Polyporus squamosus Lectin 1a (PSL1a) Exhibits Cytotoxicity in Mammalian Cells by Disruption of Focal Adhesions, Inhibition of Protein Synthesis and Induction of Apoptosis.

PSL1a is a lectin from the mushroom Polyporus squamosus that binds to sialylated glycans and glycoconjugates with high specificity and selectivity. In addition to its N-terminal carbohydrate-binding domain, PSL1a possesses a Ca2+-dependent proteolytic activity in the C-terminal domain. In the presen...

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Main Authors: Dipankar Manna, Sascha Pust, Maria L Torgersen, Gabriele Cordara, Markus Künzler, Ute Krengel, Kirsten Sandvig
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2017-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC5256987?pdf=render
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spelling doaj-648b20f6e8414a2bab10c01feb4112f52020-11-25T01:31:48ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01121e017071610.1371/journal.pone.0170716Polyporus squamosus Lectin 1a (PSL1a) Exhibits Cytotoxicity in Mammalian Cells by Disruption of Focal Adhesions, Inhibition of Protein Synthesis and Induction of Apoptosis.Dipankar MannaSascha PustMaria L TorgersenGabriele CordaraMarkus KünzlerUte KrengelKirsten SandvigPSL1a is a lectin from the mushroom Polyporus squamosus that binds to sialylated glycans and glycoconjugates with high specificity and selectivity. In addition to its N-terminal carbohydrate-binding domain, PSL1a possesses a Ca2+-dependent proteolytic activity in the C-terminal domain. In the present study, we demonstrate that PSL1a has cytotoxic effects on mammalian cancer cells, and we show that the cytotoxicity is dependent on the cysteine protease activity. PSL1a treatment leads to cell rounding and detachment from the substratum, concomitant with disruption of vinculin complexes in focal adhesions. We also demonstrate that PSL1a inhibits protein synthesis and induces apoptosis in HeLa cells, in a time- and concentration-dependent manner.http://europepmc.org/articles/PMC5256987?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Dipankar Manna
Sascha Pust
Maria L Torgersen
Gabriele Cordara
Markus Künzler
Ute Krengel
Kirsten Sandvig
spellingShingle Dipankar Manna
Sascha Pust
Maria L Torgersen
Gabriele Cordara
Markus Künzler
Ute Krengel
Kirsten Sandvig
Polyporus squamosus Lectin 1a (PSL1a) Exhibits Cytotoxicity in Mammalian Cells by Disruption of Focal Adhesions, Inhibition of Protein Synthesis and Induction of Apoptosis.
PLoS ONE
author_facet Dipankar Manna
Sascha Pust
Maria L Torgersen
Gabriele Cordara
Markus Künzler
Ute Krengel
Kirsten Sandvig
author_sort Dipankar Manna
title Polyporus squamosus Lectin 1a (PSL1a) Exhibits Cytotoxicity in Mammalian Cells by Disruption of Focal Adhesions, Inhibition of Protein Synthesis and Induction of Apoptosis.
title_short Polyporus squamosus Lectin 1a (PSL1a) Exhibits Cytotoxicity in Mammalian Cells by Disruption of Focal Adhesions, Inhibition of Protein Synthesis and Induction of Apoptosis.
title_full Polyporus squamosus Lectin 1a (PSL1a) Exhibits Cytotoxicity in Mammalian Cells by Disruption of Focal Adhesions, Inhibition of Protein Synthesis and Induction of Apoptosis.
title_fullStr Polyporus squamosus Lectin 1a (PSL1a) Exhibits Cytotoxicity in Mammalian Cells by Disruption of Focal Adhesions, Inhibition of Protein Synthesis and Induction of Apoptosis.
title_full_unstemmed Polyporus squamosus Lectin 1a (PSL1a) Exhibits Cytotoxicity in Mammalian Cells by Disruption of Focal Adhesions, Inhibition of Protein Synthesis and Induction of Apoptosis.
title_sort polyporus squamosus lectin 1a (psl1a) exhibits cytotoxicity in mammalian cells by disruption of focal adhesions, inhibition of protein synthesis and induction of apoptosis.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2017-01-01
description PSL1a is a lectin from the mushroom Polyporus squamosus that binds to sialylated glycans and glycoconjugates with high specificity and selectivity. In addition to its N-terminal carbohydrate-binding domain, PSL1a possesses a Ca2+-dependent proteolytic activity in the C-terminal domain. In the present study, we demonstrate that PSL1a has cytotoxic effects on mammalian cancer cells, and we show that the cytotoxicity is dependent on the cysteine protease activity. PSL1a treatment leads to cell rounding and detachment from the substratum, concomitant with disruption of vinculin complexes in focal adhesions. We also demonstrate that PSL1a inhibits protein synthesis and induces apoptosis in HeLa cells, in a time- and concentration-dependent manner.
url http://europepmc.org/articles/PMC5256987?pdf=render
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