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Journal articles on the topic 'Myelin protein zero'

Author: Grafiati

Published: 2 June 2025

Last updated: 31 July 2025

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1

Choe, Senyon. "Packing of Myelin Protein Zero." Neuron 17, no. 3 (1996): 363–65. http://dx.doi.org/10.1016/s0896-6273(00)80167-1.

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2

Raasakka, Arne, and Petri Kursula. "How Does Protein Zero Assemble Compact Myelin?" Cells 9, no. 8 (2020): 1832. http://dx.doi.org/10.3390/cells9081832.

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Myelin protein zero (P0), a type I transmembrane protein, is the most abundant protein in peripheral nervous system (PNS) myelin—the lipid-rich, periodic structure of membrane pairs that concentrically encloses long axonal segments. Schwann cells, the myelinating glia of the PNS, express P0 throughout their development until the formation of mature myelin. In the intramyelinic compartment, the immunoglobulin-like domain of P0 bridges apposing membranes via homophilic adhesion, forming, as revealed by electron microscopy, the electron-dense, double “intraperiod line” that is split by a narrow,

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3

Spiryda, Lisa. "Myelin protein zero and membrane adhesion." Journal of Neuroscience Research 54, no. 2 (1998): 137–46. http://dx.doi.org/10.1002/(sici)1097-4547(19981015)54:2<137::aid-jnr2>3.0.co;2-f.

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4

Raasakka, Arne, Oda C. Krokengen, Robert Schneider, and Petri Kursula. "Myelin protein zero - the structural foundation behind peripheral compact myelin." Biophysical Journal 122, no. 3 (2023): 500a. http://dx.doi.org/10.1016/j.bpj.2022.11.2669.

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5

Fernandez-Valle, C., N. Fregien, P. M. Wood, and M. B. Bunge. "Expression of the protein zero myelin gene in axon-related Schwann cells is linked to basal lamina formation." Development 119, no. 3 (1993): 867–80. http://dx.doi.org/10.1242/dev.119.3.867.

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A Schwann cell has the potential to differentiate into either a myelinating or ensheathing cell depending upon signals received from the axon that it contacts. Studies focusing on the pathway leading to myelination demonstrated that Schwann cells must form a basal lamina in order to myelinate an axon. In this report, we describe studies that indicate that initiation of basal lamina synthesis is required for Schwann cells to distinguish between myelination-inducing axons and axons that do not induce myelination, and to respond by undergoing the appropriate genetic and cellular changes. We have

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6

Warner, Laura E., Benjamin B. Roa, and James R. Lupski. "Settling the myelin protein zero question in CMT1B." Nature Genetics 11, no. 2 (1995): 119–20. http://dx.doi.org/10.1038/ng1095-119.

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7

D’Urso, Donatella, Peter Ehrhardt, and Hans Werner Müller. "Peripheral Myelin Protein 22 and Protein Zero: a Novel Association in Peripheral Nervous System Myelin." Journal of Neuroscience 19, no. 9 (1999): 3396–403. http://dx.doi.org/10.1523/jneurosci.19-09-03396.1999.

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8

Gould, Robert M., Todd Oakley, Jared V. Goldstone, Jason C. Dugas, Scott T. Brady, and Alexander Gow. "Myelin sheaths are formed with proteins that originated in vertebrate lineages." Neuron Glia Biology 4, no. 2 (2008): 137–52. http://dx.doi.org/10.1017/s1740925x09990238.

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All vertebrate nervous systems, except those of agnathans, make extensive use of the myelinated fiber, a structure formed by coordinated interplay between neuronal axons and glial cells. Myelinated fibers, by enhancing the speed and efficiency of nerve cell communication allowed gnathostomes to evolve extensively, forming a broad range of diverse lifestyles in most habitable environments. The axon-covering myelin sheaths are structurally and biochemically novel as they contain high portions of lipid and a few prominent low molecular weight proteins often considered unique to myelin. Here we se

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9

Peirano, Reto I., Derk E. Goerich, Dieter Riethmacher, and Michael Wegner. "Protein Zero Gene Expression Is Regulated by the Glial Transcription Factor Sox10." Molecular and Cellular Biology 20, no. 9 (2000): 3198–209. http://dx.doi.org/10.1128/mcb.20.9.3198-3209.2000.

