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[PMID]:27009151
[Au] Autor:Motley WW; Palaima P; Yum SW; Gonzalez MA; Tao F; Wanschitz JV; Strickland AV; Löscher WN; De Vriendt E; Koppi S; Medne L; Janecke AR; Jordanova A; Zuchner S; Scherer SS
[Ad] Endereço:Department of Neurology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA Department of Medicine, Pennsylvania Hospital, University of Pennsylvania, Philadelphia, Pennsylvania 19107, USA.
[Ti] Título:De novo PMP2 mutations in families with type 1 Charcot-Marie-Tooth disease.
[So] Source:Brain;139(Pt 6):1649-56, 2016 Jun.
[Is] ISSN:1460-2156
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We performed whole exome sequencing on a patient with Charcot-Marie-Tooth disease type 1 and identified a de novo mutation in PMP2, the gene that encodes the myelin P2 protein. This mutation (p.Ile52Thr) was passed from the proband to his one affected son, and segregates with clinical and electrophysiological evidence of demyelinating neuropathy. We then screened a cohort of 136 European probands with uncharacterized genetic cause of Charcot-Marie-Tooth disease and identified another family with Charcot-Marie-Tooth disease type 1 that has a mutation affecting an adjacent amino acid (p.Thr51Pro), which segregates with disease. Our genetic and clinical findings in these kindred demonstrate that dominant PMP2 mutations cause Charcot-Marie-Tooth disease type 1.
[Mh] Termos MeSH primário: Doença de Charcot-Marie-Tooth/genética
Proteína P2 de Mielina/genética
[Mh] Termos MeSH secundário: Adolescente
Exoma/genética
Feminino
Predisposição Genética para Doença/genética
Haplótipos
Seres Humanos
Masculino
Meia-Idade
Mutação
Condução Nervosa/genética
Linhagem
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Myelin P2 Protein); 0 (PMP2 protein, human)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160325
[St] Status:MEDLINE
[do] DOI:10.1093/brain/aww055


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[PMID]:26828946
[Au] Autor:Hong YB; Joo J; Hyun YS; Kwak G; Choi YR; Yeo HK; Jwa DH; Kim EJ; Mo WM; Nam SH; Kim SM; Yoo JH; Koo H; Park HT; Chung KW; Choi BO
[Ad] Endereço:Stem Cell and Regenerative Medicine Center, Samsung Medical Center, Seoul, Korea.
[Ti] Título:A Mutation in PMP2 Causes Dominant Demyelinating Charcot-Marie-Tooth Neuropathy.
[So] Source:PLoS Genet;12(2):e1005829, 2016 Feb.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Charcot-Marie-Tooth disease (CMT) is a heterogeneous group of peripheral neuropathies with diverse genetic causes. In this study, we identified p.I43N mutation in PMP2 from a family exhibiting autosomal dominant demyelinating CMT neuropathy by whole exome sequencing and characterized the clinical features. The age at onset was the first to second decades and muscle atrophy started in the distal portion of the leg. Predominant fatty replacement in the anterior and lateral compartment was similar to that in CMT1A caused by PMP22 duplication. Sural nerve biopsy showed onion bulbs and degenerating fibers with various myelin abnormalities. The relevance of PMP2 mutation as a genetic cause of dominant CMT1 was assessed using transgenic mouse models. Transgenic mice expressing wild type or mutant (p.I43N) PMP2 exhibited abnormal motor function. Electrophysiological data revealed that both mice had reduced motor nerve conduction velocities (MNCV). Electron microscopy revealed that demyelinating fibers and internodal lengths were shortened in both transgenic mice. These data imply that overexpression of wild type as well as mutant PMP2 also causes the CMT1 phenotype, which has been documented in the PMP22. This report might expand the genetic and clinical features of CMT and a further mechanism study will enhance our understanding of PMP2-associated peripheral neuropathy.
[Mh] Termos MeSH primário: Doença de Charcot-Marie-Tooth/genética
Doenças Desmielinizantes/genética
Genes Dominantes
Proteína P2 de Mielina/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Doença de Charcot-Marie-Tooth/patologia
Doença de Charcot-Marie-Tooth/fisiopatologia
Segregação de Cromossomos
Simulação por Computador
Fenômenos Eletrofisiológicos
Família
Feminino
Células HEK293
Seres Humanos
Perna (Membro)/fisiopatologia
Imagem por Ressonância Magnética
Masculino
Camundongos Transgênicos
Dados de Sequência Molecular
Mutação
Proteína P2 de Mielina/química
Linhagem
Fenótipo
Nervo Sural/patologia
Nervo Sural/fisiopatologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Myelin P2 Protein); 0 (PMP2 protein, human)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:160205
[Lr] Data última revisão:
160205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160202
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1005829


