Structural variability of BM-40/SPARC/osteonectin glycosylation: implications for collagen affinity.

@article{Kaufmann2004StructuralVO,
  title={Structural variability of BM-40/SPARC/osteonectin glycosylation: implications for collagen affinity.},
  author={Brigitte Kaufmann and Stefan Müller and Franz-Georg Hanisch and Ursula Hartmann and Mats Paulsson and Patrik Maurer and Frank Zaucke},
  journal={Glycobiology},
  year={2004},
  volume={14 7},
  pages={
          609-19
        }
}
We performed a detailed investigation of N-glycan structures on BM-40 purified from different sources including human bone, human platelets, mouse Engelbreth-Holm-Swarm (EHS) tumor, and human BM-40 recombinantly expressed in 293 and osteosarcoma cells. These preparations were digested with endoglycosidases and N-glycans were further characterized by sequential exoglycosidase digestion and high-performance liquid chromatography (HPLC) analyses. Bone BM-40 carries high-mannose structures as well… 
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TLDR
It is demonstrated that SPARC mediates the disassembly and degradation of ECM networks by functioning as a matricellular chaperone, and indicates thatSPARC may represent a new class of scavenger chaperones, which mediate ECM degradation, remodeling and repair by disassembling ECm networks and shuttling ECM proteins into the cell.
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TLDR
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