Literature DB >> 24462947

Direct cytocidal effect of galectin-9 localized on collagen matrices on human immune cell lines.

Youko Fukata1, Aiko Itoh1, Yasuhiro Nonaka2, Takashi Ogawa2, Takanori Nakamura2, Osamu Matsushita3, Nozomu Nishi4.   

Abstract

BACKGROUND: There is a continuous demand for new immunosuppressive agents for organ transplantation. Galectin-9, a member of the galactoside-binding animal lectin family, has been shown to suppress pathogenic T-cell responses in autoimmune disease models and experimental allograft transplantation. In this study, an attempt has been made to develop new collagen matrices, which can cause local, contact-dependent immune suppression, using galectin-9 and collagen-binding galectin-9 fusion proteins as active ingredients.
METHODS: Galectin-9 and galectin-9 fusion proteins having collagen-binding domains (CBDs) derived from bacterial collagenases and a collagen-binding peptide (CBP) were tested for their ability to bind to collagen matrices, and to induce Jurkat cell death in solution and in the collagen-bound state.
RESULTS: Galectin-9-CBD fusion proteins exhibited collagen-binding activity comparable to or lower than that of the respective CBDs, while their cytocidal activity toward Jurkat cells in solution was 80~10% that of galectin-9. Galectin-9 itself exhibited oligosaccharide-dependent collagen-binding activity. The growth of Jurkat cells cultured on collagen membranes treated with galectin-9 was inhibited by~90%. The effect was dependent on direct cell-to-membrane contact. Galectin-9-CBD/CBP fusion proteins bound to collagen membranes via CBD/CBP moieties showed a low or negligible effect on Jurkat cell growth.
CONCLUSIONS: Among the proteins tested, galectin-9 exhibited the highest cytocidal effect on Jurkat cells in the collagen-bound state. The effect was not due to galectin-9 released into the culture medium but was dependent on direct cell-to-membrane contact. GENERAL SIGNIFICANCE: The study demonstrates the possible use of galectin-9-modified collagen matrices for local, contact-dependent immune suppression in transplantation.
Copyright © 2014 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Collagen; Collagen-binding domain; Galectin; Immune suppression

Mesh:

Substances:

Year:  2014        PMID: 24462947     DOI: 10.1016/j.bbagen.2014.01.019

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

Review 1.  Galectin-9: From cell biology to complex disease dynamics.

Authors:  Sebastian John; Rashmi Mishra
Journal:  J Biosci       Date:  2016-09       Impact factor: 1.826

2.  Design of a peptidic inhibitor that targets the dimer interface of a prototypic galectin.

Authors:  Maria Claudia Vladoiu; Marilyne Labrie; Myriam Létourneau; Philippe Egesborg; Donald Gagné; Étienne Billard; Andrée-Anne Grosset; Nicolas Doucet; David Chatenet; Yves St-Pierre
Journal:  Oncotarget       Date:  2015-12-01

3.  Basic Fibroblast Growth Factor Fused with Tandem Collagen-Binding Domains from Clostridium histolyticum Collagenase ColG Increases Bone Formation.

Authors:  Hiroyuki Sekiguchi; Kentaro Uchida; Osamu Matsushita; Gen Inoue; Nozomu Nishi; Ryo Masuda; Nana Hamamoto; Takaki Koide; Shintaro Shoji; Masashi Takaso
Journal:  Biomed Res Int       Date:  2018-03-25       Impact factor: 3.411

  3 in total

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