BETA-AMYLOID PRECURSOR PROTEIN BINDS TO THE NEURITE-PROMOTING IKVAV SITE OF LAMININ
BETA-AMYLOID PRECURSOR PROTEIN BINDS TO THE NEURITE-PROMOTING IKVAV SITE OF LAMININ
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DOI：
10.1073/pnas.90.21.10150
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发表时间：
1993-11-01
影响因子：
11.1
通讯作者：
KLEINMAN, HK
中科院分区：
文献类型：
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作者：
KIBBEY, MC;JUCKER, M;KLEINMAN, HK
我们先前表征了来自脑的110-kDa膜相关层粘连蛋白结合蛋白（LBP 110），其结合层粘连蛋白A链-Ile-Lys-Val-Ala-瓦尔-（IKVAV）位点并增加损伤。在这里，我们证明，针对不同的表位的β-淀粉样前体蛋白（APP）的抗血清识别LBP 110和APP被LBP 110抗血清识别。APP特异性结合IKVAV，而不是另一种含有氨基酸序列-Tyr-Ile-Gly-Ser-Arg-的生物活性层粘连蛋白衍生肽。用反义APP RNA转染的PC-12细胞产生较少的APP和LBP 110，并且当在层粘连蛋白或IKVAV肽上培养时，它们形成较少的突起。因此，LBP 110是APP家族的成员，并且现在定义了APP在神经突生长中的功能。
We previously characterized a 110-kDa membrane-associated laminin-binding protein (LBP110) from brain which binds the laminin A chain -Ile-Lys-Val-Ala-Val-(IKVAV) site and increases in injury. Here we demonstrate that antisera directed against different epitopes of beta-amyloid precursor protein (APP) recognize LBP110 and that APP is recognized by LBP110 antiserum. APP specifically binds IKVAV and not another biologically active laminin-derived peptide containing the amino acid sequence -Tyr-Ile-Gly-Ser-Arg-. PC-12 cells transfected with antisense APP RNA produce less APP and LBP110, and they form fewer processes when cultured on either laminin or the IKVAV peptide. Thus, LBP110 is a member of the APP family and a function for APP in neurite outgrowth is now defined.