Liu M, Zeng J, Robey F A
Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Peptides. 1999;20(2):185-91. doi: 10.1016/s0196-9781(98)00158-2.
Treatment of HUT78 cells with CD4-binding peptide constructs derived from the C4 domain of HIV-1 gp120 results in autophosphorylation of a src-related kinase, p56lck. This leads to p56lck activation and the subsequent phosphorylation of tyrosine residues in several intracellular proteins. The phosphorylation is specific to the C4 peptides as no new phosphorylation occurs when the cells are treated with control peptides or polymers. The induction of tyrosine phosphorylation by the C4 peptide constructs depends on the capability of the peptide to assume a helical conformation because similar peptide constructs that were not able to form helices did not induce cellular tyrosine phosphorylation.
用源自HIV-1 gp120的C4结构域的CD4结合肽构建体处理HUT78细胞，会导致一种与src相关的激酶p56lck发生自磷酸化。这会导致p56lck激活，并随后使几种细胞内蛋白质中的酪氨酸残基发生磷酸化。这种磷酸化对C4肽具有特异性，因为当用对照肽或聚合物处理细胞时不会发生新的磷酸化。C4肽构建体对酪氨酸磷酸化的诱导取决于肽呈现螺旋构象的能力，因为不能形成螺旋的类似肽构建体不会诱导细胞酪氨酸磷酸化。
