Deprez P N, Inestrosa N C
Departamento de Biología Celular y Molecular, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago.
J Biol Chem. 1995 May 12;270(19):11043-6. doi: 10.1074/jbc.270.19.11043.
The collagen-tailed form of acetylcholinesterase (AChE) binds to heparin and heparan sulfate proteoglycans. We have employed synthetic peptides corresponding to the central collagenic region of the tail of AChE, to identify the heparin-binding domains of the tail of asymmetric AChE. Two putative heparin-binding consensus sequences were localized in the collagenic tail. Peptides containing such sequences (P-(145-159) and P-(249-262)) were able to release asymmetric AChE bound to heparin-agarose. A triple mutation, Asn-Asp-Gly-Gly instead of Arg-His-Gly-Arg, completely abolishes the capacity of the peptide P-(145-159) to elute AChE from the heparin column. Our results suggest that the interaction between the collagen-tailed AChE and proteoglycans is mediated by clusters of basic residues that form two belts around the triple helix of the collagenic tail.
乙酰胆碱酯酶（AChE）的胶原尾型与肝素和硫酸乙酰肝素蛋白聚糖结合。我们使用了与AChE尾部中央胶原区域相对应的合成肽，以鉴定不对称AChE尾部的肝素结合结构域。两个假定的肝素结合共有序列位于胶原尾中。含有此类序列的肽（P-(145-159)和P-(249-262)）能够释放与肝素琼脂糖结合的不对称AChE。由Asn-Asp-Gly-Gly取代Arg-His-Gly-Arg的三重突变完全消除了肽P-(145-159)从肝素柱上洗脱AChE的能力。我们的结果表明，胶原尾型AChE与蛋白聚糖之间的相互作用是由碱性残基簇介导的，这些残基在胶原尾的三螺旋周围形成两条带。
