SC1/hevin - An extracellular calcium-modulated protein that binds collagen I

SC1/hevin - An extracellular calcium-modulated protein that binds collagen I
复制标题

DOI:
10.1074/jbc.m212291200
复制
发表时间:
2003-03-28
影响因子:
4.8
通讯作者:
Hartmann, U
Hartmann, U
中科院分区:
生物学2区
文献类型:
--
作者:
Hambrock, HO;Nitsche, DP;Hartmann, U

文献摘要

被引文献

相似文献

SC1是细胞外基质蛋白BM-40家族的一员,在真核表达系统中重组表达。在非变性条件下,全长蛋白和截断的蛋白被纯化到均匀性。基质辅助激光解吸电离飞行时间质谱分析显示全长SC1的质量为87.8 kDa,其中16.8 kDa是由翻译后修饰贡献的。在电镜下,阴性染色后,SC1显示为附着在线状结构上的球体。荧光光谱可以证明SC1构象的钙依赖性。在培养的骨肉瘤细胞的细胞外基质中发现SC1与含I型胶原原纤维相关,并且通过免疫金标和电镜可以证明SC1与重组的I型胶原原纤维结合。SC1在多种组织中广泛表达。
SC1, a member of the BM-40 family of extracellular matrix proteins, was recombinantly expressed in a eukaryotic expression system. The full-length protein as well as truncated versions were purified to homogeneity under non-denaturing conditions. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry of full-length SC1 revealed a mass of 87.8 kDa of which 16.8 kDa is contributed by posttranslational modifications. In electron microscopy, after negative staining, SC1 was revealed as a globule attached to a thread-like structure. A calcium dependence of the SC1 conformation could be demonstrated by fluorescence spectroscopy. In the extracellular matrix of cultured osteosarcoma cells SC1 was found associated with collagen I-containing fibrils, and binding of SC1 to reconstituted collagen I fibrils could be demonstrated by immunogold labeling and electron microscopy. SC1 showed a broad expression in a variety of tissues.