Böhmer F D, Böhmer S A, Heldin C H
Ludwig Institute for Cancer Research, Biomedical Center, Uppsala, Sweden.
FEBS Lett. 1993 Oct 4;331(3):276-80. doi: 10.1016/0014-5793(93)80352-u.
Comparison of the phosphotyrosine-specific dephosphorylation of the autophosphorylated receptors for epidermal growth factor (EGF) and platelet-derived growth factor (PDGF) in Swiss 3T3 cell membranes by the endogenous phosphatases revealed striking differences. EGF receptor dephosphorylation was clearly faster than PDGF receptor dephosphorylation and strongly inhibited by Triton X-100 and octylglucoside, whereas PDGF receptor dephosphorylation was to a lesser extent detergent-susceptible. PDGF receptor dephosphorylation was effectively inhibited by phenylarsineoxide, protamine and poly-lysine and partially by N-ethylmaleinimide, whereas EGF receptor dephosphorylation was not affected by these agents. We suggest that these differences in dephosphorylation of EGF and PDGF receptors are due to their differential interaction with membrane-associated protein-tyrosine phosphatases and important for differential regulation of receptor signalling.
通过内源性磷酸酶对瑞士3T3细胞膜中表皮生长因子（EGF）和血小板衍生生长因子（PDGF）的自磷酸化受体进行磷酸酪氨酸特异性去磷酸化的比较，结果显示出显著差异。EGF受体的去磷酸化明显快于PDGF受体的去磷酸化，并且受到Triton X-100和辛基葡糖苷的强烈抑制，而PDGF受体的去磷酸化对去污剂的敏感性较低。苯砷氧化物、鱼精蛋白和聚赖氨酸可有效抑制PDGF受体的去磷酸化，N-乙基马来酰亚胺可部分抑制，而这些试剂对EGF受体的去磷酸化没有影响。我们认为，EGF和PDGF受体去磷酸化的这些差异是由于它们与膜相关蛋白酪氨酸磷酸酶的不同相互作用所致，并且对受体信号的差异调节很重要。