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[PMID]:26527266
[Au] Autor:Laulumaa S; Blakeley MP; Raasakka A; Moulin M; Härtlein M; Kursula P
[Ad] Endereço:Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, PO Box 5400, 90014 Oulu, Finland.
[Ti] Título:Production, crystallization and neutron diffraction of fully deuterated human myelin peripheral membrane protein P2.
[So] Source:Acta Crystallogr F Struct Biol Commun;71(Pt 11):1391-5, 2015 Nov.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The molecular details of the formation of the myelin sheath, a multilayered membrane in the nervous system, are to a large extent unknown. P2 is a peripheral membrane protein from peripheral nervous system myelin, which is believed to play a role in this process. X-ray crystallographic studies and complementary experiments have provided information on the structure-function relationships in P2. In this study, a fully deuterated sample of human P2 was produced. Crystals that were large enough for neutron diffraction were grown by a ten-month procedure of feeding, and neutron diffraction data were collected to a resolution of 2.4 Å from a crystal of 0.09 mm(3) in volume. The neutron crystal structure will allow the positions of H atoms in P2 and its fatty-acid ligand to be visualized, as well as shedding light on the fine details of the hydrogen-bonding networks within the P2 ligand-binding cavity.
[Mh] Termos MeSH primário: Proteína P2 de Mielina/biossíntese
Proteína P2 de Mielina/genética
Bainha de Mielina/genética
Bainha de Mielina/metabolismo
Difração de Nêutrons/métodos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Cristalização
Seres Humanos
Dados de Sequência Molecular
Proteína P2 de Mielina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Myelin P2 Protein)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151104
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X15017902


  4 / 693 MEDLINE  
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[PMID]:26257172
[Au] Autor:Gonzaga-Jauregui C; Harel T; Gambin T; Kousi M; Griffin LB; Francescatto L; Ozes B; Karaca E; Jhangiani SN; Bainbridge MN; Lawson KS; Pehlivan D; Okamoto Y; Withers M; Mancias P; Slavotinek A; Reitnauer PJ; Goksungur MT; Shy M; Crawford TO; Koenig M; Willer J; Flores BN; Pediaditrakis I; Us O; Wiszniewski W; Parman Y; Antonellis A; Muzny DM; Katsanis N; Battaloglu E; Boerwinkle E; Gibbs RA; Lupski JR; Baylor-Hopkins Center for Mendelian Genomics
[Ad] Endereço:Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA; Center for Human Disease Modeling, Duke University, Durham, NC 27701, USA.
[Ti] Título:Exome Sequence Analysis Suggests that Genetic Burden Contributes to Phenotypic Variability and Complex Neuropathy.
[So] Source:Cell Rep;12(7):1169-83, 2015 Aug 18.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Charcot-Marie-Tooth (CMT) disease is a clinically and genetically heterogeneous distal symmetric polyneuropathy. Whole-exome sequencing (WES) of 40 individuals from 37 unrelated families with CMT-like peripheral neuropathy refractory to molecular diagnosis identified apparent causal mutations in ∼ 45% (17/37) of families. Three candidate disease genes are proposed, supported by a combination of genetic and in vivo studies. Aggregate analysis of mutation data revealed a significantly increased number of rare variants across 58 neuropathy-associated genes in subjects versus controls, confirmed in a second ethnically discrete neuropathy cohort, suggesting that mutation burden potentially contributes to phenotypic variability. Neuropathy genes shown to have highly penetrant Mendelizing variants (HPMVs) and implicated by burden in families were shown to interact genetically in a zebrafish assay exacerbating the phenotype established by the suppression of single genes. Our findings suggest that the combinatorial effect of rare variants contributes to disease burden and variable expressivity.
[Mh] Termos MeSH primário: Doença de Charcot-Marie-Tooth/genética
Exoma
Carga Genética
Doenças do Sistema Nervoso Periférico/genética
Fenótipo
[Mh] Termos MeSH secundário: Animais
Feminino
Variação Genética
Proteínas de Choque Térmico HSP40/genética
Seres Humanos
Masculino
Mutação
Proteína P2 de Mielina/genética
Linhagem
Penetrância
Serina C-Palmitoiltransferase/genética
Supressão Genética
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNAJB5 protein, human); 0 (HSP40 Heat-Shock Proteins); 0 (Myelin P2 Protein); 0 (PMP2 protein, human); EC 2.3.1.50 (SPTLC3 protein, human); EC 2.3.1.50 (Serine C-Palmitoyltransferase)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150811
[St] Status:MEDLINE


