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At least 19 recordsLinked to original sources
PubMed2003

Neural CAMS and their role in the development and organization of myelin sheaths.

Myelination of axons is a prerequisite for the rapid propagation of nerve impulses, and thus for the proper functioning of the nervous system. Phenotypic analysis of genetically engineered mice has provided evidence that cell adhesion molecules are critically involved in the interaction of myelin-forming glial cells with axons, the formation of regularly spaced myelin internodes along axons and the organisation of paranodes and the myelin-free gaps separating the internodes, the nodes of Ranvier. This review will focus on three members of the immunoglobulin-superfamily, the myelin-associated glycoprotein (MAG), the neural cell adhesion molecule (NCAM) and the neural adhesion molecule L1 and will discuss studies on transgenic mice that have analyzed the role of these cell adhesion molecules in the initiation of myelination, formation of structurally intact myelin sheaths and/or maintenance of myelin and axon integrity.

Animals↗
PubMed2001

Chemical deacylation reduces the adhesive properties of proteolipid protein and leads to decompaction of the myelin sheath.

Myelin proteolipid protein (PLP) contains thioester-bound, long-chain fatty acids which are known to influence the structure of the molecule. To gain further insights into the role of this post-translational modification, we studied the effect that chemical deacylation of PLP had on the morphology of myelin and on the protein's ability to mediate the clustering of lipid vesicles. Incubation of rat optic nerves in isoosmotic solutions containing 100 mM hydroxylamine (HA) pH 7.4 led to deacylation of PLP and decompaction of myelin lamellae at the level of the intraperiod line. Incubation of nerves with milder nucleophilic agents (Tris and methylamine) or diluted HA, conditions that do not remove protein-bound fatty acids, caused no alterations in myelin structure. Other possible effects of HA which could have affected myelin compaction indirectly were ruled out. Incubation of optic nerves with 50 mM dithioerythritol (DTE) also led to the splitting of the myelin intraperiod line and this change again coincided with the removal of fatty acids. In addition, the apparently compacted CNS myelin in the PLP-less myelin-deficient rat, like that in tissue containing deacylated PLP, was readily decompacted upon incubation in isoosmotic buffers, suggesting that the function of PLP as a stabilizer of the interlamellar attachment is, at least in part, mediated by fatty acylation. Furthermore, in contrast to the native protein, PLP deacylated with either HA or DTE failed to induce the clustering of phosphatidylcholine/cholesterol vesicles in vitro. This phenomenon is not due to side-effects of the deacylation procedure since, upon partial repalmitoylation, the protein recovered most of its original vesicle-clustering activity. Collectively, these findings suggest that palmitoylation, by influencing the adhesive properties of PLP, is important for stabilizing the multilamellar structure of myelin.

Acylation↗
PubMed1974

Comparison of Weigert stained sections with unfixed, unstained sections for study of myelin sheaths.

Myelinated fibers can be demonstrated in thin unstained brain sections of freshly killed uninjected animals. With this method myelinated fibers stand out as clearly as in stained Weigert sections from formalin-fixed brains. Unstained unfixed sections can be viewed under ordinary light within minutes after death of the animal and immediately photographed for permanent records. Such sections have value for neuroanatomical studies, and for rapid localization of various types of experimental lesions.

Animals↗
PubMed1981

Fine structure of the central myelin sheath in the myelin deficient mutant Shiverer mouse, with special reference to the pattern of myelin formation by oligodendroglia.

The central myelin sheaths of the recessive autosomal mutant mouse, Shiverer, were investigated by electron microscopy with special reference to the pattern of myelin formation. The results obtained may be summarized as follows: (1) the major dense line of myelin lamellae generally failed to be formed, but the axons were enclosed by tri-lamellar structures of about 14 nm in width, which were composed of one central membrane formed by fusion of outer leaflets of adjacent cytoplasmic sheets of oligodendroglia, corresponding to the intraperiod line, and two outer membranes which were identical with inner leaflets of adjacent cytoplasmic sheets and became highly electron-dense. However, major dense lines were sporadically observed; (2) the myelin sheath was not generally formed by spiralling of one cytoplasmic process of the oligodendroglia, but by enclosing an axon with several stratified layers of cytoplasmic sheets, some of which were certainly formed by the splitting of one process; and (3) aberrant myelination frequently occurred around the soma of oligodendroglia, not related to any axons.

Animals↗
PubMed1998

Morphology of cryofixed myelin sheath.

The myelin sheath is formed by concentrically apposed membrane pairs and shows a regularly layered pattern of alternating light lines and dense lines. Observation of cryofixed myelin demonstrated that the structures represent aqueous spaces. All lamellae of the myelin sheath show globular aggregates of particles and these particles are corresponding with aggregates observed after detergent extraction of the myelin. Experimental fusion of myelin lamellae shows an intermixing of the globular particles or subunits. The interaction of these structural units in the bilayers may provide the stability of the myelin lamellae and their lamination.

Animals↗
PubMed2006

Structural properties of proteins specific to the myelin sheath.

