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Ceramide Domains in Health and Disease: A Biophysical Perspective

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Book cover Bioactive Ceramides in Health and Disease

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 1159))

Abstract

Ceramides are the central molecules in sphingolipid metabolism. In addition, they are recognized as important modulators of cell function, playing key roles in several cellular processes that range from cell proliferation to cell death. Moreover, ceramides were implicated in multiple diseases, including cancer, neurodegenerative and metabolic diseases, and also in infection by different pathogens. The mechanisms underlying the diverse biological and pathological actions of ceramides are yet to be fully elucidated. Several lines of evidence suggest that the structural features of ceramides, namely their high hydrophobicity and ability to establish strong H-bond network, are responsible for changes in the biophysical properties of biological membranes that can affect the activity of proteins and activate signaling pathways. Ceramide-induced alterations in membrane biophysical properties might also influence the internalization, trafficking and sorting of lipids, proteins, drugs and even pathogens contributing to cell pathophysiology. In this chapter, we critically discuss the ability of ceramides to form lipid domains with atypical biophysical properties and how these domains can be involved in those processes.

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Abbreviations

ACDase:

Acid Ceramidase

AFM:

Atomic Force Microscopy

ASAH1:

N-Acylsphingosine Amidohydrolase 1

aSMase:

Acid Sphingomyelinase

C1P:

Ceramide 1-Phosphate

C1PP:

Phosphatase C1P

CAPK:

Ceramide-activated Protein Kinase

CAPP:

Ceramide-activated Protein Phosphatase

CD95:

Cluster of Differentiation 95

CDase:

Ceramidase

Cer:

Ceramide

CerS:

Ceramide Synthase

CERT:

Ceramide Transfer Protein

Chol:

Cholesterol

CerK:

Ceramide Kinase

CPTP:

C1P-specific Transfer Protein

DEPE:

1,2-Dielaidoyl-sn-glycero-3-phosphoethanolamine

DES:

Dihydroceramide Desaturase

dhCer:

Dihydroceramide

DISC:

Death-inducing Signaling Complex

DMPC:

1,2-dimyristoyl-sn-glycero-3-phosphocholine

DOPC:

1,2-dioleyol-sn-glycero-3-phosphocholine

DPPC:

1,2-dipalmitoyl-sn-glycero-3-phosphocholine

DSC:

Differential Scanning Calorimetry

ER:

Endoplasmic Reticulum

FAPP2:

Phosphatidylinositol-4-phosphate Adaptor Protein 2

FCS:

Fluorescence Correlation Spectroscopy

FD:

Farber Disease

FTIR:

Fourier-Transform Infrared Spectroscopy

GCS:

Glucosylceramide Synthase

GlcCer:

Glucosylceramide

GSLs:

Glycosphingolipids

H-bonds:

Hydrogen Bonds

HIV:

Human Immunodeficiency Virus

hTERT:

human Telomerase Reverse Transcriptase

KDS:

3-ketosphinganine reductase

lo:

Liquid Ordered

LSD:

Lysosomal Storage Disease

MAMs:

Mitochondria Associated Endoplasmic Reticulum Membranes

MAPK:

Mitogen-activated Protein Kinase

MD:

Molecular Dynamic

NMR:

Nuclear Magnetic Resonance

nSMase:

Neutral Sphingomyelinase

PC:

Phosphatidylcholine

PD:

Parkinson’s disease

PKCζ:

Protein Kinase Cζ

PM:

Plasma Membrane

POPC:

1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine

POPE:

1-palmitoyl-2-oleoyl phosphatidylcholine

ROS:

Reactive Oxygen Species

S1P:

Sphingosine 1-Phosphate

SK:

Sphingosine Kinase

SL:

Sphingolipid

SM:

Sphingomyelin

SMase:

Sphingomyelinase

SMS:

Sphingomyelin Synthase

Sph:

Sphingosine

SPL:

S1P lyase

SPT:

serine palmitoyltransferase

TEM:

Transmission Electron Microscopy

Tm :

Melting Temperature

TRAIL:

TNF-Related Apoptosis Inducing Ligand

UV:

Ultraviolet Radiation

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Acknowledgments

The authors acknowledge funding from Fundação para a Ciência e Tecnologia (FCT), Portugal, grant references PTDC/BBB-BQB/3710/2014, PTDC/BIA-BFS/29448/2017, SFRH/BD/104205/2014 to A.E. Ventura, and Investigador FCT to L.C. Silva (IF/00437/2014).

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Correspondence to Liana C. Silva .

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Ventura, A.E., Mestre, B., Silva, L.C. (2019). Ceramide Domains in Health and Disease: A Biophysical Perspective. In: Stiban, J. (eds) Bioactive Ceramides in Health and Disease. Advances in Experimental Medicine and Biology, vol 1159. Springer, Cham. https://doi.org/10.1007/978-3-030-21162-2_6

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