Anja Krajnc (Author), Aljaž Gaber (Author), Brigita Lenarčič (Author), Miha Pavšič (Author)

Abstract

Testicans are modular proteoglycans of the extracellular matrix of various tissues where they contribute to matrix integrity and exert cellular effects like neurite outgrowth and cell migration. Using testican-2 as a representative member of the family, we tackle the complete lack of general structural information and structure–function relationship. First, we show using isothermal titration calorimetry and modeling that extracellular calcium-binding domain (EC) has only one active calcium-binding site, while the other potential site is inactive, and that testican-2 is within extracellular matrix always in the calcium-loaded form. Next, we demonstrate using various prediction methods that N- and C-terminal regions plus interdomain connections are flexible. We support this by small-angle X-ray-scattering analysis of C-terminally truncated testican-2, which indicates that the triplet follistatin-EC-thyroglobulin domain forms a moderately compact core while the unique N-terminal is disordered. Finally, using cell exclusion zone assay, we show that it is this domain triplet that is responsible for promoting cell migration and not the N- and C-terminal regions.

Keywords

testikan;SPOCK;vezava kalcijevih ionov;model strukture;celična migracija;testican;calcium-binding;structural model;cell migration;

Data

Language: English
Year of publishing:
Typology: 1.01 - Original Scientific Article
Organization: UL FKKT - Faculty of Chemistry and Chemical Technology
UDC: 577.112.85
COBISS: 42261507 Link will open in a new window
ISSN: 1661-6596
Views: 248
Downloads: 87
Average score: 0 (0 votes)
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Other data

Secondary language: Slovenian
Secondary keywords: testikan;SPOCK;vezava kalcijevih ionov;model strukture;celična migracija;
Type (COBISS): Article
Pages: str. 1-17
Volume: ǂVol. ǂ21
Issue: ǂiss. ǂ24
Chronology: Dec. 2020
DOI: 10.3390/ijms21249413
ID: 14444840