Ostrowski J, Trzeciak L, Kołodziejski J, Bomsztyk K
Department of Gastroenterology, Medical Center of Postgraduate Education at the Maria Skłodowska-Curie Memorial Cancer Center and Institute of Oncology, Warsaw, Poland.
Br J Cancer. 1998 Nov;78(10):1301-6. doi: 10.1038/bjc.1998.675.
Protein kinases play a key role in intracellular signalling, participating at multiple levels along the transduction cascades that trigger mitogenic response. Because protein kinases are involved in mitogenic pathways, they are likely to play a role in the abnormal proliferation of malignant cells. In this study we compared activity of mitogen-activated protein (MAP) kinase and several renaturable kinases in homogenates of 30 surgically resected colorectal cancers and their adjacent normal tissues. Using sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and membrane autophosphorylation assay on homogenates obtained from normal colon mucosa and adenocarcinoma, we identified at least four renaturable kinases (50, 55, 85, 200 kDa). Compared with adjacent tissue, in most of the cancer samples only the 85-kDa kinase exhibited a higher level of autophosphorylation activity than those in normal matched tissue (P < 0.001). Moreover, the 85-kDa kinase from nearly all cancer homogenates showed faster electrophoretic mobility than the 85-kDa kinase from normal tissue homogenates. Interestingly, the 50-kDa kinase had significantly lower autophosphorylation activity in cancer tissues than those of normal tissue (P< 0.05). To assess p42-p44 MAP kinase activity, proteins were immunoprecipitated from adjacent colon mucosa and adenocarcinoma with anti-extracellular signal-related kinase (ERK) 1/2 antibodies, and MAP kinase activity was measured using MBP as a substrate. These studies revealed that MAP kinase activity in colorectal cancer was significantly higher (P < 0.001) than that in adjacent mucosa. Thus, the constitutive activity of MAP kinase and autophosphorylation activity of 85-kDa kinase are increased, whereas the autophosphorylation activity of another kinase, 50 kDa, is decreased in colorectal adenocarcinoma. However, although signal transduction pathways are markedly altered in this cancer, neither p42/p44 MAP kinase activity nor 85-kDa autokinase activity could be correlated with the established prognostic indicators.
蛋白激酶在细胞内信号传导中起关键作用,在触发有丝分裂原反应的转导级联反应的多个层面发挥作用。由于蛋白激酶参与有丝分裂原途径,它们很可能在恶性细胞的异常增殖中发挥作用。在本研究中,我们比较了30例手术切除的结直肠癌及其相邻正常组织匀浆中丝裂原活化蛋白(MAP)激酶和几种可复性激酶的活性。使用十二烷基硫酸钠聚丙烯酰胺凝胶电泳(SDS-PAGE)和对从正常结肠黏膜和腺癌获得的匀浆进行膜自磷酸化测定,我们鉴定出至少四种可复性激酶(50、55、85、200 kDa)。与相邻组织相比,在大多数癌症样本中,只有85 kDa激酶表现出比正常匹配组织更高水平的自磷酸化活性(P < 0.001)。此外,几乎所有癌症匀浆中的85 kDa激酶比正常组织匀浆中的85 kDa激酶表现出更快的电泳迁移率。有趣的是,50 kDa激酶在癌组织中的自磷酸化活性明显低于正常组织(P < 0.05)。为了评估p42-p44 MAP激酶活性,用抗细胞外信号调节激酶(ERK)1/2抗体从相邻结肠黏膜和腺癌中免疫沉淀蛋白质,并以髓磷脂碱性蛋白(MBP)为底物测量MAP激酶活性。这些研究表明,结直肠癌中的MAP激酶活性明显高于相邻黏膜(P < 0.001)。因此,在结直肠癌中,MAP激酶的组成性活性和85 kDa激酶的自磷酸化活性增加,而另一种50 kDa激酶的自磷酸化活性降低。然而,尽管该癌症中的信号转导途径明显改变,但p42/p44 MAP激酶活性和85 kDa自激酶活性均与既定的预后指标无关。