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ABSTRACT Myelinating glia express high levels of a unique set of genes which code for structural proteins of the myelin sheath. Few transcription factors have so far been implicated in the regulation of any myelin gene. Here we show that the protein zero (P0) gene, a myelin gene exclusively expressed in the Schwann cell lineage of the peripheral nervous system, is controlled in its expression by the high-mobility-group domain protein Sox10 both in tissue culture and in vivo. Induction of wild-type Sox10, but not of other transcription factors or Sox10 mutants, strongly increased endogenous P0e

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10

Georgiou, John, and Milton P. Charlton. "Non-myelin-forming perisynaptic Schwann cells express protein zero and myelin-associated glycoprotein." Glia 27, no. 2 (1999): 101–9. http://dx.doi.org/10.1002/(sici)1098-1136(199908)27:2<101::aid-glia1>3.0.co;2-h.

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11

Souayah, Nizar, and Peter Siao Tick Chong. "Asymmetric Phenotype Associated With Rare Myelin Protein Zero Mutation." Journal of Clinical Neuromuscular Disease 11, no. 3 (2010): 110–13. http://dx.doi.org/10.1097/cnd.0b013e3181c5058a.

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12

Mandich, P., G. L. Mancardi, A. Varese, et al. "Congenital hypomyelination due to myelin protein zero Q215X mutation." Annals of Neurology 45, no. 5 (1999): 676–78. http://dx.doi.org/10.1002/1531-8249(199905)45:5<676::aid-ana21>3.0.co;2-k.

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13

Hasse, Birgit, Frank Bosse, Helmut Hanenberg, and Hans Werner Müller. "Peripheral myelin protein 22 kDa and protein zero: domain specific trans-interactions." Molecular and Cellular Neuroscience 27, no. 4 (2004): 370–78. http://dx.doi.org/10.1016/j.mcn.2004.06.009.

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14

Plotkowski, Megan L., Sanguk Kim, Martin L. Phillips, Anthony W. Partridge, Charles M. Deber, and James U. Bowie. "Transmembrane Domain of Myelin Protein Zero Can Form Dimers: Possible Implications for Myelin Construction†." Biochemistry 46, no. 43 (2007): 12164–73. http://dx.doi.org/10.1021/bi701066h.

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15

Murad, Abbas Mahmood, Maysaa Jalal Majeed, Rafid Badri Al-Ameri, and Ahmed Salim AL-Haidari. "Serum Myelin Oligodendrocyte Glycoprotein and Myelin Protein Zero as Diagnostic Biomarkers in Diabetic Neuropathy." AL-Kindy College Medical Journal 19, no. 1 (2023): 42–47. http://dx.doi.org/10.47723/kcmj.v19i1.859.

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Background: Diabetic neuropathy can affect any peripheral nerve, including sensory neurons, motor neurons, and the autonomic nervous system. Therefore, diabetic neuropathy has the potential to affect essentially any organ and can affect parts of the nervous system like the optic nerve, spinal cord, and brain. In addition, chronic hyperglycemia affects Schwann cells, and more severe patterns of diabetic neuropathy in humans involve demyelization. Schwann cell destruction might cause a number of changes in the axon. study aims to evaluate serum myelin protein level as a predicting marker in the

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16

Kim, Hye-Jung, Cha-Gyun Jung, Mark A. Jensen, Danuta Dukala, and Betty Soliven. "Targeting of Myelin Protein Zero in a Spontaneous Autoimmune Polyneuropathy." Journal of Immunology 181, no. 12 (2008): 8753–60. http://dx.doi.org/10.4049/jimmunol.181.12.8753.

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17

Sago, Haruhiko, Ying Su, and Roger Lebo. "Reply to “Settling the myelin protein zero question in CMT1B”." Nature Genetics 11, no. 2 (1995): 120. http://dx.doi.org/10.1038/ng1095-120.

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18

Shy, Michael E. "Peripheral neuropathies caused by mutations in the myelin protein zero." Journal of the Neurological Sciences 242, no. 1-2 (2006): 55–66. http://dx.doi.org/10.1016/j.jns.2005.11.015.

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19

Souayah, Nizar, W. K. Seltzer, Thomas H. Brannagan, Russell L. Chin, and Howard W. Sander. "Rare myelin protein zero sequence variant in late onset CMT1B." Journal of the Neurological Sciences 263, no. 1-2 (2007): 177–79. http://dx.doi.org/10.1016/j.jns.2007.05.020.

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20

Souayah, N., and P. Siao Tick Chong. "58. Asymmetric phenotype associated with rare Myelin protein zero mutation." Clinical Neurophysiology 120, no. 2 (2009): e105. http://dx.doi.org/10.1016/j.clinph.2008.10.076.

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21

Brösamle, Christian. "The myelin proteolipid DMalpha in fishes." Neuron Glia Biology 6, no. 2 (2009): 109–12. http://dx.doi.org/10.1017/s1740925x09000131.

