺陷直接相关。