AI Article Synopsis
- Recombinant glycoprotein TSC-36/Flik was expressed in human cells to analyze its structural and functional attributes compared to other members of the BM-40/SPARC/osteonectin family.
- TSC-36 exists in two different charge isoforms due to variations in sialylation of N-linked oligosaccharides, but shows no significant structural changes when calcium levels fluctuate.
- The study suggests that TSC-36 lacks important functional features found in other BM-40 family members, indicating it has developed unique properties despite its genetic similarities.
Article 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.
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| http://dx.doi.org/10.1074/jbc.M309318200 | DOI Listing |
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