Proteolipid protein and DM-20 are synthesized by Schwann cells, present in myelin membrane, but they are not fatty acylated

1991 ◽  
Vol 16 (8) ◽  
pp. 855-858 ◽  
Author(s):  
Harish C. Agrawal ◽  
Daya Agrawal
Keyword(s):  
Schwann Cells ◽  
Proteolipid Protein ◽  
Myelin Membrane

scholarly journals Murine Esophagus Expresses Glial-Derived Central Nervous System Antigens

2021 ◽  
Vol 22 (6) ◽  
pp. 3233
Author(s):  
Christopher Kapitza ◽  
Rittika Chunder ◽  
Anja Scheller ◽  
Katherine S. Given ◽  
Wendy B. Macklin ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Schwann Cells ◽  
Glial Cells ◽  
Proteolipid Protein ◽  
Pcr Analysis ◽  
Specific Expression ◽  
Enteric Glial Cells ◽  
Cell Type Specific Expression ◽  
Long Time

Multiple sclerosis (MS) has been considered to specifically affect the central nervous system (CNS) for a long time. As autonomic dysfunction including dysphagia can occur as accompanying phenomena in patients, the enteric nervous system has been attracting increasing attention over the past years. The aim of this study was to identify glial and myelin markers as potential target structures for autoimmune processes in the esophagus. RT-PCR analysis revealed glial fibrillary acidic protein (GFAP), proteolipid protein (PLP), and myelin basic protein (MBP) expression, but an absence of myelin oligodendrocyte glycoprotein (MOG) in the murine esophagus. Selected immunohistochemistry for GFAP, PLP, and MBP including transgenic mice with cell-type specific expression of PLP and GFAP supported these results by detection of (1) GFAP, PLP, and MBP in Schwann cells in skeletal muscle and esophagus; (2) GFAP, PLP, but no MBP in perisynaptic Schwann cells of skeletal and esophageal motor endplates; (3) GFAP and PLP, but no MBP in glial cells surrounding esophageal myenteric neurons; and (4) PLP, but no GFAP and MBP in enteric glial cells forming a network in the esophagus. Our results pave the way for further investigations regarding the involvement of esophageal glial cells in the pathogenesis of dysphagia in MS.

Thyroid hormone affects Schwann cell and oligodendrocyte gene expression at the glial transition zone of the VIIIth nerve prior to cochlea function

Development ◽  
1998 ◽  
Vol 125 (18) ◽  
pp. 3709-3718 ◽  
Author(s):  
M. Knipper ◽  
C. Bandtlow ◽  
L. Gestwa ◽  
I. Kopschall ◽  
K. Rohbock ◽  
...  
Keyword(s):  
Gene Expression ◽  
Thyroid Hormone ◽  
Schwann Cells ◽  
Nerve Conduction ◽  
Time Course ◽  
Hormone Receptors ◽  
Marker Gene ◽  
Cranial Nerves ◽  
Proteolipid Protein ◽  
Viiith Nerve

All cranial nerves, as well as the VIIIth nerve which invades the cochlea, have a proximal end in which myelin is formed by Schwann cells and a distal end which is surrounded by oligodendrocytes. The question which arises in this context is whether peripheral and central parts of these nerves myelinate simultaneously or subsequently and whether the myelination of either of the parts occurs simultaneously at the onset of the cochlea function and under the control of neuronal activity. In the present paper, we examined the relative time course of the myelinogenesis of the distal part of the VIIIth nerve by analyzing the expression of peripheral protein P0, proteolipid protein and myelin basic protein. To our surprise, we observed that the expression of myelin markers in the peripheral and central part of the intradural part of the VIIIth nerve started simultaneously, from postnatal day 2 onwards, long before the onset of cochlea function. The expression rapidly achieved saturation levels on the approach to postnatal day 12, the day on which the cochlea function commenced. Because of its importance for the neuronal and morphological maturation of the cochlea during this time, an additional role of thyroid hormone in cochlear myelinogenesis was considered. Indeed, it transpires that this hormone ensures the rapid accomplishment of glial gene expression, not only in the central but also in the peripheral part of the cochlea. Furthermore, an analysis of the thyroid hormone receptors, TRaplha and TRbeta, indicates that TRbeta is necessary for myelinogenesis of the VIIIth nerve. Rapid thyroid hormone-dependent saturation of myelin marker gene expression in Schwann cells and oligodendrocytes of the VIIIth nerve may guarantee nerve conduction and synchronized impulse transmission at the onset of hearing. The thyroid hormone-dependent commencement of nerve conduction is discussed in connection with the patterning refinement of central auditory pathways and the acquisition of deafness.

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.

Myelin-specific proteolipid protein is expressed in myelinating schwann cells but is not incorporated into myelin sheaths

1987 ◽  
Vol 18 (4) ◽  
pp. 511-518 ◽  
Author(s):  
C. Puckett ◽  
L. Hundson ◽  
K. Ono ◽  
V. Friedrich ◽  
J. Benecke ◽  
...  
Keyword(s):  
Schwann Cells ◽  
Proteolipid Protein ◽  
Myelin Sheaths

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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