Myelin-associated glycoprotein and myelin basic protein are present in central and peripheral nerve myelin throughout phylogeny

doi:10.1016/0197-0186(86)90186-5

Neurochemistry International

Volume 8, Issue 4, 1986, Pages 521-526

https://doi.org/10.1016/0197-0186(86)90186-5 Get rights and content

Abstract

This phylogenetic study of central and peripheral nervous system myelin proteins demonstrates that important changes occur in the composition of certain myelin proteins during evolution. Only two components, myelin basic protein (MBP) and myelin-associated glycoprotein (MAG) are present in all Gnathostomata representatives investigated. While MBP components varied considerably even among the representatives of a given order, the apparent molecular weight of MAG showed little variation indicating that the conservation of the molecular structure could be important for the function of MAG in glia axon interactions.

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Cited by (18)

Evolution of myelinated nervous systems
2007, Evolution of Nervous Systems
It is probably not surprising that the myelinated nervous system and jaws are two characters that originated in the common gnathostome ancestors. For myelination would both allow rapid wielding of powerful jaws and rapid swimming responses as a means to escape. Clearly the structural features of oligodendrocyte (OL)-based central nervous system (CNS) myelin and Schwann cell-based peripheral nervous system (PNS) originated in the common gnathostome ancestor, as, without exception, among species examined, OLs myelinate all large-caliber CNS axons and Schwann cells myelinate all large-caliber PNS axons. In spite of the fact that most of our current understanding of myelination comes from studies with common laboratory animals, mainly rodents, and that many current techniques are designed for working with these animals, a substantial and growing literature exists on myelination in nonmammalian vertebrate species and, to a lesser extent, myelination in invertebrates. The need for more diversification has recently been stressed, and investigators who consider their research from an evolutionary perspective, e.g., use GenBank data to suggest evolutionary features of molecular interactions, as was done for ion channel–ankyrin interactions, will give their research wider scope.
Understanding Myelination Through Studying Its Evolution
2006, International Review of Neurobiology
Citation Excerpt :
Among these, identifications of homologs in nonmammalian vertebrates are growing. Antibody‐based evidence that MAG is ubiquitously expressed among vertebrates (Matthieu et al., 1986), had been disputed (Hammer et al., 1993; Zand et al., 1991) and the issue was not resolved until recent screening of pufferfish and zebrafish genomes identifying several MAG, also called siglec‐4 (sialic acid binding protein) isoforms in these fish (Lehmann et al., 2004). Finding fish homologs of MAG is having an impact on efforts to understand the evolutionary loss of CNS regeneration (see Section VI).
This chapter discusses many studies that provide insights into the origins of central (CNS) and peripheral nervous system (PNS) myelination and into the reasons that CNS regeneration in adult vertebrates is restricted to fish and amphibians. As in other fields, studying biological processes through their evolutionary history, in their own right, provides important and novel insights into human diseases in which myelin sheaths develop abnormally and/or following normal development they disassemble and are degraded. The chapter studies mechanisms for the adaptation of sophisticated regulation that underlies myelination for animals living under conditions far different from example, without thermoregulation or different osmotic environments. Among the animal models with a rapidly growing following is the zebra, which is being used more frequently by ‘‘myelin ’’ scientists. As more and more sequences from genome-sequencing projects relevant to vertebrate and invertebrate evolution become available, appreciation of evolutionary adaptations made by the plethora of molecules associated with differing facets of the myelination process is realized.
Conservation of functionally important epitopes on myelin associated glycoprotein (MAG)
1995, Comparative Biochemistry and Physiology -- Part B: Biochemistry and
