Lopez de los Santos, Yossef; Bernard, David N.; Egesborg, Philippe; Létourneau, Myriam; Lafortune, Clara; Cuneo, Monica; Urvoas, Agathe; Chatenet, David; Mahy, Jean-Pierre; St-Pierre, Yves 
ORCID: https://orcid.org/0000-0002-1948-2041; Ricoux, Rémy et Doucet, Nicolas ORCID: https://orcid.org/0000-0002-1952-9380
(2020).
Binding of a Soluble meso-Tetraarylporphyrin to Human Galectin-7 Induces Oligomerization and Modulates Its Pro-Apoptotic Activity
Biochemistry
, vol. 59
, nº 48.
pp. 4591-4600.
DOI: 10.1021/acs.biochem.0c00736.
Résumé
The selective targeting of protein-protein interactions remains a significant determinant for the proper modulation and regulation of cell apoptosis. Prototypic galectins such as human galectin-7 (GAL-7) are characterized by their ability to form homodimers that control the molecular fate of a cell by mediating subtle yet critical glycan-dependent interactions between pro- and anti-apoptotic molecular partners. Altering the structural architecture of GAL-7 can therefore result in resistance to apoptosis in various human cancer cells, further illustrating its importance in cell survival. In this study, we used a combination of biophysical and cellular assays to illustrate that binding of a water-soluble meso-tetraarylporphyrin molecule to GAL-7 induces protein oligomerization and modulation of GAL-7-induced apoptosis in human Jurkat T cells. Our results suggest that the integrity of the GAL-7 homodimer architecture is essential for its molecular function, in addition to providing an interesting porphyrin binding modulator for controlling apoptosis in mammalian cells.
| Type de document: | Article |
|---|---|
| Mots-clés libres: | - |
| Centre: | Centre INRS-Institut Armand Frappier |
| Date de dépôt: | 20 juill. 2021 04:03 |
| Dernière modification: | 15 févr. 2022 15:36 |
| URI: | https://espace.inrs.ca/id/eprint/11630 |
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