CLONING AND SEQUENCE-ANALYSIS OF RAT BONE SIALOPROTEIN (OSTEOPONTIN) CDNA REVEALS AN ARG-GLY-ASP CELL-BINDING SEQUENCE
CLONING AND SEQUENCE-ANALYSIS OF RAT BONE SIALOPROTEIN (OSTEOPONTIN) CDNA REVEALS AN ARG-GLY-ASP CELL-BINDING SEQUENCE
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DOI：
10.1073/pnas.83.23.8819
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发表时间：
1986-12-01
影响因子：
11.1
通讯作者：
HEINEGARD, D
中科院分区：
文献类型：
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作者：
OLDBERG, A;FRANZEN, A;HEINEGARD, D
从克隆的cDNA推导出骨特异性唾液酸蛋白的一级结构。从大鼠骨肉瘤（ROS 17/2.8）噬菌体Gt 11文库中分离的cDNA克隆之一具有1473个碱基对长的插入物，其编码具有317个氨基酸残基的蛋白质。该cDNA克隆似乎代表唾液蛋白mRNA的完整编码区，包括推定的AUG起始密码子和信号肽序列。从cDNA推导的氨基酸序列含有几个Ser-Xaa-Glu序列，可能代表O-糖苷连接的寡糖的附着点和一个Asn-Xaa-Ser序列，代表N-糖苷连接的寡糖的可能位点。一个有趣的观察是Gly-Arg-Gly-Asp-Ser序列，其与纤连蛋白中鉴定的细胞结合序列相同。该序列的存在促使我们研究唾液蛋白的细胞结合特性。ROS 17/2.8细胞附着并在涂有唾液蛋白的表面上获得铺展形态。我们可以证明，合成的精氨酸-甘氨酸-天冬氨酸肽有效地抑制附着的细胞唾液蛋白包被的基板。结果表明，Arg-Gly-Asp序列也赋予骨特异性唾液酸蛋白细胞结合特性。为了更好地反映骨唾液酸蛋白的潜在功能，我们建议将这种蛋白质命名为“骨桥蛋白”。
The primary structure of a bone-specific sialoprotein was deduced from cloned cDNA. One of the cDNA clones isolated from a rat osteosarcoma (ROS 17/2.8) phage .lambda.gt11 library had a 1473-base-pair-long insert that encoded a protein with 317 amino acid residues. This cDNA clone appears to represent the complete coding region of sialoprotein mRNA, including a putative AUG initiation codon and a signal peptide sequence. The amino acid sequence deduced from the cDNA contains several Ser-Xaa-Glu sequences, possibly representing attachment points for O-glycosidically linked oligosaccharides and one Asn-Xaa-Ser sequence representing a likely site for the N-glycosidically linked oligosaccharide. An interesting observation is the Gly-Arg-Gly-Asp-Ser sequence, which is identical to the cell-binding sequence identified in fibronectin. The presence of this sequence prompted us to investigate the cell-binding properties of sialoprotein. The ROS 17/2.8 cells attached and attained a spread morphology on surfaces coated with sialoprotein. We could demonstrate that synthetic Arg-Gly-Asp-containing peptides efficiently inhibited the attachment of cells to sialoprotein-coated substrates. The results show that the Arg-Gly-Asp sequence also confers cell-binding properties on bone-specific sialoprotein. To better reflect the potential function of bone sialoprotein we propose the name "osteopontin" for this protein.