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Journal articles on the topic 'Utrophin'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Marshall, Jamie L., Johan Holmberg, Eric Chou, Amber C. Ocampo, Jennifer Oh, Joy Lee, Angela K. Peter, Paul T. Martin, and Rachelle H. Crosbie-Watson. "Sarcospan-dependent Akt activation is required for utrophin expression and muscle regeneration." Journal of Cell Biology 197, no. 7 (June 25, 2012): 1009–27. http://dx.doi.org/10.1083/jcb.201110032.

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Utrophin is normally confined to the neuromuscular junction (NMJ) in adult muscle and partially compensates for the loss of dystrophin in mdx mice. We show that Akt signaling and utrophin levels were diminished in sarcospan (SSPN)-deficient muscle. By creating several transgenic and knockout mice, we demonstrate that SSPN regulates Akt signaling to control utrophin expression. SSPN determined α-dystroglycan (α-DG) glycosylation by affecting levels of the NMJ-specific glycosyltransferase Galgt2. After cardiotoxin (CTX) injury, regenerating myofibers express utrophin and Galgt2-modified α-DG aro

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2

Perkins, Kelly J., Utpal Basu, Murat T. Budak, Caroline Ketterer, Santhosh M. Baby, Olga Lozynska, John A. Lunde, Bernard J. Jasmin, Neal A. Rubinstein, and Tejvir S. Khurana. "Ets-2 Repressor Factor Silences Extrasynaptic Utrophin by N-Box–mediated Repression in Skeletal Muscle." Molecular Biology of the Cell 18, no. 8 (August 2007): 2864–72. http://dx.doi.org/10.1091/mbc.e06-12-1069.

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Utrophin is the autosomal homologue of dystrophin, the protein product of the Duchenne's muscular dystrophy (DMD) locus. Utrophin expression is temporally and spatially regulated being developmentally down-regulated perinatally and enriched at neuromuscular junctions (NMJs) in adult muscle. Synaptic localization of utrophin occurs in part by heregulin-mediated extracellular signal-regulated kinase (ERK)-phosphorylation, leading to binding of GABPα/β to the N-box/EBS and activation of the major utrophin promoter-A expressed in myofibers. However, molecular mechanisms contributing to concurrent

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3

Moorwood, Catherine, Neha Soni, Gopal Patel, Steve D. Wilton, and Tejvir S. Khurana. "A Cell-Based High-Throughput Screening Assay for Posttranscriptional Utrophin Upregulation." Journal of Biomolecular Screening 18, no. 4 (October 30, 2012): 400–406. http://dx.doi.org/10.1177/1087057112465648.

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Duchenne muscular dystrophy (DMD) is a devastating muscle-wasting disease caused by mutations in the dystrophin gene. Utrophin is a homologue of dystrophin that can compensate for its absence when overexpressed in DMD animal models. Utrophin upregulation is therefore a promising therapeutic approach for DMD. Utrophin is regulated at both transcriptional and posttranscriptional levels. Transcriptional regulation has been studied extensively, and assays have been described for the identification of utrophin promoter-targeting molecules. However, despite the profound impact that posttranscription

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4

Fabbrizio, E., J. Latouche, F. Rivier, G. Hugon, and D. Mornet. "Re-evaluation of the distributions of dystrophin and utrophin in sciatic nerve." Biochemical Journal 312, no. 1 (November 15, 1995): 309–14. http://dx.doi.org/10.1042/bj3120309.

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Differential expression of proteins belonging to the dystrophin family was analysed in peripheral nerves. In agreement with previous reports, no full-size dystrophin was detectable, only Dp116, one of the short dystrophin products of the Duchenne muscular dystrophy (DMD) gene. We used specific monoclonal antibodies to fully investigate the presence of utrophin, a dystrophin homologue encoded by a gene located on chromosome 6q24. Evidence is presented here of the presence of two potential isoforms of full-length utrophin in different nerve structures, which may differ by alternative splicing of

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5

Khurana, Tejvir S., Alan G. Rosmarin, Jing Shang, Thomas O. B. Krag, Saumya Das та Steen Gammeltoft. "Activation of Utrophin Promoter by Heregulin via theets-related Transcription Factor Complex GA-binding Protein α/β". Molecular Biology of the Cell 10, № 6 (червень 1999): 2075–86. http://dx.doi.org/10.1091/mbc.10.6.2075.

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Utrophin/dystrophin-related protein is the autosomal homologue of the chromosome X-encoded dystrophin protein. In adult skeletal muscle, utrophin is highly enriched at the neuromuscular junction. However, the molecular mechanisms underlying regulation of utrophin gene expression are yet to be defined. Here we demonstrate that the growth factor heregulin increases de novo utrophin transcription in muscle cell cultures. Using mutant reporter constructs of the utrophin promoter, we define the N-box region of the promoter as critical for heregulin-mediated activation. Using this region of the utro

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6

MORRIS, Glenn E., Nguyen thi MAN, Nguyen thi Ngoc HUYEN, Alexander PEREBOEV, John KENDRICK-JONES, and Steven J. WINDER. "Disruption of the utrophin–actin interaction by monoclonal antibodies and prediction of an actin-binding surface of utrophin." Biochemical Journal 337, no. 1 (December 17, 1998): 119–23. http://dx.doi.org/10.1042/bj3370119.

