Cargando…

Ceramide activation of RhoA/Rho kinase impairs actin polymerization during aggregated LDL catabolism

Macrophages use an extracellular, hydrolytic compartment formed by local actin polymerization to digest aggregated LDL (agLDL). Catabolism of agLDL promotes foam cell formation and creates an environment rich in LDL catabolites, including cholesterol and ceramide. Increased ceramide levels are prese...

Descripción completa

Detalles Bibliográficos
Autores principales: Singh, Rajesh K., Haka, Abigail S., Brumfield, Alexandria, Grosheva, Inna, Bhardwaj, Priya, Chin, Harvey F., Xiong, Yuquan, Hla, Timothy, Maxfield, Frederick R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Biochemistry and Molecular Biology 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5625121/
https://www.ncbi.nlm.nih.gov/pubmed/28814641
http://dx.doi.org/10.1194/jlr.M076398
_version_ 1783268342624157696
author Singh, Rajesh K.
Haka, Abigail S.
Brumfield, Alexandria
Grosheva, Inna
Bhardwaj, Priya
Chin, Harvey F.
Xiong, Yuquan
Hla, Timothy
Maxfield, Frederick R.
author_facet Singh, Rajesh K.
Haka, Abigail S.
Brumfield, Alexandria
Grosheva, Inna
Bhardwaj, Priya
Chin, Harvey F.
Xiong, Yuquan
Hla, Timothy
Maxfield, Frederick R.
author_sort Singh, Rajesh K.
collection PubMed
description Macrophages use an extracellular, hydrolytic compartment formed by local actin polymerization to digest aggregated LDL (agLDL). Catabolism of agLDL promotes foam cell formation and creates an environment rich in LDL catabolites, including cholesterol and ceramide. Increased ceramide levels are present in lesional LDL, but the effect of ceramide on macrophage proatherogenic processes remains unknown. Here, we show that macrophages accumulate ceramide in atherosclerotic lesions. Using macrophages from sphingosine kinase 2 KO (SK2KO) mice to mimic ceramide-rich conditions of atherosclerotic lesions, we show that SK2KO macrophages display impaired actin polymerization and foam cell formation in response to contact with agLDL. C16-ceramide treatment impaired wild-type but not SK2KO macrophage actin polymerization, confirming that this effect is due to increased ceramide levels. We demonstrate that knockdown of RhoA or inhibition of Rho kinase restores agLDL-induced actin polymerization in SK2KO macrophages. Activation of RhoA in macrophages was sufficient to impair actin polymerization and foam cell formation in response to agLDL. Finally, we establish that during catabolism, macrophages take up ceramide from agLDL, and inhibition of ceramide generation modulates actin polymerization. These findings highlight a critical regulatory pathway by which ceramide impairs actin polymerization through increased RhoA/Rho kinase signaling and regulates foam cell formation.
format Online
Article
Text
id pubmed-5625121
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher The American Society for Biochemistry and Molecular Biology
record_format MEDLINE/PubMed
spelling pubmed-56251212017-10-04 Ceramide activation of RhoA/Rho kinase impairs actin polymerization during aggregated LDL catabolism Singh, Rajesh K. Haka, Abigail S. Brumfield, Alexandria Grosheva, Inna Bhardwaj, Priya Chin, Harvey F. Xiong, Yuquan Hla, Timothy Maxfield, Frederick R. J Lipid Res Research Articles Macrophages use an extracellular, hydrolytic compartment formed by local actin polymerization to digest aggregated LDL (agLDL). Catabolism of agLDL promotes foam cell formation and creates an environment rich in LDL catabolites, including cholesterol and ceramide. Increased ceramide levels are present in lesional LDL, but the effect of ceramide on macrophage proatherogenic processes remains unknown. Here, we show that macrophages accumulate ceramide in atherosclerotic lesions. Using macrophages from sphingosine kinase 2 KO (SK2KO) mice to mimic ceramide-rich conditions of atherosclerotic lesions, we show that SK2KO macrophages display impaired actin polymerization and foam cell formation in response to contact with agLDL. C16-ceramide treatment impaired wild-type but not SK2KO macrophage actin polymerization, confirming that this effect is due to increased ceramide levels. We demonstrate that knockdown of RhoA or inhibition of Rho kinase restores agLDL-induced actin polymerization in SK2KO macrophages. Activation of RhoA in macrophages was sufficient to impair actin polymerization and foam cell formation in response to agLDL. Finally, we establish that during catabolism, macrophages take up ceramide from agLDL, and inhibition of ceramide generation modulates actin polymerization. These findings highlight a critical regulatory pathway by which ceramide impairs actin polymerization through increased RhoA/Rho kinase signaling and regulates foam cell formation. The American Society for Biochemistry and Molecular Biology 2017-10 2017-08-16 /pmc/articles/PMC5625121/ /pubmed/28814641 http://dx.doi.org/10.1194/jlr.M076398 Text en Copyright © 2017 by the American Society for Biochemistry and Molecular Biology, Inc. http://creativecommons.org/licenses/by/4.0/ Author’s Choice—Final version free via Creative Commons CC-BY license.
spellingShingle Research Articles
Singh, Rajesh K.
Haka, Abigail S.
Brumfield, Alexandria
Grosheva, Inna
Bhardwaj, Priya
Chin, Harvey F.
Xiong, Yuquan
Hla, Timothy
Maxfield, Frederick R.
Ceramide activation of RhoA/Rho kinase impairs actin polymerization during aggregated LDL catabolism
title Ceramide activation of RhoA/Rho kinase impairs actin polymerization during aggregated LDL catabolism
title_full Ceramide activation of RhoA/Rho kinase impairs actin polymerization during aggregated LDL catabolism
title_fullStr Ceramide activation of RhoA/Rho kinase impairs actin polymerization during aggregated LDL catabolism
title_full_unstemmed Ceramide activation of RhoA/Rho kinase impairs actin polymerization during aggregated LDL catabolism
title_short Ceramide activation of RhoA/Rho kinase impairs actin polymerization during aggregated LDL catabolism
title_sort ceramide activation of rhoa/rho kinase impairs actin polymerization during aggregated ldl catabolism
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5625121/
https://www.ncbi.nlm.nih.gov/pubmed/28814641
http://dx.doi.org/10.1194/jlr.M076398
work_keys_str_mv AT singhrajeshk ceramideactivationofrhoarhokinaseimpairsactinpolymerizationduringaggregatedldlcatabolism
AT hakaabigails ceramideactivationofrhoarhokinaseimpairsactinpolymerizationduringaggregatedldlcatabolism
AT brumfieldalexandria ceramideactivationofrhoarhokinaseimpairsactinpolymerizationduringaggregatedldlcatabolism
AT groshevainna ceramideactivationofrhoarhokinaseimpairsactinpolymerizationduringaggregatedldlcatabolism
AT bhardwajpriya ceramideactivationofrhoarhokinaseimpairsactinpolymerizationduringaggregatedldlcatabolism
AT chinharveyf ceramideactivationofrhoarhokinaseimpairsactinpolymerizationduringaggregatedldlcatabolism
AT xiongyuquan ceramideactivationofrhoarhokinaseimpairsactinpolymerizationduringaggregatedldlcatabolism
AT hlatimothy ceramideactivationofrhoarhokinaseimpairsactinpolymerizationduringaggregatedldlcatabolism
AT maxfieldfrederickr ceramideactivationofrhoarhokinaseimpairsactinpolymerizationduringaggregatedldlcatabolism