Myelin lipids: A phylogenetic study

Bürgisser, Philippe; Matthieu, Jean‐Marie; Jeserich, G.; Waehneldt, Thomas V.

doi:10.1007/bf00966121

Cited by 30 publications

(11 citation statements)

References 29 publications

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“…A similar lipid composition has been reported for other teleosts, and the same lipids are present in higher vertebrates [16]. Phosphatidylcholine was more abundant in the PNS than CNS, in contrast to that of trout that had displayed similar levels [16,48], and ran ahead of the standard.…”

Section: P0-like Proteins Were Found In Both the Cns And Pns Myelins supporting

confidence: 74%

Myelin Structure and Composition in Zebrafish

et al. 2006

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To establish a standard for genotype/phenotype studies on the myelin of zebrafish (Danio rerio), an organism increasingly popular as a model system for vertebrates, we have initiated a detailed characterization of the structure and biochemical composition of its myelinated central and peripheral nervous system (CNS; PNS) tissues. Myelin periods, determined by X-ray diffraction from whole, unfixed optic and lateral line nerves, were approximately 153 and approximately 162 Angstrom, respectively. In contrast with the lability of PNS myelin in higher vertebrates, zebrafish lateral line nerve myelin exhibited structural stability when exposed to substantial changes in pH and ionic strength. Neither optic nor lateral line nerves showed swelling at the cytoplasmic apposition in CaCl(2)-containing Ringer's solution, in contrast with nerves from other teleost and elasmobranch fishes. Zebrafish optic nerve showed greater stability against changes in NaCl and CaCl(2) than lateral line nerve. The nerves from zebrafish having mutations in the gene for myelin basic protein (mbpAla2Thr and mbpAsp25Val) showed similar myelin periods as the wildtype (WT), but gave approximately 20% less compact myelin. Analysis of proteins by SDS-PAGE and Western blotting identified in both CNS and PNS of WT zebrafish two orthologues of myelin P0 glycoprotein that have been characterized extensively in trout--intermediate protein 1 (24 kDa) and intermediate protein 2 (28 kDa). Treatment with endoglycosidase-F demonstrated a carbohydrate moiety of approximately 7 kDa, which is nearly threefold larger than for higher vertebrates. Thin-layer chromatography for lipids revealed a similar composition as for other teleosts. Taken together, these data will serve as a baseline for detecting changes in the structure and/or amount of myelin resulting from mutations in myelin-related genes or from exogenous, potentially cytotoxic compounds that could affect myelin formation or stability.

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Section: P0-like Proteins Were Found In Both the Cns And Pns Myelins supporting

confidence: 74%

Myelin Structure and Composition in Zebrafish

et al. 2006

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“…Indeed, the high cholesterol level in myelin may have evolved by its molecular association with PLP. This idea is supported by the finding that the cholesterol content of myelin is similar across various tetrapod species (Burgisser et al, 1986) but lower in fish (Kirschner et al, 1989). Together this suggests an intriguing correlation between the evolutionarily increased abundance of PLP and of cholesterol in CNS myelin at the root of tetrapods, coinciding with the emergence of the PLP-specific loop.…”

Section: Coevolution Of Myelin Protein and Lipid Compositionmentioning

confidence: 70%

A critical role for the cholesterol‐associated proteolipids PLP and M6B in myelination of the central nervous system

Werner

Krämer-Albers

Strenzke

et al. 2013

Glia

103

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The formation of central nervous system myelin by oligodendrocytes requires sterol synthesis and is associated with a significant enrichment of cholesterol in the myelin membrane. However, it is unknown how oligodendrocytes concentrate cholesterol above the level found in nonmyelin membranes. Here, we demonstrate a critical role for proteolipids in cholesterol accumulation. Mice lacking the most abundant myelin protein, proteolipid protein (PLP), are fully myelinated, but PLP-deficient myelin exhibits a reduced cholesterol content. We therefore hypothesized that "high cholesterol" is not essential in the myelin sheath itself but is required for an earlier step of myelin biogenesis that is fully compensated for in the absence of PLP. We also found that a PLP-homolog, glycoprotein M6B, is a myelin component of low abundance. By targeting the Gpm6b-gene and crossbreeding, we found that single-mutant mice lacking either PLP or M6B are fully myelinated, while double mutants remain severely hypomyelinated, with enhanced neurodegeneration and premature death. As both PLP and M6B bind membrane cholesterol and associate with the same cholesterol-rich oligodendroglial membrane microdomains, we suggest a model in which proteolipids facilitate myelination by sequestering cholesterol. While either proteolipid can maintain a threshold level of cholesterol in the secretory pathway that allows myelin biogenesis, lack of both proteolipids results in a severe molecular imbalance of prospective myelin membrane. However, M6B is not efficiently sorted into mature myelin, in which it is 200-fold less abundant than PLP. Thus, only PLP contributes to the high cholesterol content of myelin by association and co-transport.

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“…Previous studies have identified the major myelin proteins present in teleosts (Burgisser et al, 1986). To confirm that these proteins are similar in zebrafish, myelin was purified from adult zebrafish brains, using sucrose gradients, separated on a 4 -12% gradient acrylamide gel, and stained with GelCode Blue reagent (Pierce) to reveal major myelin proteins (p100, p64, p36, p24, p17, p14, and p8) (Fig.…”

Section: Protein Composition Of Zebrafish Myelin Is Similar To Mammalmentioning

confidence: 98%

The 36K protein of zebrafish CNS myelin is a short‐chain dehydrogenase

Morris

Willard

Yin

et al. 2003

Glia

Self Cite

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Previous studies identified homologues to mammalian myelin genes expressed in the teleost central nervous system (CNS), including myelin basic protein (MBP), protein zero (P0), and a member of the proteolipid protein family, DM20. In addition, an uncharacterized 36-kDa (36K) protein is a major component of teleost myelin, but is not a major component of myelin in other species. In the present study, we sought to better understand myelin proteins and myelination in one teleost, zebrafish, by molecular characterization of the zebrafish 36K protein. Purified zebrafish CNS myelin was isolated and the amino acid sequences of peptides present in the 36-kDa band were determined by mass spectrometry. These sequences matched a previously uncharacterized EST in The Institute for Genome Research (TIGR) zebrafish database that is related to the short-chain dehydrogenase/reductase (SDR) protein family. In vitro expression of the zebrafish 36K cDNA in Neuro 2a cells resulted in a protein product that was recognized by a 36K polyclonal antibody. The zebrafish 36K mRNA and protein expression patterns were determined and correlated to other known myelin gene expression profiles. In addition, we determined by in situ hybridization that a human 36K homologue (FLJ13639) is expressed in oligodendrocytes and neurons in the adult human cortex. This study identified a major myelin protein in zebrafish, 36K, as a member of the SDR superfamily; an expression pattern similar to other myelin genes was demonstrated.

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Myelin lipids: A phylogenetic study

Cited by 30 publications

References 29 publications

Myelin Structure and Composition in Zebrafish

Myelin Structure and Composition in Zebrafish

A critical role for the cholesterol‐associated proteolipids PLP and M6B in myelination of the central nervous system

The 36K protein of zebrafish CNS myelin is a short‐chain dehydrogenase

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