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[PMID]:26186926
[Au] Autor:Calik MW; Shankarappa SA; Langert KA; Stubbs EB
[Ad] Endereço:Center for Narcolepsy, Sleep and Health Research, Department of Biobehavioral Health Science, University of Illinois at Chicago, Chicago, IL, USA.
[Ti] Título:Forced Exercise Preconditioning Attenuates Experimental Autoimmune Neuritis by Altering Th1 Lymphocyte Composition and Egress.
[So] Source:ASN Neuro;7(4), 2015 Jul-Aug.
[Is] ISSN:1759-0914
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A short-term exposure to moderately intense physical exercise affords a novel measure of protection against autoimmune-mediated peripheral nerve injury. Here, we investigated the mechanism by which forced exercise attenuates the development and progression of experimental autoimmune neuritis (EAN), an established animal model of Guillain-Barré syndrome. Adult male Lewis rats remained sedentary (control) or were preconditioned with forced exercise (1.2 km/day × 3 weeks) prior to P2-antigen induction of EAN. Sedentary rats developed a monophasic course of EAN beginning on postimmunization day 12.3 ± 0.2 and reaching peak severity on day 17.0 ± 0.3 (N = 12). By comparison, forced-exercise preconditioned rats exhibited a similar monophasic course but with significant (p < .05) reduction of disease severity. Analysis of popliteal lymph nodes revealed a protective effect of exercise preconditioning on leukocyte composition and egress. Compared with sedentary controls, forced exercise preconditioning promoted a sustained twofold retention of P2-antigen responsive leukocytes. The percentage distribution of pro-inflammatory (Th1) lymphocytes retained in the nodes from sedentary EAN rats (5.1 ± 0.9%) was significantly greater than that present in nodes from forced-exercise preconditioned EAN rats (2.9 ± 0.6%) or from adjuvant controls (2.0 ± 0.3%). In contrast, the percentage of anti-inflammatory (Th2) lymphocytes (7-10%) and that of cytotoxic T lymphocytes (∼20%) remained unaltered by forced exercise preconditioning. These data do not support an exercise-inducible shift in Th1:Th2 cell bias. Rather, preconditioning with forced exercise elicits a sustained attenuation of EAN severity, in part, by altering the composition and egress of autoreactive proinflammatory (Th1) lymphocytes from draining lymph nodes.
[Mh] Termos MeSH primário: Linfonodos/patologia
Neurite Autoimune Experimental/patologia
Neurite Autoimune Experimental/prevenção & controle
Condicionamento Físico Animal/métodos
Células Th1/fisiologia
[Mh] Termos MeSH secundário: Análise de Variância
Animais
Antígenos CD/metabolismo
Citocinas
Modelos Animais de Doenças
Citometria de Fluxo
Leucócitos/patologia
Masculino
Proteína P2 de Mielina/química
Proteína P2 de Mielina/toxicidade
Neurite Autoimune Experimental/induzido quimicamente
Ratos
Ratos Endogâmicos Lew
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Cytokines); 0 (Myelin P2 Protein)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150719
[St] Status:MEDLINE


  6 / 693 MEDLINE  
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[PMID]:26068118
[Au] Autor:Laulumaa S; Nieminen T; Lehtimäki M; Aggarwal S; Simons M; Koza MM; Vattulainen I; Kursula P; Natali F
[Ad] Endereço:Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Oulu, Finland; German Electron Synchrotron (DESY), Hamburg, Germany; European Spallation Source (ESS), Lund, Sweden.
[Ti] Título:Dynamics of the Peripheral Membrane Protein P2 from Human Myelin Measured by Neutron Scattering--A Comparison between Wild-Type Protein and a Hinge Mutant.
[So] Source:PLoS One;10(6):e0128954, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Myelin protein P2 is a fatty acid-binding structural component of the myelin sheath in the peripheral nervous system, and its function is related to its membrane binding capacity. Here, the link between P2 protein dynamics and structure and function was studied using elastic incoherent neutron scattering (EINS). The P38G mutation, at the hinge between the ß barrel and the α-helical lid, increased the lipid stacking capacity of human P2 in vitro, and the mutated protein was also functional in cultured cells. The P38G mutation did not change the overall structure of the protein. For a deeper insight into P2 structure-function relationships, information on protein dynamics in the 10 ps to 1 ns time scale was obtained using EINS. Values of mean square displacements mainly from protein H atoms were extracted for wild-type P2 and the P38G mutant and compared. Our results show that at physiological temperatures, the P38G mutant is more dynamic than the wild-type P2 protein, especially on a slow 1-ns time scale. Molecular dynamics simulations confirmed the enhanced dynamics of the mutant variant, especially within the portal region in the presence of bound fatty acid. The increased softness of the hinge mutant of human myelin P2 protein is likely related to an enhanced flexibility of the portal region of this fatty acid-binding protein, as well as to its interactions with the lipid bilayer surface requiring conformational adaptations.
[Mh] Termos MeSH primário: Proteína P2 de Mielina/química
[Mh] Termos MeSH secundário: Dicroísmo Circular
Cristalografia por Raios X
Seres Humanos
Bicamadas Lipídicas/química
Bicamadas Lipídicas/metabolismo
Simulação de Dinâmica Molecular
Mutagênese Sítio-Dirigida
Proteína P2 de Mielina/genética
Proteína P2 de Mielina/metabolismo
Difração de Nêutrons
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Espalhamento de Radiação
Temperatura Ambiente
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Lipid Bilayers); 0 (Myelin P2 Protein); 0 (Recombinant Proteins)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150613
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0128954


