Conformational Changes and Association of Membrane-Interacting Peptides in Myelin Membrane Models: A Case of the C-Terminal Peptide of Proteolipid Protein and the Antimicrobial Peptide Melittin

2015 ◽  
Vol 119 (47) ◽  
pp. 14821-14830 ◽  
Author(s):  
Ashtina Appadu ◽  
Masoud Jelokhani-Niaraki ◽  
Lillian DeBruin
Keyword(s):  
Antimicrobial Peptide ◽  
Conformational Changes ◽  
Proteolipid Protein ◽  
Myelin Membrane ◽  
Membrane Models

scholarly journals Photo-initiated rupture of azobenzene micelles to enable the spectroscopic analysis of antimicrobial peptide dynamics

RSC Advances ◽  
2020 ◽  
Vol 10 (36) ◽  
pp. 21464-21472
Author(s):  
Matthew G. Roberson ◽  
Julia M. Duncan ◽  
Keveen J. Flieth ◽  
Laina M. Geary ◽  
Matthew J. Tucker
Keyword(s):  
Antimicrobial Peptide ◽  
Conformational Changes ◽  
Spectroscopic Analysis ◽  
Peptide Dynamics

Membrane mediated peptide conformational changes via photo-induced micelle disruption.

Effect of proteolipid protein on central nervous system myelin membrane fluidity

1985 ◽  
Vol 59 (2) ◽  
pp. 149-154 ◽  
Author(s):  
Frank R. Brown ◽  
Jeanne C. Beck ◽  
Jennifer R. Niebyl ◽  
Inderjit Singh
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Membrane Fluidity ◽  
Proteolipid Protein ◽  
Myelin Membrane

scholarly journals The Major Myelin-Resident Protein PLP Is Transported to Myelin Membranes via a Transcytotic Mechanism: Involvement of Sulfatide

2014 ◽  
Vol 35 (1) ◽  
pp. 288-302 ◽  
Author(s):  
Wia Baron ◽  
Hande Ozgen ◽  
Bert Klunder ◽  
Jenny C. de Jonge ◽  
Anita Nomden ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Body ◽  
Proteolipid Protein ◽  
Membrane Microdomains ◽  
Apical Surface ◽  
Membrane Domains ◽  
Myelin Membrane ◽  
Conformational Alteration ◽  
Syntaxin 3 ◽  
Triton X

Myelin membranes are sheet-like extensions of oligodendrocytes that can be considered membrane domains distinct from the cell's plasma membrane. Consistent with the polarized nature of oligodendrocytes, we demonstrate that transcytotic transport of the major myelin-resident protein proteolipid protein (PLP) is a key element in the mechanism of myelin assembly. Upon biosynthesis, PLP traffics to myelin membranes via syntaxin 3-mediated docking at the apical-surface-like cell body plasma membrane, which is followed by subsequent internalization and transport to the basolateral-surface-like myelin sheet. Pulse-chase experiments, in conjunction with surface biotinylation and organelle fractionation, reveal that following biosynthesis, PLP is transported to the cell body surface in Triton X-100 (TX-100)-resistant microdomains. At the plasma membrane, PLP transiently resides within these microdomains and its lateral dissipation is followed by segregation into 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS)-resistant domains, internalization, and subsequent transport toward the myelin membrane. Sulfatide triggers PLP's reallocation from TX-100- into CHAPS-resistant membrane domains, while inhibition of sulfatide biosynthesis inhibits transcytotic PLP transport. Taking these findings together, we propose a model in which PLP transport to the myelin membrane proceeds via a transcytotic mechanism mediated by sulfatide and characterized by a conformational alteration and dynamic, i.e., transient, partitioning of PLP into distinct membrane microdomains involved in biosynthetic and transcytotic transport.

scholarly journals Neuron to glia signaling triggers myelin membrane exocytosis from endosomal storage sites

2006 ◽  
Vol 172 (6) ◽  
pp. 937-948 ◽  
Author(s):  
Katarina Trajkovic ◽  
Ajit Singh Dhaunchak ◽  
José T. Goncalves ◽  
Dirk Wenzel ◽  
Anja Schneider ◽  
...  
Keyword(s):  
Membrane Trafficking ◽  
Proteolipid Protein ◽  
Myelin Membrane ◽  
Vertebrate Brain ◽  
Late Endosomes ◽  
Membrane Growth ◽  
Neuronal Signal ◽  
Endocytosis Pathway ◽  
Guanosine Triphosphatase

