| Literature DB >> 14701841 |
Harald O Hambrock1, Brigitte Kaufmann, Stefan Müller, Franz-Georg Hanisch, Kiyoshi Nose, Mats Paulsson, Patrik Maurer, Ursula Hartmann.
Abstract
Recombinant forms of the glycoprotein TSC-36/Flik were expressed in human cells and used to compare their structural and functional properties with those described for other members of the BM-40/SPARC/osteonectin protein family. TSC-36 was found to occur in two charge isoforms that differ in the extent of sialylation of otherwise identical N-linked, complex type oligosaccharides. Conformational analysis with both circular dichroism and intrinsic fluorescence spectroscopy showed a lack of significant structural changes upon calcium addition or depletion. This finding is in contrast to results obtained for several other BM-40 family members and indicates that the extracellular calcium-binding domain in TSC-36 is non-functional. The lack of conservation of important functional features common to several other members of the BM-40 family indicates that TSC-36, despite its sequence homology to BM-40, has evolved clearly distinct properties.Entities:
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Year: 2003 PMID： 14701841 DOI： 10.1074/jbc.M309318200
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157