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[PMID]:25546800
[Au] Autor:Klehmet J; Meisel C; Meisel A
[Ad] Endereço:Department of Neurology, University Hospital Charité, Berlin, Germany.
[Ti] Título:Efficiency of long-term treatment with intravenous immunoglobulins correlates with reduced autoreactive T cell responses in chronic inflammatory demyelinating polyneuropathy patients.
[So] Source:Clin Exp Immunol;178 Suppl 1:149-50, 2014 Dec.
[Is] ISSN:1365-2249
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Linfócitos T CD4-Positivos/imunologia
Linfócitos T CD8-Positivos/imunologia
Imunoglobulinas Intravenosas/administração & dosagem
Imunoglobulinas Intravenosas/imunologia
Polirradiculoneuropatia Desmielinizante Inflamatória Crônica/imunologia
Polirradiculoneuropatia Desmielinizante Inflamatória Crônica/terapia
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
Seres Humanos
Interferon gama/imunologia
Monócitos/imunologia
Proteína P2 de Mielina/imunologia
Proteínas da Mielina/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Immunoglobulins, Intravenous); 0 (Myelin P2 Protein); 0 (Myelin Proteins); 0 (PMP22 protein, human); 82115-62-6 (Interferon-gamma)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:151201
[Lr] Data última revisão:
151201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141230
[St] Status:MEDLINE
[do] DOI:10.1111/cei.12549


  8 / 693 MEDLINE  
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[PMID]:24849898
[Au] Autor:Zenker J; Stettner M; Ruskamo S; Domènech-Estévez E; Baloui H; Médard JJ; Verheijen MH; Brouwers JF; Kursula P; Kieseier BC; Chrast R
[Ad] Endereço:Department of Medical Genetics, University of Lausanne, Switzerland; Graduate Program in Neurosciences, University of Lausanne, Switzerland.
[Ti] Título:A role of peripheral myelin protein 2 in lipid homeostasis of myelinating Schwann cells.
[So] Source:Glia;62(9):1502-12, 2014 Sep.
[Is] ISSN:1098-1136
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Peripheral myelin protein 2 (Pmp2, P2 or Fabp8), a member of the fatty acid binding protein family, was originally described together with myelin basic protein (Mbp or P1) and myelin protein zero (Mpz or P0) as one of the most abundant myelin proteins in the peripheral nervous system (PNS). Although Pmp2 is predominantly expressed in myelinated Schwann cells, its role in glia is currently unknown. To study its function in PNS biology, we have generated a complete Pmp2 knockout mouse (Pmp2(-/-) ). Comprehensive characterization of Pmp2(-/-) mice revealed a temporary reduction in their motor nerve conduction velocity (MNCV). While this change was not accompanied by any defects in general myelin structure, we detected transitory alterations in the myelin lipid profile of Pmp2(-/-) mice. It was previously proposed that Pmp2 and Mbp have comparable functions in the PNS suggesting that the presence of Mbp can partially mask the Pmp2(-/-) phenotype. Indeed, we found that Mbp lacking Shi(-/-) mice, similar to Pmp2(-/-) animals, have preserved myelin structure and reduced MNCV, but this phenotype was not aggravated in Pmp2(-/-) /Shi(-/-) mutants indicating that Pmp2 and Mbp do not substitute each other's functions in the PNS. These data, together with our observation that Pmp2 binds and transports fatty acids to membranes, uncover a role for Pmp2 in lipid homeostasis of myelinating Schwann cells.
[Mh] Termos MeSH primário: Proteína P2 de Mielina/metabolismo
Células de Schwann/metabolismo
[Mh] Termos MeSH secundário: Animais
Membrana Celular/metabolismo
Ácidos Graxos/metabolismo
Homeostase/fisiologia
Camundongos Endogâmicos C3H
Camundongos Endogâmicos C57BL
Camundongos Knockout
Proteína Básica da Mielina/genética
Proteína Básica da Mielina/metabolismo
Proteína P2 de Mielina/genética
Bainha de Mielina/metabolismo
Bainha de Mielina/patologia
Condução Nervosa
Fenótipo
RNA Mensageiro/metabolismo
Nervo Isquiático/patologia
Nervo Isquiático/fisiopatologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Mbp protein, mouse); 0 (Myelin Basic Protein); 0 (Myelin P2 Protein); 0 (Pmp2 protein, mouse); 0 (RNA, Messenger)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:140721
[Lr] Data última revisão:
140721
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140523
[St] Status:MEDLINE
[do] DOI:10.1002/glia.22696


