Joliot A, Le Roux I, Volovitch M, Bloch-Gallego E, Prochiantz A
CNRS URA 1414, Ecole Normale Supérieure, Paris, France.
Ann Genet. 1993;36(1):70-2.
The sixty aminoacid-long peptide corresponding to the homeobox of Antennapedia (pAntp) translocates through the membrane of neurons in culture and reaches their nuclei. This process is followed by an enhanced morphological differentiation of the neurons. Internalization by neurons is 4-fold that observed with fibroblasts. This difference is abolished upon treatment with Endo-N which specifically cleaves alpha, 2-8 bounds in polysialic acid (PSA). To understand the mode of action of the peptide, the authors constructed three mutants modified in their capacity to specifically bind promoters and/or to translocate through the cell membrane. The biological properties of the mutants demonstrate that the neurotrophic action of pAntp requires its internalization and the integrity of its specific DNA-binding capacity.
与触角足蛋白（pAntp）同源异型框相对应的60个氨基酸长的肽穿过培养神经元的膜并到达其细胞核。此过程之后神经元的形态分化增强。神经元的内化作用是成纤维细胞的4倍。用内切神经氨酸酶N处理后这种差异消失，该酶能特异性切割多唾液酸（PSA）中的α2-8键。为了解该肽的作用方式，作者构建了三个突变体，其在特异性结合启动子和/或穿过细胞膜的能力方面有所改变。突变体的生物学特性表明，pAntp的神经营养作用需要其内化及其特异性DNA结合能力的完整性。
