Tryptophan to Arginine Substitution in Puroindoline-b Alters Binding to Model Eukaryotic Membrane

Langmuir (2017)

Michael Sanders Luke A. Clifton Richard A. Frazier Rebecca Green

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Abstract:

We have studied how puroindoline-b (PINB) mutants bind to model eukaryotic membranes dependent on binary composition of anionic:zwitterionic phospholipids and the presence of cholesterol and sphingomyelin in the model membrane. We have found that the trends in lipid binding behavior are different for wild-type PINB compared to its naturally occurring PINB(Trp44Arg) mutant form and have seen evidence of protein-induced domain formation within the lipid layer structure. Results show that selective binding of antimicrobial peptides to different membrane types is as a result of differences in lipid composition and the arrangement of lipids within the membrane surface. However, membrane-binding behavior is not easily predicted; it is determined by net charge, hydrophobicity, and the amphiphilicity of the protein/peptide lipid-binding domain.

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Lipid Membrane Structure and Behavior

Antimicrobial Peptides and Activities

Sphingolipid Metabolism and Signaling

10.1021/acs.langmuir.6b03030

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Lysosomal involvement in cellular turnover of plasma membrane sphingomyelin

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism (1984)

Sarah L. Sutrina Winston W. Chen

Acid sphingomyelinase

Niemann–Pick disease

Sphingomyelin phosphodiesterase

10.1016/0005-2760(84)90318-7

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Citations (23)

Metabolism of 3-[3H]sphingosine sphingomyelin labeled with [14C]palmitic or [14C]linoleic acid by Hep G2 cells and rat liver in vivo

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism (1991)

Y. Stein K. Oette Y. Dabach G. Hollander M. Ben-Naim

Sphingolipid

10.1016/0005-2760(91)90059-q

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Citations (5)

Nuclear Membrane Sphingomyelin–Cholesterol Changes in Rat Liver after Hepatectomy

Biochemical and Biophysical Research Communications (1999)

Elisabetta Albi Isabella Peloso Mariapia Viola Magni

Sphingomyelin phosphodiesterase

Sphingolipid

Acid sphingomyelinase

10.1006/bbrc.1999.1188

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Citations (31)

Divergent fate of unsaturated and saturated ceramides and sphingomyelins in rat liver and cells in culture

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism (1989)

Oliver Stein K. Oette G. Hollander Y. Dabach M. Ben-Naim

Sphingolipid

Phosphatidylethanolamine

10.1016/0005-2760(89)90252-x

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Citations (13)

Content and structure of ceramide and sphingomyelin and sphingomyelinase activity in mouse hepatoma-22.

PubMed (1999)

Rylova Sn Somova Og Zubova Es Dudnik Lb Kogtev Ls

Sphingolipid

Sphingomyelin phosphodiesterase

Catabolism

Source

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Citations (8)

Lysenin: A sphingomyelin specific pore-forming toxin

Biochimica et Biophysica Acta (BBA) - General Subjects (2007)

Hidehiko Shogomori Toshihide Kobayashi

Sphingolipid

Sphingomyelin phosphodiesterase

Second messenger system

Lipid raft

10.1016/j.bbagen.2007.09.001

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Citations (86)

Sphingomyelinase D, a novel probe for cellular sphingomyelin

Journal of Lipid Research (2003)

Papasani V. Subbaiah Stephen J. Billington B. Helen Jost J. Glenn Songer Yvonne Lange

Sphingomyelin (SM) and free cholesterol (FC) are concentrated in the plasma membranes of eukaryotes; however, the physiological significance of their association is unclear. A common tool for studying the role of membrane SM is digestion with bacterial sphingomyelinase (SMase) C, which hydrolyzes SM to ceramide. However, it is not known whether the observed effects of SMase C treatment are due to the loss of SM per se or to the signaling effects of ceramide. In this study, we tested SMase D from Corynebacterium pseudotuberculosis, which hydrolyzes SM to ceramide phosphate, as an alternative probe. This enzyme specifically hydrolyzed SM in fibroblasts without causing accumulation of ceramide. Treatment of fibroblasts with SMase D stimulated translocation of PM FC to intracellular sites by <20% of the rate observed after SMase C digestion. The cells regenerated SM nearly completely within 5 h after SMase C treatment. However, even after 20 h, no regeneration occurred following SMase D digestion. These findings suggest that the translocation of PM FC caused by SMase C digestion is due to the cellular effects of ceramide rather than the loss of SM. Since ceramide phosphate does not appear to have such effects, we suggest that SMase D is a useful probe of membrane SM.

Sphingomyelin phosphodiesterase

Sphingolipid

10.1194/jlr.m300103-jlr200

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Citations (26)

An Enzymatic Assay for Quantifying Sphingomyelin in Tissues and Plasma from Humans and Mice with Niemann–Pick Disease

Analytical Biochemistry (2001)

Xingxuan He Fei Chen Shimon Gátt Edward H. Schuchman

Sphingomyelin phosphodiesterase

Niemann–Pick disease

Phosphorylcholine

Sphingolipid