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Vertebrate myelin membranes are compacted and held in close apposition by three structural proteins of myelin, myelin basic protein, myelin protein zero (MPZ) and myelin proteolipid protein (PLP1/DMalpha). PLP1/DMalpha is considered to function as a scaffolding protein and play a role in intracellular trafficking in oligodendrocytes. In humans, point mutations, duplications or deletions of PLP1 are associated with Pelizaeus–Merzbacher disease and spastic paraplegia Type 2. PLP1 is highly conserved between mammals, but less so in lower vertebrates. This has led some researchers to question whet

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22

Luo, XiaoYang, Deepak Sharma, Hideyo Inouye та ін. "Cytoplasmic Domain of Human Myelin Protein Zero Likely Folded as β-Structure in Compact Myelin". Biophysical Journal 92, № 5 (2007): 1585–97. http://dx.doi.org/10.1529/biophysj.106.094722.

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23

Smirnova, Evgeniya V., Tatiana V. Rakitina, Rustam H. Ziganshin, et al. "Identification of Myelin Basic Protein Proximity Interactome Using TurboID Labeling Proteomics." Cells 12, no. 6 (2023): 944. http://dx.doi.org/10.3390/cells12060944.

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Myelin basic protein (MBP) is one of the key structural elements of the myelin sheath and has autoantigenic properties in multiple sclerosis (MS). Its intracellular interaction network is still partially deconvoluted due to the unfolded structure, abnormally basic charge, and specific cellular localization. Here we used the fusion protein of MBP with TurboID, an engineered biotin ligase that uses ATP to convert biotin to reactive biotin-AMP that covalently attaches to nearby proteins, to determine MBP interactome. Despite evident benefits, the proximity labeling proteomics technique generates

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24

Raasakka, Arne, Nykola C. Jones, Søren Vrønning Hoffmann, and Petri Kursula. "Ionic strength and calcium regulate membrane interactions of myelin basic protein and the cytoplasmic domain of myelin protein zero." Biochemical and Biophysical Research Communications 511, no. 1 (2019): 7–12. http://dx.doi.org/10.1016/j.bbrc.2019.02.025.

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25

Fratta, Pietro, Francesca Ornaghi, Gabriele Dati, et al. "A nonsense mutation in myelin protein zero causes congenital hypomyelination neuropathy through altered P0 membrane targeting and gain of abnormal function." Human Molecular Genetics 28, no. 1 (2018): 124–32. http://dx.doi.org/10.1093/hmg/ddy336.

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Abstract Protein zero (P0) is the major structural protein in peripheral myelin, and mutations in the Myelin Protein Zero (Mpz) gene produce wide-ranging hereditary neuropathy phenotypes. To gain insight in the mechanisms underlying a particularly severe form, congenital hypomyelination (CH), we targeted mouse Mpz to encode P0Q215X, a nonsense mutation associated with the disease, that we show escapes nonsense mediated decay and is expressed in CH patient nerves. The knock-in mice express low levels of the resulting truncated protein, producing a milder phenotype when compared to patients, all

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26

LeBlanc, Scott E., Rebecca M. Ward, and John Svaren. "Neuropathy-Associated Egr2 Mutants Disrupt Cooperative Activation of Myelin Protein Zero by Egr2 and Sox10." Molecular and Cellular Biology 27, no. 9 (2007): 3521–29. http://dx.doi.org/10.1128/mcb.01689-06.

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ABSTRACT Dominant mutations in the early growth response 2 (Egr2/Krox20) transactivator, a critical regulator of peripheral myelin development, have been associated with peripheral myelinopathies. These dominant mutants interfere with the expression of genes required for myelination by Schwann cells, including that for the most abundant peripheral myelin protein, Myelin protein zero (Mpz). In this study, we show that Egr2 mutants specifically affect an Egr2-responsive element within the Mpz first intron that also contains binding sites for the transcription factor Sox10. Furthermore, Egr2 acti

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27

Watanabe, M., N. Yamamoto, N. Ohkoshi, et al. "Corticosteroid- responsive asymmetric neuropathy with a myelin protein zero gene mutation." Neurology 59, no. 5 (2002): 767–69. http://dx.doi.org/10.1212/wnl.59.5.767.

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28

LeBlanc, Scott E., Sung-Wook Jang, Rebecca M. Ward, Lawrence Wrabetz, and John Svaren. "Direct Regulation of Myelin Protein Zero Expression by the Egr2 Transactivator." Journal of Biological Chemistry 281, no. 9 (2005): 5453–60. http://dx.doi.org/10.1074/jbc.m512159200.

