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Cellular and Molecular Biology Letters

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1689-1392
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Volume 20, Issue 5

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MGL induces nuclear translocation of EndoG and AIF in caspase-independent T cell death

Qingpan Bu
  • School of Life Sciences, Northeast Normal University, #5268, Renmin Street, Changchun, Jilin 130024, P.R. China
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/ Jianhui Wang
  • School of Life Sciences, Northeast Normal University, #5268, Renmin Street, Changchun, Jilin 130024, P.R. China
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  • De Gruyter OnlineGoogle Scholar
/ Yi Zheng
  • School of Life Sciences, Northeast Normal University, #5268, Renmin Street, Changchun, Jilin 130024, P.R. China
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/ Yingying Zou
  • School of Life Sciences, Northeast Normal University, #5268, Renmin Street, Changchun, Jilin 130024, P.R. China
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/ Min Wei
  • Corresponding author
  • School of Life Sciences, Northeast Normal University, #5268, Renmin Street, Changchun, Jilin 130024, P.R. China
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Published Online: 2016-03-05 | DOI: https://doi.org/10.1515/cmble-2015-0051

Abstract

Macrophage galactose-type lectin (MGL) participates in the regulation of T cell apoptosis, but the exact death pathway remains unclear. Here, we demonstrated that MGL-induced T cell death occurs in a caspaseindependent manner. Furthermore, MGL treatment triggers the translocation of endonuclease G (EndoG) and apoptosis-inducing factor (AIF) from the mitochondria to the nucleus. Because galectin-1 (Gal-1) can also initiate similar mitochondrial events, we speculate that this death pathway may be widely used by the lectin family.

Keywords: MGL; Gal-1; Lectin; T cell apoptosis; Caspase; EndoG; AIF

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About the article

Received: 2015-08-16

Accepted: 2015-10-21

Published Online: 2016-03-05

Published in Print: 2015-12-01


Citation Information: Cellular and Molecular Biology Letters, Volume 20, Issue 5, Pages 816–824, ISSN (Online) 1689-1392, DOI: https://doi.org/10.1515/cmble-2015-0051.

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