During vertebrate brain development, axons are enwrapped by myelin, an insulating membrane produced by oligodendrocytes. Neuron-derived signaling molecules are temporally and spatially required to coordinate oligodendrocyte differentiation. In this study, we show that neurons regulate myelin membrane trafficking in oligodendrocytes. In the absence of neurons, the major myelin membrane protein, the proteolipid protein (PLP), is internalized and stored in late endosomes/lysosomes (LEs/Ls) by a cholesterol-dependent and clathrin-independent endocytosis pathway that requires actin and the RhoA guanosine triphosphatase. Upon maturation, the rate of endocytosis is reduced, and a cAMP-dependent neuronal signal triggers the transport of PLP from LEs/Ls to the plasma membrane. These findings reveal a fundamental and novel role of LEs/Ls in oligodendrocytes: to store and release PLP in a regulated fashion. The release of myelin membrane from LEs/Ls by neuronal signals may represent a mechanism to control myelin membrane growth.

scholarly journals Effects of Detergent on α-Synuclein Structure: A Native MS-Ion Mobility Study

2020 ◽  
Vol 21 (21) ◽  
pp. 7884
Author(s):  
Rani Moons ◽  
Renate van der Wekken-de Bruijne ◽  
Stuart Maudsley ◽  
Filip Lemière ◽  
Anne-Marie Lambeir ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Ion Mobility ◽  
Intrinsically Disordered Protein ◽  
Detergent Concentration ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Native Ms ◽  
Different Types ◽  
Membrane Models ◽  
Mobility Study

The intrinsically disordered protein α-synuclein plays a major role in Parkinson’s disease. The protein can oligomerize resulting in the formation of various aggregated species in neuronal cells, leading to neurodegeneration. The interaction of α-synuclein with biological cell membranes plays an important role for specific functions of α-synuclein monomers, e.g., in neurotransmitter release. Using different types of detergents to mimic lipid molecules present in biological membranes, including the presence of Ca2+ ions as an important structural factor, we aimed to gain an understanding of how α-synuclein interacts with membrane models and how this affects the protein conformation and potential oligomerization. We investigated detergent binding stoichiometry, affinity and conformational changes of α-synuclein taking detergent concentration, different detergent structures and charges into account. With native nano-electrospray ionization ion mobility-mass spectrometry, we were able to detect unique conformational patterns resulting from binding of specific detergents to α-synuclein. Our data demonstrate that α-synuclein monomers can interact with detergent molecules irrespective of their charge, that protein-micelle interactions occur and that micelle properties are an important factor.

Inhibition of the synthesis of glycosphingolipids affects the translocation of proteolipid protein to the myelin membrane

1989 ◽  
Vol 22 (3) ◽  
pp. 289-296 ◽  
Author(s):  
J. M. Pasquini ◽  
M. M. Guarna ◽  
M. A. Besio-Moreno ◽  
M. T. Iturregui ◽  
P. I. Oteiza ◽  
...  
Keyword(s):  
Proteolipid Protein ◽  
Myelin Membrane

An animal model for late onset chronic demyelination disease caused by failed terminal differentiation of oligodendrocytes

2005 ◽  
Vol 2 (2) ◽  
pp. 81-91 ◽  
Author(s):  
JIANMEI MA ◽  
MICHIO MATSUMOTO ◽  
KENJI F. TANAKA ◽  
HIROHIDE TAKEBAYASHI ◽  
KAZUHIRO IKENAKA
Keyword(s):  
Late Stage ◽  
Protein Gene ◽  
Late Onset ◽  
Proteolipid Protein ◽  
Transgenic Animals ◽  
Wild Type ◽  
Myelin Membrane ◽  
Demyelinating Disorder ◽  
Demyelinating Lesions

Various animal models are available for studying human multiple sclerosis (MS). Most of them model the initial phase of MS, including the immune-triggered attack of the myelin membrane and/or oligodendrocytes and, occasionally, demonstrate the remission and relapsing phases. However, few mimic the late chronic demyelinating phase. Overexpression of the proteolipid protein gene (Plp) causes a unique demyelinating disorder in mice in which normal-appearing myelin forms early in life and chronic demyelination occurs later. We found that remyelination is severely affected in this late demyelinating phase, but is not caused by deprivation of oligodendrocyte progenitors expressing PDGF receptor alpha (PDGFRα) and Olig2, which are present at an even higher number in the demyelinated white matter of the mutants than in wild-type controls. Furthermore, mature oligodendrocytes containing PLP were observed, but failed to remyelinate. The ability of oligodendrocytes from older transgenic animals to produce a myelin membrane-like structure was not impaired when cultured in vitro, which indicates that the lack of remyelination is not simply caused by changes in the intrinsic properties of the oligodendrocytes. Glial activation also occurred much earlier than active demyelination in mutant mice. Thus, in addition to intrinsic mechanisms, extrinsic mechanisms might also have an important role in defects of remyelination. These features are also observed in patients at a late stage of MS, leading to chronic demyelinating lesions. Thus, this mouse model partly mimics the late stage of MS and can be used to study the cause of inhibition of remyelination.

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