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29

Marchini, Corrado, Sandro Zambito Marsala, Matteo Bendini, et al. "Myelin protein zero Val102fs mutation manifesting with isolated spinal root hypertrophy." Neuromuscular Disorders 19, no. 12 (2009): 849–52. http://dx.doi.org/10.1016/j.nmd.2009.09.004.

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30

Lemke, Greg, Elise Lamar, and John Patterson. "Isolation and analysis of the gene encoding peripheral myelin protein zero." Neuron 1, no. 1 (1988): 73–83. http://dx.doi.org/10.1016/0896-6273(88)90211-5.

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31

Latour, P., C. Bonnebouche, M. Bost, et al. "A Rsal RFLP at the human myelin protein zero (MPZ) locus." Clinical Genetics 46, no. 4 (2008): 327–28. http://dx.doi.org/10.1111/j.1399-0004.1994.tb04172.x.

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32

Prada, Valeria, Mario Passalacqua, Maria Bono, et al. "Gain of glycosylation: A new pathomechanism of myelin protein zero mutations." Annals of Neurology 71, no. 3 (2012): 427–31. http://dx.doi.org/10.1002/ana.22695.

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33

Liu, Zhigang, Yong Wang, Ravikiran S. Yedidi, et al. "Crystal structure of the extracellular domain of human myelin protein zero." Proteins: Structure, Function, and Bioinformatics 80, no. 1 (2011): 307–13. http://dx.doi.org/10.1002/prot.23164.

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34

Yoshida, M., and D. R. Colman. "Parallel Evolution and Coexpression of the Proteolipid Proteins and Protein Zero in Vertebrate Myelin." Neuron 16, no. 6 (1996): 1115–26. http://dx.doi.org/10.1016/s0896-6273(00)80138-5.

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35

Bielecki, Bartosz, Claudia Mattern, Abdel M. Ghoumari, et al. "Unexpected central role of the androgen receptor in the spontaneous regeneration of myelin." Proceedings of the National Academy of Sciences 113, no. 51 (2016): 14829–34. http://dx.doi.org/10.1073/pnas.1614826113.

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Lost myelin can be replaced after injury or during demyelinating diseases in a regenerative process called remyelination. In the central nervous system (CNS), the myelin sheaths, which protect axons and allow the fast propagation of electrical impulses, are produced by oligodendrocytes. The abundance and widespread distribution of oligodendrocyte progenitors (OPs) within the adult CNS account for this remarkable regenerative potential. Here, we report a key role for the male gonad, testosterone, and androgen receptor (AR) in CNS remyelination. After lysolecithin-induced demyelination of the ma

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36

Stögbauer, Florian, Peter Young, Heiko Wiebusch, et al. "Absence of mutations in peripheral myelin protein-22, myelin protein zero, and connexin 32 in autosomal recessive Dejerine-Sottas syndrome." Neuroscience Letters 240, no. 1 (1998): 1–4. http://dx.doi.org/10.1016/s0304-3940(97)00887-2.

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37

Catapano, M., T. Ewart, and S. Baker. "Auto-antibodies against gangliosides in patients with Charcot-Marie-Tooth disease." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 42, S1 (2015): S34. http://dx.doi.org/10.1017/cjn.2015.158.

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Background: In Charcot-Marie Tooth (CMT), vital components of either the myelin sheath or axon are abnormal, slowing nerve conduction and causing functional disability. Recently, there has been speculation the CMT may have an autoimmune component resulting from abnormal protein expression. Methods: Custom autoimmune neuropathy-focused microarray panels were printed in-house using antigens from Sigma, Abnova, Fitzgerald and Matreya according to Cambridge Life Science instructions. Antigens including Myelin Protein Zero, Peripheral Myelin Protein 22, and 20 other well-known gangliosides were tes

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38

Gaboreanu, Ana-Maria, Ronald Hrstka, Wenbo Xu та ін. "Myelin protein zero/P0 phosphorylation and function require an adaptor protein linking it to RACK1 and PKCα". Journal of Cell Biology 177, № 4 (2007): 707–16. http://dx.doi.org/10.1083/jcb.200608060.

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Point mutations in the cytoplasmic domain of myelin protein zero (P0; the major myelin protein in the peripheral nervous system) that alter a protein kinase Cα (PKCα) substrate motif (198HRSTK201) or alter serines 199 and/or 204 eliminate P0-mediated adhesion. Mutation in the PKCα substrate motif (R198S) also causes a form of inherited peripheral neuropathy (Charcot Marie Tooth disease [CMT] 1B), indicating that PKCα-mediated phosphorylation of P0 is important for myelination. We have now identified a 65-kD adaptor protein that links P0 with the receptor for activated C kinase 1 (RACK1). The i

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39

Fabrizi, G. M., F. Taioli, T. Cavallaro, et al. "Focally folded myelin in Charcot-Marie-Tooth neuropathy type 1B with Ser49Leu in the myelin protein zero." Acta Neuropathologica 100, no. 3 (2000): 299–304. http://dx.doi.org/10.1007/s004019900175.

