Glycobiology Advance Access originally published online on March 24, 2004
Glycobiology 2004 14(7):609-619; doi:10.1093/glycob/cwh063
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Glycobiology vol. 14 no. 7 © Oxford University Press 2004; all rights reserved.
Structural variability of BM-40/SPARC/osteonectin glycosylation: implications for collagen affinity
2 Center for Biochemistry, Medical Faculty, University of Cologne, Joseph-Stelzmann-Str. 52, D-50931 Cologne, Germany; and 3 Center for Molecular Medicine, Medical Faculty, University of Cologne, Joseph-Stelzmann-Str. 52, D-50931 Cologne, Germany
Received on November 26, 2003; revised on February 12, 2004; accepted on February 14, 2004
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 as biantennary complex type N-glycans, whereas the protein from platelets and 293 cells has exclusively bi- and triantennary complex type structures. BM-40 derived from the EHS tumor carries biantennary complex type and additional hybrid structures. Using the osteosarcoma-derived MHH-ES1 cell line we successfully expressed a recombinant BM-40 that bears at least in part the bone-specific high-mannose N-glycosylation in addition to complex type and hybrid structures. Using chromatography on Concanavalin-A Sepharose, we further purified a fraction enriched in high-mannose structures. This array of differentially glycosylated BM-40 proteins was assayed by surface plasmon resonance measurements to investigate the binding to collagen I. BM-40 carrying high-mannose structures binds collagen I with higher affinity, suggesting that differentially glycosylated forms may have different functional roles in vivo.
1 To whom correspondence should be addressed; e-mail: frank.zaucke{at}uni-koeln.de
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
T. Reding, U. Wagner, A. B. Silva, L-K. Sun, M. Bain, S.-Y. Kim, D. Bimmler, and R. Graf Inflammation-dependent expression of SPARC during development of chronic pancreatitis in WBN/Kob rats and a microarray gene expression analysis Physiol Genomics, July 9, 2009; 38(2): 196 - 204. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. W.M. Schellings, D. Vanhoutte, M. Swinnen, J. P. Cleutjens, J. Debets, R. E.W. van Leeuwen, J. d'Hooge, F. Van de Werf, P. Carmeliet, Y. M. Pinto, et al. Absence of SPARC results in increased cardiac rupture and dysfunction after acute myocardial infarction J. Exp. Med., January 16, 2009; 206(1): 113 - 123. [Abstract] [Full Text] [PDF] |
||||
![]() |
E. Hohenester, T. Sasaki, C. Giudici, R. W. Farndale, and H. P. Bachinger Structural basis of sequence-specific collagen recognition by SPARC PNAS, November 25, 2008; 105(47): 18273 - 18277. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. Giudici, N. Raynal, H. Wiedemann, W. A. Cabral, J. C. Marini, R. Timpl, H. P. Bachinger, R. W. Farndale, T. Sasaki, and R. Tenni Mapping of SPARC/BM-40/Osteonectin-binding Sites on Fibrillar Collagens J. Biol. Chem., July 11, 2008; 283(28): 19551 - 19560. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. Stork, K. A. Zettlitz, D. Muller, M. Rether, F.-G. Hanisch, and R. E. Kontermann N-Glycosylation as Novel Strategy to Improve Pharmacokinetic Properties of Bispecific Single-chain Diabodies J. Biol. Chem., March 21, 2008; 283(12): 7804 - 7812. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Martinek, J. Shahab, J. Sodek, and M. Ringuette Is SPARC an Evolutionarily Conserved Collagen Chaperone? Journal of Dental Research, April 1, 2007; 86(4): 296 - 305. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. Parry, F. G. Hanisch, S.-H. Leir, M. Sutton-Smith, H. R. Morris, A. Dell, and A. Harris N-Glycosylation of the MUC1 mucin in epithelial cells and secretions Glycobiology, July 1, 2006; 16(7): 623 - 634. [Abstract] [Full Text] [PDF] |
||||
![]() |
Q. Shi, S. Bao, J. A. Maxwell, E. D. Reese, H. S. Friedman, D. D. Bigner, X.-F. Wang, and J. N. Rich Secreted Protein Acidic, Rich in Cysteine (SPARC), Mediates Cellular Survival of Gliomas through AKT Activation J. Biol. Chem., December 10, 2004; 279(50): 52200 - 52209. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. Ge, N.-S. Seo, X. Liang, D. R. Hopkins, M. Hook, and D. S. Greenspan Bone Morphogenetic Protein-1/Tolloid-related Metalloproteinases Process Osteoglycin and Enhance Its Ability to Regulate Collagen Fibrillogenesis J. Biol. Chem., October 1, 2004; 279(40): 41626 - 41633. [Abstract] [Full Text] [PDF] |
||||





