Multiple domains of the large fibroblast proteoglycan, versican.

Multiple domains of the large fibroblast proteoglycan, versican.
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DOI:
10.1002/j.1460-2075.1989.tb08447.x
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发表时间:
1989-10
期刊:
The EMBO Journal
影响因子:
--
通讯作者:
Dieter R. Zimmermann;E. Ruoslahti
Dieter R. Zimmermann;E. Ruoslahti
中科院分区:
其他
文献类型:
--
作者:
Dieter R. Zimmermann;E. Ruoslahti

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人成纤维细胞表达的大硫酸软骨素蛋白聚糖的一级结构已被确定。重叠cDNA克隆编码整个2389个氨基酸长的核心蛋白和20个残基的信号肽。该序列预测氨基末端部分存在潜在的透明质酸结合结构域。该结构域包含与来自胶质透明质酸结合蛋白的部分肽序列几乎相同的序列。推定的糖胺聚糖附着位点位于蛋白质的中间。羧基末端部分包括两个表皮生长因子(EGF)样重复序列,一个凝集素样序列和一个补体调节蛋白样结构域。在一类新的细胞粘附分子中也发现了相同的结合元件。成纤维细胞核心蛋白的氨基和羧基末端部分与软骨肉瘤细胞的大硫酸软骨素蛋白聚糖的核心蛋白密切相关。然而,核心蛋白中间的糖胺聚糖附着区是不同的,只有成纤维细胞核心蛋白含有EGF样重复序列。基于其结构域与其他蛋白质的各种结合元件的相似性,我们认为,大的成纤维细胞蛋白聚糖,本文称为多功能蛋白聚糖,可能在细胞识别中发挥作用,可能通过连接细胞外基质成分和细胞表面糖蛋白。
The primary structure of a large chondroitin sulfate proteoglycan expressed by human fibroblasts has been determined. Overlapping cDNA clones code for the entire 2389 amino acid long core protein and the 20‐residue signal peptide. The sequence predicts a potential hyaluronic acid‐binding domain in the amino‐terminal portion. This domain contains sequences virtually identical to partial peptide sequences from a glial hyaluronate‐binding protein. Putative glycosaminoglycan attachment sites are located in the middle of the protein. The carboxy‐terminal portion includes two epidermal growth factor (EGF)‐like repeats, a lectin‐like sequence and a complement regulatory protein‐like domain. The same set of binding elements has also been identified in a new class of cell adhesion molecules. Amino‐ and carboxy‐terminal portions of the fibroblast core protein are closely related to the core protein of a large chondroitin sulfate proteoglycan of chondrosarcoma cells. However, the glycosaminoglycan attachment regions in the middle of the core proteins are different and only the fibroblast core protein contains EGF‐like repeats. Based on the similarities of its domains with various binding elements of other proteins, we suggest that the large fibroblast proteoglycan, herein referred to as versican, may function in cell recognition, possibly by connecting extracellular matrix components and cell surface glycoproteins.