Joliot A H, Triller A, Volovitch M, Pernelle C, Prochiantz A
CNRS URA 1414, Ecole Normale Supérieure, Paris, France.
New Biol. 1991 Nov;3(11):1121-34.
A synthetic peptide that is 60 amino acids in length and corresponds to the homeobox sequence of antennapedia protein (pAntp) is specifically and efficiently captured by neurons in culture and conveyed to their nuclei. The internalization process is followed by a strong induction of neuronal morphological differentiation. In the study described here, all treatments masking or removing the alpha-2,8-polysialic acid (PSA) chains specific to the neuronal cell adhesion molecule (NCAM) were found to block the penetration of pAntp and abolish its morphogenetic effects. Structural comparison between PSA and double-stranded DNA suggests that a sequence of eight sialic acid residues can mimic one large groove of the DNA. We propose that this structural similarity is the basis for the property of NCAM polysialic acid to participate in the internalization of the homebox polypeptide.
一种长度为60个氨基酸且对应触角足蛋白（pAntp）同源异型框序列的合成肽，在培养物中被神经元特异性且高效地捕获并转运至其细胞核。内化过程之后是神经元形态分化的强烈诱导。在本研究中，发现所有掩盖或去除神经元细胞黏附分子（NCAM）特有的α-2,8-多聚唾液酸（PSA）链的处理都会阻断pAntp的穿透并消除其形态发生效应。PSA与双链DNA之间的结构比较表明，八个唾液酸残基的序列可以模拟DNA的一个大沟。我们提出这种结构相似性是NCAM多聚唾液酸参与同源异型框多肽内化特性的基础。