  9 / 693 MEDLINE  
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[PMID]:24419389
[Au] Autor:Ruskamo S; Yadav RP; Sharma S; Lehtimäki M; Laulumaa S; Aggarwal S; Simons M; Bürck J; Ulrich AS; Juffer AH; Kursula I; Kursula P
[Ad] Endereço:Department of Biochemistry, University of Oulu, Oulu, Finland.
[Ti] Título:Atomic resolution view into the structure-function relationships of the human myelin peripheral membrane protein P2.
[So] Source:Acta Crystallogr D Biol Crystallogr;70(Pt 1):165-76, 2014 Jan.
[Is] ISSN:1399-0047
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:P2 is a fatty acid-binding protein expressed in vertebrate peripheral nerve myelin, where it may function in bilayer stacking and lipid transport. P2 binds to phospholipid membranes through its positively charged surface and a hydrophobic tip, and accommodates fatty acids inside its barrel structure. The structure of human P2 refined at the ultrahigh resolution of 0.93 Šallows detailed structural analyses, including the full organization of an internal hydrogen-bonding network. The orientation of the bound fatty-acid carboxyl group is linked to the protonation states of two coordinating arginine residues. An anion-binding site in the portal region is suggested to be relevant for membrane interactions and conformational changes. When bound to membrane multilayers, P2 has a preferred orientation and is stabilized, and the repeat distance indicates a single layer of P2 between membranes. Simulations show the formation of a double bilayer in the presence of P2, and in cultured cells wild-type P2 induces membrane-domain formation. Here, the most accurate structural and functional view to date on P2, a major component of peripheral nerve myelin, is presented, showing how it can interact with two membranes simultaneously while going through conformational changes at its portal region enabling ligand transfer.
[Mh] Termos MeSH primário: Proteína P2 de Mielina/química
Proteína P2 de Mielina/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Linhagem Celular
Membrana Celular/metabolismo
Seres Humanos
Modelos Moleculares
Dados de Sequência Molecular
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Myelin P2 Protein)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140115
[St] Status:MEDLINE
[do] DOI:10.1107/S1399004713027910


  10 / 693 MEDLINE  
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[PMID]:24150643
[Au] Autor:Islamov RR; Lannik NI; Shaimardanova GF; Rezvyakov PN; Tyapkina OV; Rizvanov AA; Chelyshev YA; Kozlovskaya IB; Nikolskii EE
[Ad] Endereço:Kazan State Medical University, ul. Butlerova 49, Kazan, 420012, Tatarstan, Russia.
[Ti] Título:Effect of hindlimb unloading on myelinated fibers in the mouse lumbar spinal cord.
[So] Source:Dokl Biol Sci;452:266-8, 2013 Sep.
[Is] ISSN:1608-3105
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Membro Posterior/inervação
Fibras Nervosas Mielinizadas/metabolismo
Medula Espinal/metabolismo
[Mh] Termos MeSH secundário: Animais
Elevação dos Membros Posteriores
Região Lombossacral/fisiologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Proteína P2 de Mielina/genética
Proteína P2 de Mielina/metabolismo
Proteínas da Mielina/genética
Proteínas da Mielina/metabolismo
Fibras Nervosas Mielinizadas/fisiologia
Fibras Nervosas Mielinizadas/ultraestrutura
Medula Espinal/fisiologia
Medula Espinal/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Myelin P2 Protein); 0 (Myelin Proteins); 0 (Pmp2 protein, mouse); 0 (Pmp22 protein, mouse)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131024
[St] Status:MEDLINE
[do] DOI:10.1134/S0012496613050086



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