Structural characterization of TSC-36/Flik -: Analysis of two charge isoforms

被引：72

作者：

Hambrock, HO

Kaufmann, B

Müller, S

Hanisch, FG

Nose, K

Paulsson, M

Maurer, P

Hartmann, U

机构：

[1] Univ Cologne, Fac Med, Ctr Biochem, D-50931 Cologne, Germany

[2] Univ Cologne, Fac Med, Ctr Mol Med, D-50931 Cologne, Germany

[3] Showa Univ, Sch Pharmaceut Sci, Dept Microbiol, Tokyo 1428555, Japan

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2004年 / 279卷 / 12期

关键词：

D O I：

10.1074/jbc.M309318200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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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页码：11727 / 11735

页数：9

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