CHARACTERIZATION OF A 21 AMINO-ACID PEPTIDE SEQUENCE OF THE LAMININ G2 DOMAIN THAT IS INVOLVED IN HNK-1 CARBOHYDRATE-BINDING AND CELL-ADHESION
CHARACTERIZATION OF A 21 AMINO-ACID PEPTIDE SEQUENCE OF THE LAMININ G2 DOMAIN THAT IS INVOLVED IN HNK-1 CARBOHYDRATE-BINDING AND CELL-ADHESION
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DOI：
10.1093/glycob/5.4.435
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发表时间：
1995-06-01
期刊：
影响因子：
4.3
通讯作者：
SCHACHNER, M
中科院分区：
文献类型：
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作者：
HALL, H;VORHERR, T;SCHACHNER, M
由几个识别分子表达的N-连接的HNK-1碳水化合物介导了早期出生后小脑神经元与层粘连蛋白α1链末端球状结构域的G2结构域的黏附(H.Hall等人，提交)。为了更准确地定义这个结合位点，使用G2衍生的合成肽进行结合和竞争研究。由G2的3431-3451氨基酸残基组成的多肽5-G2以浓度依赖且饱和的方式抑制携带HNK-1糖脂与层粘连蛋白之间的相互作用。仅与该序列部分重叠的多肽干扰较少，包含来自G2的其他氨基酸序列的多肽，以及来自G1和G3的多肽或5-G2的扰乱版本的多肽，没有表现出显著的影响。此外，5-G2肽还与HNK-1糖脂直接结合，并以浓度依赖和饱和的方式干扰生后早期小脑神经元与层粘连蛋白的黏附。这些观察结果表明，层粘连蛋白G2结构域的3431-3451位氨基酸残基参与了HNK-1糖介导的细胞黏附。
The N-linked HNK-1 carbohydrate expressed by several recognition molecules mediates the adhesion of early postnatal cerebellar neurons to the G2 domain of the terminal globular domain of the laminin alpha 1 chain (H.Hall ed al., submitted). To define this binding site more precisely, G2-derived synthetic peptides were used for binding and competition studies. Peptide 5-G2, comprising the amino acid residues 3431-3451 of G2, inhibited the interaction between the HNK-1-carrying glycolipid and laminin in a concentration-dependent and saturable manner. Peptides which overlap only partially with this sequence interfered less, Peptides comprising other amino acid sequences from G2, and peptides derived from G1 and G3 or a scrambled version of peptide 5-G2, did not show significant effects. Direct binding of peptide 5-G2 to the HNK-1 glycolipid was also demonstrated, Furthermore, peptide 5-G2 interfered in a concentration-dependent and saturable manner with the adhesion of early postnatal cerebellar neurons to laminin. These observations indicate that amino acid residues 3431-3451 of the laminin G2 domain are involved in HNK-1 carbohydrate-mediated cell adhesion.