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40

Shames, Igor, Andrew Fraser, Joshua Colby, Wayel Orfali, and G. Jackson Snipes. "Phenotypic Differences between Peripheral Myelin Protein-22 (PMP22) and Myelin Protein Zero (P0) Mutations Associated with Charcot-Marie-Tooth-Related Diseases." Journal of Neuropathology & Experimental Neurology 62, no. 7 (2003): 751–64. http://dx.doi.org/10.1093/jnen/62.7.751.

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41

Saiki, Tomokazu, Nobuhisa Nakamura, Megumi Miyabe, et al. "The Effects of Insulin on Immortalized Rat Schwann Cells, IFRS1." International Journal of Molecular Sciences 22, no. 11 (2021): 5505. http://dx.doi.org/10.3390/ijms22115505.

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Schwann cells play an important role in peripheral nerve function, and their dysfunction has been implicated in the pathogenesis of diabetic neuropathy and other demyelinating diseases. The physiological functions of insulin in Schwann cells remain unclear and therefore define the aim of this study. By using immortalized adult Fischer rat Schwann cells (IFRS1), we investigated the mechanism of the stimulating effects of insulin on the cell proliferation and expression of myelin proteins (myelin protein zero (MPZ) and myelin basic protein (MBP). The application of insulin to IFRS1 cells increas

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42

Su, Y., D. G. Brooks, L. Li, et al. "Myelin protein zero gene mutated in Charcot-Marie-tooth type 1B patients." Proceedings of the National Academy of Sciences 90, no. 22 (1993): 10856–60. http://dx.doi.org/10.1073/pnas.90.22.10856.

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43

Brown, Adrienne M., and Greg Lemke. "Multiple Regulatory Elements Control Transcription of the Peripheral Myelin Protein Zero Gene." Journal of Biological Chemistry 272, no. 46 (1997): 28939–47. http://dx.doi.org/10.1074/jbc.272.46.28939.

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44

Salerno, G., C. Ortez, H. Gálvez, et al. "G.P.88 Peripheral neuropathies caused by mutations in the myelin protein zero." Neuromuscular Disorders 22, no. 9-10 (2012): 868. http://dx.doi.org/10.1016/j.nmd.2012.06.218.

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45

Wrabetz, L. "Different Intracellular Pathomechanisms Produce Diverse Myelin Protein Zero Neuropathies in Transgenic Mice." Journal of Neuroscience 26, no. 8 (2006): 2358–68. http://dx.doi.org/10.1523/jneurosci.3819-05.2006.

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46

Maeda, Meiko Hashimoto, Jun Mitsui, Bing-Wen Soong, et al. "Increased gene dosage of myelin protein zero causes Charcot-Marie-Tooth disease." Annals of Neurology 71, no. 1 (2012): 84–92. http://dx.doi.org/10.1002/ana.22658.

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47

Briani, Chiara, Fausto Adami, Tiziana Cavallaro, Federica Taioli, Sergio Ferrari, and Gianmaria Fabrizi. "Axonal neuropathy due to myelin protein zero mutation misdiagnosed as amyloid neuropathy." Muscle & Nerve 38, no. 1 (2008): 921–23. http://dx.doi.org/10.1002/mus.21062.

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48

Bond, Jeremy P., Raul A. Saavedra, and Daniel A. Kirschner. "Expression and Purification of the Extracellular Domain of Human Myelin Protein Zero." Protein Expression and Purification 23, no. 3 (2001): 398–410. http://dx.doi.org/10.1006/prep.2001.1525.

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49

Pham, Bach-Nga, Milan Rudic, Didier Bouccara, et al. "Antibodies to myelin protein zero (P0) protein as markers of auto-immune inner ear diseases." Autoimmunity 40, no. 3 (2007): 202–7. http://dx.doi.org/10.1080/08916930701248555.

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50

Yu, Tianshu, Ling Liang, Xuyang Zhao, and Yuxin Yin. "Structural and biochemical studies of the extracellular domain of Myelin protein zero-like protein 1." Biochemical and Biophysical Research Communications 506, no. 4 (2018): 883–90. http://dx.doi.org/10.1016/j.bbrc.2018.10.161.

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