Phylogenetic conservation of protein domains often points to functionally important regions. As a step toward mapping these sites on myelin associated glycoprotein (MAG) we have determined the species distribution of epitopes recognized by a panel of anti-MAG antibodies (Ab). Monoclonal antibodies (mAb) B11F7, GenS3 and 28 recognized MAG only in mammalian species. However, the mAb 513 which inhibits MAG binding recognized a conformational epitope in a wider distribution of species including, human (Homo sapiens), bovine (Bos taurus), rat (Rattus norvegicus), chicken (Gallus gallus), quail (Coturnix coturnix japonica), lizard (Iguana iguana), snake (Thamnophis sirtalis), frog (Xenopus laevis) and turtle (all tetrapods) but not in goldfish (Crassius aurata) (a teleost). However, only MAG from mammals was shown to bind rat dorsal ganglion neurons (DRGs) suggesting that structures additional to those recognized by mAb 513 must be involved in function. Antibody 28, on the other hand, recognized only MAG species which bound to neurons, suggesting that this epitope, in comparison with mAb 513, more closely represented the functionally important region of MAG. Observed species differences in glycosylation of MAG may be functionally significant. A newly developed polyclonal Ab against MAG recognized the protein in tetrapods and teleosts, but not chondricthyes. The results show that MAG is present in a wide spectrum of species.
Patterns of spread of different demyelinating processes in the myelin sheath
1992, Progress in Neurobiology
A glycosylated proteolipid protein is common to CNS myelin of recent lungfish (Ceratodiae, Lepidosirenidae)
1987, Comparative Biochemistry and Physiology -- Part B: Biochemistry and
- 1.
  1. Myelin proteins from the CNS of recent lungfish (Lepidosiren paradoxa, Protopterus dolloi, Neoceratodus forsteri) were separated and analysed by staining and immunoblotting.
- 2.
  2. All species showed a glycosylated component (g-PLP) that cross-reacted with antibodies against tetrapod proteolipid protein (PLP), indicating phylogenetic relationships with amphibia.
- 3.
  3. Actinopterygian IP or teleostean 36 k components were not detectable in lungfish CNS myelin.
- 4.
  4. The identical size of g-PLPs from Lepidosiren and Protopterus (M_r = 29,000) underlines the close relationship of the Lepidosirenidae. The smaller size of g-PLP from the ceratodidan Neoceratodus forsteri (M_r = 27,500) pointed to an earlier diversion.
Appearance of Myelin proteins during vertebrate evolution
1986, Neurochemistry International
Myelin, defined as an arrangement of spirally fused unit membranes, is an acquisition of vertebrates and first appeared during evolution in Gnathostomata. In all species studied PNS and CNS myelins contain the myelin-associated glycoprotein (MAG) and the myelin basic protein (MBP). Throughout phylogeny PNS myelin is characterized by the major P₀ glycoprotein which is called IP in fishes. The PNS myelin proteins did not evolve further except for the addition of P₂ protein from reptiles onward. In Elasmobranchii and Chondrostei, PNS and CNS myelin proteins are similar. CNS myelin of actinopterygian fishes possesses a 36,000 Da protein (36K) in addition to P₀-like IP glycoproteins. In tetrapod CNS myelin, P₀ is replaced by the proteolipid protein (PLP) and the Wolfgram protein (WP). Of particular interest in a transitional phylogenetic sense are the lungfish Protopterus, carrying glycosylated PLP (g-PLP) but no P₀, 36K or WP, and the bichir Polypterus, showing simultaneous presence of P₀, 36K and PLP.
These results indicate that myelin proteins could be valuable molecular markers in establishing vertebrate phylogenetic relationships and in reconstructing the fish-tetrapod transition.

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Myelin-associated glycoprotein and myelin basic protein are present in central and peripheral nerve myelin throughout phylogeny

Abstract

Neurosci. Lett.

J. biol. Chem.

Brain Res.

FEBS Lett.

Cell

J. biol. Chem.

Devl Biol.

Brain Res.

Brain Res.

Neurosci. Lett.

Brain Res.

Biochim. biophys. Acta

Brain Res.

Neurochem. Int.

Neurosci. Lett.

Partial characterization of a new myelin protein component

J. Neurochem.

Comparison of 2′,3′-cyclic nucleotide 3′-phosphodiesterase and the major component of Wolfgram protein WI

J. Neurochem.

Biochemical demonstration of the myelin-associated glycoprotein in the peripheral nervous system

J. Neurochem.

IgM in a human neuropathy related to paraproteinemia binds to a carbohydrate determinant in the myelin-associated glycoprotein and to a ganglioside

Bony fish myelin: evidence for common major structural glycoproteins in central and peripheral myelin of trout

J. Neurochem.