SC1/hevin. An extracellular calcium-modulated protein that binds collagen I |
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Authors: | Hambrock Harald O Nitsche D Patric Hansen Uwe Bruckner Peter Paulsson Mats Maurer Patrik Hartmann Ursula |
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Institution: | Center for Biochemistry, Medical Faculty, University of Cologne, D-50931 Cologne, Germany. |
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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. |
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