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1.
Mult Scler ; 26(4): 505-508, 2020 04.
Artigo em Inglês | MEDLINE | ID: mdl-30657002

RESUMO

BACKGROUND: The Arm Function in Multiple Sclerosis Questionnaire (AMSQ) has been developed to assess upper extremity function of patients with multiple sclerosis (MS). A minimal clinically important difference (MCID) value has not been determined yet. OBJECTIVE: The objective of this study is to determine an MCID for AMSQ. METHODS: We used the sensitivity- and specificity-based approach with dichotomized global perceived effect as an anchor. RESULTS: The receiver operating characteristic (ROC) curve yielded an optimal threshold value of 14.5 (sensitivity 0.68 and specificity 0.79). The area under the ROC curve value was 0.77. CONCLUSION: We identified an MCID of 15 points for the AMSQ (range 31-186).


Assuntos
Braço/fisiopatologia , Diferença Mínima Clinicamente Importante , Esclerose Múltipla/tratamento farmacológico , Medidas de Resultados Relatados pelo Paciente , Bloqueadores dos Canais de Potássio/farmacologia , Psicometria/normas , 4-Aminopiridina/farmacologia , Adulto , Feminino , Seguimentos , Humanos , Masculino , Pessoa de Meia-Idade , Esclerose Múltipla/fisiopatologia , Psicometria/instrumentação , Sensibilidade e Especificidade
2.
Biochim Biophys Acta ; 1833(6): 1421-33, 2013 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-23454728

RESUMO

RTN1A is a reticulon protein with predominant localization in the endoplasmic reticulum (ER). It was previously shown that RTN1A is expressed in neurons of the mammalian central nervous system but functional information remains sparse. To elucidate the neuronal function of RTN1A, we chose to focus our investigation on identifying possible novel binding partners specifically interacting with the unique N-terminus of RTN1A. Using a nonbiased approach involving GST pull-downs and MS analysis, we identified the intracellular calcium release channel ryanodine receptor 2 (RyR2) as a direct binding partner of RTN1A. The RyR2 binding site was localized to a highly conserved 150-amino acid residue region. RTN1A displays high preference for RyR2 binding in vitro and in vivo and both proteins colocalize in hippocampal neurons and Purkinje cells. Moreover, we demonstrate the precise subcellular localization of RTN1A in Purkinje cells and show that RTN1A inhibits RyR channels in [(3)H]ryanodine binding studies on brain synaptosomes. In a functional assay, RTN1A significantly reduced RyR2-mediated Ca(2+) oscillations. Thus, RTN1A and RyR2 might act as functional partners in the regulation of cytosolic Ca(2+) dynamics the in neurons.


Assuntos
Cálcio/metabolismo , Hipocampo/metabolismo , Proteínas do Tecido Nervoso/metabolismo , Neurônios/metabolismo , Canal de Liberação de Cálcio do Receptor de Rianodina/metabolismo , Animais , Sítios de Ligação , Western Blotting , Células Cultivadas , Citosol/metabolismo , Hipocampo/citologia , Humanos , Técnicas Imunoenzimáticas , Imunoprecipitação , Masculino , Camundongos , Neurônios/citologia , Ligação Proteica , Ratos , Ratos Sprague-Dawley , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Rianodina/metabolismo , Espectrometria de Massas em Tandem
3.
Proteomics ; 7(8): 1249-60, 2007 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-17366474

RESUMO

A 2-D reference map in pI range 3-10 was constructed for the soluble protein fraction of Phanerochaete chrysosporium growing vegetatively under standard conditions. Functional annotation could be made for 517 spots out of 720 that were subjected to MALDI-TOF-MS analysis, according to the specific accession numbers from the P. chrysosporium genomic database. Further analysis of the data revealed 314 distinct ORFs, 118 of which yielded multiple spots on the master gel. Functional classification of the proteins was made according to the eukaryote orthologous groups defined in the organism's genome website. The functional class of PTMs, protein turnover and chaperones was represented with the highest number (63) of the identified ORFs. Six proteins were assigned to the hypothetical proteins and 29 were predicted to have a signal peptide sequence. Subcellular localization predictions were also made for the identified proteins. Of the protein spots detected on the master gel, 380 were found to be probably phosphorylated and 96 of these matched to the identified proteins. The reference map was efficiently used in the identification of the proteins differentially expressed under cadmium and copper stress. Three new ribosomal proteins as well as zinc-containing alcohol dehydrogenase, glucose-6-phosphate isomerase, flavonol/cinnamoyl-CoA reductase, H+-transporting two-sector ATPase, ribosomal protein S7, ribosomal protein S21e, elongation factor EF-1 alpha subunit were demonstrated as the most strongly induced.


Assuntos
Proteínas Fúngicas/análise , Phanerochaete/química , Proteoma/análise , Cádmio/metabolismo , Cobre/metabolismo , Eletroforese em Gel Bidimensional , Proteínas Fúngicas/classificação , Proteínas Fúngicas/genética , Proteínas Fúngicas/metabolismo , Dados de Sequência Molecular , Phanerochaete/genética , Phanerochaete/metabolismo , Sinais Direcionadores de Proteínas , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
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