Open AccessBinding of a Soluble meso-Tetraarylporphyrin to Human Galectin-7 Induces Oligomerization and Modulates Its Pro-Apoptotic Activity
Author(s) -
Yossef López de los Santos,
David Bernard,
Philippe Egesborg,
Myriam Létourneau,
Clara Lafortune,
M.J. Cuneo,
Agathe Urvoas,
David Chatenet,
JeanPierre Mahy,
Yves StPierre,
Rémy Ricoux,
Nicolas Doucet
Publication year - 2020
Publication title -
biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.43
H-Index - 253
eISSN - 1520-4995
pISSN - 0006-2960
DOI - 10.1021/acs.biochem.0c00736
Subject(s) - jurkat cells , galectin , apoptosis , microbiology and biotechnology , galectin 3 , cell , cancer cell , galectin 1 , function (biology) , chemistry , plasma protein binding , biology , biochemistry , cancer , t cell , immunology , genetics , immune system
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.