The myelin sheath is an insulating membrane layer surrounding myelinated axons in vertebrates, which is formed when the plasma membrane of an oligodendrocyte or a Schwann cell wraps itself around the axon. A large fraction of the total protein in this membrane layer is comprised of only a small number of individual proteins, which have certain intriguing structural properties. The myelin proteins are implicated in a number of neurological diseases, including, for example, autoimmune diseases and peripheral neuropathies. In this review, the structural properties of a number of myelin-specific proteins are described.

2',3'-Cyclic Nucleotide 3'-Phosphodiesterase↗
PubMed1992

Nodes of Ranvier and myelin sheath dimensions along exceptionally thin myelinated vertebrate PNS axons.

The trigeminal alveolar branch in the lower jaw of the cichlid Tilapia mariae was examined by light and electron microscopy on single and serial sections, and by light microscopy on teased fibre preparations. The principal purpose was to find out if the exceptionally thin myelinated axons (d < 1 micron) present in this nerve possess true nodes of Ranvier, and to determine the dimensions of their myelin sheaths. This necessitated analysis of the whole size range of myelinated fibres, with respect to nodal and internodal morphology. The results show that the exceptionally thin myelinated fibres exhibit primitive nodal regions, with patches of axolemmal undercoating, and few Schwann cell processes in the node gap. This contrasts with the more complex nodal organization seen in larger trigeminal alveolar branch fibres. For the whole population of myelinated fibres the number of myelin lamellae increases rectilinearly with axon diameter, and sheath length increases with fibre diameter according to a logarithmic expression. The myelin sheaths of the exceptionally thin trigeminal alveolar branch fibres are composed of 10-20 lamellae, and extend 35-50 microns along the axon. These results show that the structural complexity of nodal regions in the trigeminal alveolar branch decreases with decreasing fibre size, that the exceptionally thin myelinated trigeminal alveolar branch fibres possess primitive nodes and that they have very short myelin sheaths. Our crude theoretical calculations suggest that these fibres might be capable of saltatory conduction.

Animals↗
PubMed2001

The current status of structural studies on proteins of the myelin sheath (Review).

Myelin, the multilayered membrane structure surrounding axons, provides a unique environment to its proteins, which are either transmembrane proteins or interacting intimately with the membrane surface. Although myelin-specific proteins have been studied for decades, remarkably little is known of their three-dimensional structures. In addition, the exact functions of myelin proteins are to a large extent unknown. In this report, our current knowledge of peripheral nervous system myelin protein structures is reviewed, and the current status of attempts to solve the structures of full-length myelin proteins is evaluated. Furthermore, molecular models for the extracellular domain of the myelin-associated glycoprotein and the putative kinase-like domain of 2',3'-cyclic nucleotide 3'-phosphodiesterase are presented and discussed.

2',3'-Cyclic-Nucleotide Phosphodiesterases↗
PubMed1975

Topographical arrangement of membrane proteins in the intact myelin sheath. Lactoperoxidase incorproation of iodine into myelin surface proteins.

The lactoperoxidase-catalyzed iodination technique was utilized to incorporate radioactive iodine into membrane proteins which lie on the outer surface of the myelin sheath. An intact, myelinated nerve bundle, the dorsal column of the cat spinal cord, was employed. The enzymatically iodinated proteins were identified by polyacrylamide gel electrophoresis, and the specific radioactivity was determined. Results indicated that several high molecular weight proteins were predominantly labeled by the nonpenetrating lactopreoxidase. Proteolipid protein was also labeled, although to a lesser extent; basic protein was not labeled under these conditions. The data suggest that several high molecular weight proteins are exposed on the outer surface of the myelin sheath. Proteolipid protein is at least partially exposed on the outer surface, although it could be present at both membrane surfaces. Evidence is presented which suggests that the basic protein is located at the inner surface of the membrane, corresponding to the major dense line of myelin.

Animals↗
PubMed1998

Functional gap junctions in the schwann cell myelin sheath.

The Schwann cell myelin sheath is a multilamellar structure with distinct structural domains in which different proteins are localized. Intracellular dye injection and video microscopy were used to show that functional gap junctions are present within the myelin sheath that allow small molecules to diffuse between the adaxonal and perinuclear Schwann cell cytoplasm. Gap junctions are localized to periodic interruptions in the compact myelin called Schmidt-Lanterman incisures and to paranodes; these regions contain at least one gap junction protein, connexin32 (Cx32). The radial diffusion of low molecular weight dyes across the myelin sheath was not interrupted in myelinating Schwann cells from cx32-null mice, indicating that other connexins participate in forming gap junctions in these cells. Owing to the unique geometry of myelinating Schwann cells, a gap junction-mediated radial pathway may be essential for rapid diffusion between the adaxonal and perinuclear cytoplasm, since this radial pathway is approximately one million times faster than the circumferential pathway.

Animals↗
PubMed1991

Myelin sheath survival following axonal degeneration in doubly myelinated nerve fibers.

