<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Manta, Panagiota</style></author><author><style face="normal" font="default" size="100%">Terzis, Gerasimos</style></author><author><style face="normal" font="default" size="100%">Papadimitriou, Constantinos</style></author><author><style face="normal" font="default" size="100%">Kontou, Chrysanthi</style></author><author><style face="normal" font="default" size="100%">Vassilopoulos, Demetris</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Emerin expression in tubular aggregates.</style></title><secondary-title><style face="normal" font="default" size="100%">Acta Neuropathol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Acta Neuropathol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adult</style></keyword><keyword><style  face="normal" font="default" size="100%">AMP Deaminase</style></keyword><keyword><style  face="normal" font="default" size="100%">Calcium-Transporting ATPases</style></keyword><keyword><style  face="normal" font="default" size="100%">Cyclooxygenase 2</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydro-Lyases</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunohistochemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Isoenzymes</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Microscopy, Electron</style></keyword><keyword><style  face="normal" font="default" size="100%">Middle Aged</style></keyword><keyword><style  face="normal" font="default" size="100%">Muscle, Skeletal</style></keyword><keyword><style  face="normal" font="default" size="100%">Muscular Dystrophy, Emery-Dreifuss</style></keyword><keyword><style  face="normal" font="default" size="100%">Myopathies, Structural, Congenital</style></keyword><keyword><style  face="normal" font="default" size="100%">NAD</style></keyword><keyword><style  face="normal" font="default" size="100%">Nuclear Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Phosphopyruvate Hydratase</style></keyword><keyword><style  face="normal" font="default" size="100%">Prostaglandin-Endoperoxide Synthases</style></keyword><keyword><style  face="normal" font="default" size="100%">Sarcoplasmic Reticulum Calcium-Transporting ATPases</style></keyword><keyword><style  face="normal" font="default" size="100%">Thymopoietins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2004</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2004 Jun</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">107</style></volume><pages><style face="normal" font="default" size="100%">546-52</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Emerin is an inner nuclear membrane protein that is mutated or not expressed in patients with X-linked Emery-Dreifuss muscular dystrophy (X-EDMD/EMD). Cytoplasmic localization of emerin in cultured cells or tissues has been reported, although this remains a controversial issue. Tubular aggregates (TAs) are pathological structures seen in the sarcoplasm of human skeletal muscle fibers in various disorders. The TAs derive from the sarcoplasmic reticulum (SR) and represent, probably, an adaptive response of the SR to various insults to the muscle fibers. In the present study, we present immunohistochemical evidence of emerin expression in TAs. Muscle biopsies with tubular aggregates from four male, unrelated patients were studied. The percentage of muscle fibers containing TAs varied between 5 and 20%. Routine histochemistry revealed intense reaction of TAs with NADH-TR, AMPDA, and NSE, but not with COX, SDH, myosin ATPase (pH 9.4, 4.3, 4.6), PAS, and Oil red O staining. Immunohistochemical study revealed strong immunostaining of TAs with antibodies against emerin and 7 SERCA2-ATPase. Immunostaining of TAs was also seen with antibodies against heat shock protein and dysferlin, but not with antibodies to lamin A, dystrophin, adhalin, beta, gamma, delta sarcoglycans, and merosin. These results suggest that emerin, an inner nuclear membrane protein, is present at the TAs. The interpretation and significance of this finding is discussed in relation to experimental data suggesting that normal emerin localization at the inner nuclear membrane depends on lamin A and mutations in the N-terminal domain of emerin cause mislocalization of the protein to the sarcoplasmic membranes.</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/15085358?dopt=Abstract</style></custom1></record></records></xml>