| Literature DB >> 12538579 |
Harald O Hambrock1, D Patric Nitsche, Uwe Hansen, Peter Bruckner, Mats Paulsson, Patrik Maurer, Ursula Hartmann.
Abstract
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.Entities:
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Year: 2003 PMID: 12538579 DOI: 10.1074/jbc.M212291200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157