Axonal contact plays a critical role in initiating myelin formation by Schwann cells. However, recent studies of "double myelination" have indicated that myelin maintenance continues in Schwann cells completely displaced from physical contact with the axon. This raises the possibility either that diffusible trophic factors are produced by the axon, or that the axon is not required for myelin maintenance by these displaced Schwann cells. To test these hypotheses, the axons involved in double myelination in the mouse superior cervical ganglion (SCG) were transected surgically by a transganglionic lesion. The inferior pole of the SCG was resected to limit axonal regeneration. This method produced a typical Wallerian pattern of degeneration in the superior pole, without compromising the blood supply or introducing nonspecific trauma. EM analysis at 1 and 5 d postoperatively showed that initially the axon degenerated, followed by breakdown of the inner myelin sheath. In those configurations where the outer Schwann cell was only partly displaced from the axon, the outer myelin sheath degenerated simultaneously. However, in completely displaced internodes the outer sheath survived degeneration of the axon and inner sheath. Outer internodes remained intact for at least 5 weeks after transection (the longest time point in this study), at which time they enclosed reorganized processes of the inner Schwann cells, their basal lamina, and numerous collagen fibrils. Axonal regeneration within surviving outer internodes was rare and was characterized by the development of typical Remak ensheathment by the inner Schwann cells. We conclude that in the mouse SCG, myelin maintenance does not depend on the continued presence of the axon. These data suggest further that myelin breakdown in Wallerian degeneration may be initiated by mechanisms other than absence of a viable axon.

Animals↗
PubMed2001

Schwann cells and oligodendrocytes read distinct signals in establishing myelin sheath thickness.

Schwann cells and oligodendrocytes produce myelin sheaths of widely varying sizes. How these cells determine the size of myelin sheath for a particular axon is incompletely understood. Axonal diameter has long been suspected to be a signal in this process. We have analyzed myelin sheath thickness in L5 lumbar root and spinal cord white matter of a series of mouse mutants with diminished axonal calibers resulting from a deficiency of neurofilaments (NFs). In the PNS, average axonal diameters were reduced by 20-37% in the NF mutants. Remarkably, the average myelin sheath thickness remained unchanged from control values, and regression analysis showed sheaths abnormally thick for a given size of axon. These data show that a genetically induced reduction in axonal caliber does not cause a reduction in myelin sheath thickness in PNS and indicate that Schwann cells read some intrinsic signal on axons that can be uncoupled from axonal diameter. Interestingly, myelin sheaths in the spinal cord of these animals were not abnormally thick, arguing that axonal diameter may contribute directly to the regulation of myelination in the CNS and that oligodendrocytes and Schwann cells use different cues to set myelin sheath thickness.

Animals↗
PubMed1976

[The Schmidt-Lantermann incisures of the myelin sheath of Mauthner axons: site of longitudinal myelin growth].

The myelin sheath of the Mauthner axons in the spinal cord of young and adult fish belonging to the family Cyprinidae was examined by phase and electron microscopy. The sheath thickened considerably with age, the number of lamellae increasing from 200-230 in young fish (length 2--4 cm) to 250-300 in adult animals (length 20-25 cm). During this growth, the myelin sheath remained fairly compact and of optimal thickness for impulse propagation, the axon/fiber thickness ratio being 0.67-0.72 in young and 0.76-0.78 in adult fish. As already observed by previous investigators, the Mauthner axons lacked nodes of Ranvier. However, Schmidt-Lantermann's clefts (SLC) were present at irregular intervals. Within the SLC, parallel arranged osmiophilic bands of variable length and with a thickness of approx. 42-44 nm were observed to form a transitional zone between the cytoplasmic areas of the oligodendrocyte and the typical myelin structure. Between such adjacent 'D-bands', which thinned out to build up the major dense lines, an electron translucent area measuring approx. 25--26 nm in width contained a thin 'I-band' (8--10 nm) which was continuous with the intraperiod line. It is speculated that, in the Mauthner axon, the SLCs may be sites where freshly synthesized myelin is added to the lamellae already present, thus permitting their longitudinal growth.

Animals↗
PubMed2005

Subsurface cisterna-lined axonal invaginations and double-walled vesicles at the axonal-myelin sheath interface.

The axonal-myelin sheath interface of vertebrate myelinated axons possesses special structural complexities, and there may be an intercellular macromolecular traffic transversing the periaxonal cleft that spans the internodal axon. By conventional electron microscopy and serial sectioning, we observed a category of double-walled vesicles at the axonal-myelin sheath interface, which often contained ribosome-like particles or endoplasmic reticulum. Some of them were demonstrated to continue with the subjacent axon with a thin stalk. In addition, we described a special category of axonal invaginations, probably mediated by subsurface cisternae. The functional implications of these specialized structures were discussed.

Action Potentials↗
PubMed2002

Measurement of the repeat period of myelin sheath using ultrathin frozen sections.

The myelin sheath of peripheral nerves was observed by transmission electron microscopy (TEM) using plastic-embedded sections and ultrathin frozen sections. Repeat distances of myelin sheaths were measured in high-powered electron micrographs. The ultrathin frozen sections showed a longer repeat distance than the plastic-embedded sections. The ultrathin frozen sections were thought to contain fewer artefacts, as they had not been subject to dehydration and embedding. It is known that broken myelin sheaths are often observed under conventional TEM. It is thought that these procedures cause contraction and partial destruction of the myelin sheath.

Animals↗