Aoyagi T, Umeda K, Kato N, Fukaya T, Kobayashi H, Koizumi H, Miura Y
J Invest Dermatol. 1983 Jul;81(1):49-53. doi: 10.1111/1523-1747.ep12538417.
Endogenous protein phosphorylation of pig epidermis by epidermal growth factor (EGF) was studied to elucidate biologic roles of EGF on epidermal cells. EGF stimulated phosphorylation of keratin proteins (Mr: 65,000, 60,000, 56,000, and 51,000) identified by the Ouchterlony immunodiffusion analysis, a low Mr protein (16,000 dalton) of the urea-SDS-mercaptoethanol soluble fraction, and a 30,000 dalton Tris-HCl soluble protein. The phosphorylated epidermal proteins such as keratin proteins and a 30,000 dalton protein of the Tris-HCl soluble fraction were slightly dephosphorylated following the addition of unlabeled phosphate. Anti-EGF serum eliminated the EGF-stimulated phosphorylation of keratin proteins, a low Mr protein, and a 30,000 dalton Tris-HCl soluble protein. The overall results indicate that EGF specifically stimulated phosphorylation of several epidermal proteins, one of which was keratin protein.
为阐明表皮生长因子（EGF）对表皮细胞的生物学作用，研究了EGF对猪表皮内源性蛋白质磷酸化的影响。通过免疫双扩散分析鉴定，EGF刺激了角蛋白（分子量分别为65,000、60,000、56,000和51,000）、尿素-SDS-巯基乙醇可溶组分中的一种低分子量蛋白（16,000道尔顿）以及一种30,000道尔顿的Tris-HCl可溶蛋白的磷酸化。加入未标记的磷酸盐后，角蛋白等磷酸化的表皮蛋白以及Tris-HCl可溶组分中的30,000道尔顿蛋白会发生轻微的去磷酸化。抗EGF血清消除了EGF刺激的角蛋白、低分子量蛋白以及30,000道尔顿Tris-HCl可溶蛋白的磷酸化。总体结果表明，EGF特异性地刺激了几种表皮蛋白的磷酸化，其中之一是角蛋白。