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Monoclonal antibody (mAb) binding sites in the N-terminal actin-binding domain of utrophin have been identified using phage-displayed peptide libraries, and the mAbs have been used to probe functional regions of utrophin involved in actin binding. mAbs were characterized for their ability to interact with the utrophin actin-binding domain and to affect actin binding to utrophin in sedimentation assays. One of these antibodies was able to inhibit utrophin–F-actin binding and was shown to recognize a predicted helical region at residues 13–22 of utrophin, close to a previously predicted actin-bi

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7

James, M., A. Nuttall, J. L. Ilsley, K. Ottersbach, J. M. Tinsley, M. Sudol, and S. J. Winder. "Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin." Journal of Cell Science 113, no. 10 (May 15, 2000): 1717–26. http://dx.doi.org/10.1242/jcs.113.10.1717.

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Many cell adhesion-dependent processes are regulated by tyrosine phosphorylation. In order to investigate the role of tyrosine phosphorylation of the utrophin-dystroglycan complex we treated suspended or adherent cultures of HeLa cells with peroxyvanadate and immunoprecipitated (beta)-dystroglycan and utrophin from cell extracts. Western blotting of (β)-dystroglycan and utrophin revealed adhesion- and peroxyvanadate-dependent mobility shifts which were recognised by anti-phospho-tyrosine antibodies. Using maltose binding protein fusion constructs to the carboxy-terminal domains of utrophin we

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8

Winder, S. J., L. Hemmings, S. K. Maciver, S. J. Bolton, J. M. Tinsley, K. E. Davies, D. R. Critchley, and J. Kendrick-Jones. "Utrophin actin binding domain: analysis of actin binding and cellular targeting." Journal of Cell Science 108, no. 1 (January 1, 1995): 63–71. http://dx.doi.org/10.1242/jcs.108.1.63.

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Utrophin, or dystrophin-related protein, is an autosomal homologue of dystrophin. The protein is apparently ubiquitously expressed and in muscle tissues the expression is developmentally regulated. Since utrophin has a similar domain structure to dystrophin it has been suggested that it could substitute for dystrophin in dystrophic muscle. Like dystrophin, utrophin has been shown to be associated with a membrane-bound glycoprotein complex. Here we demonstrate that expressed regions of the predicted actin binding domain in the NH2 terminus of utrophin are able to bind to F-actin in vitro, but d

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9

Dubowitz, Victor. "Utrophin euphoria." Neuromuscular Disorders 7, no. 1 (January 1997): 5–6. http://dx.doi.org/10.1016/s0960-8966(96)00432-4.

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10

Gramolini, Anthony O., Guy Bélanger, and Bernard J. Jasmin. "Distinct regions in the 3′ untranslated region are responsible for targeting and stabilizing utrophin transcripts in skeletal muscle cells." Journal of Cell Biology 154, no. 6 (September 10, 2001): 1173–84. http://dx.doi.org/10.1083/jcb.200101108.

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In this study, we have sought to determine whether utrophin transcripts are targeted to a distinct subcellular compartment in skeletal muscle cells, and have examined the role of the 3′ untranslated region (UTR) in regulating the stability and localization of utrophin transcripts. Our results show that utrophin transcripts associate preferentially with cytoskeleton-bound polysomes via actin microfilaments. Because this association is not evident in myoblasts, our findings also indicate that the localization of utrophin transcripts with cytoskeleton-bound polysomes is under developmental influe

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11

Guiraud, Simon, Benjamin Edwards, Arran Babbs, Sarah E. Squire, Adam Berg, Lee Moir, Matthew J. Wood, and Kay E. Davies. "The potential of utrophin and dystrophin combination therapies for Duchenne muscular dystrophy." Human Molecular Genetics 28, no. 13 (March 5, 2019): 2189–200. http://dx.doi.org/10.1093/hmg/ddz049.

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Abstract Duchenne muscular dystrophy (DMD) is a lethal neuromuscular disorder caused by loss of dystrophin. Several therapeutic modalities are currently in clinical trials but none will achieve maximum functional rescue and full disease correction. Therefore, we explored the potential of combining the benefits of dystrophin with increases of utrophin, an autosomal paralogue of dystrophin. Utrophin and dystrophin can be co-expressed and co-localized at the same muscle membrane. Wild-type (wt) levels of dystrophin are not significantly affected by a moderate increase of utrophin whereas higher l

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12

Gramolini, Anthony O., Guy Bélanger, Jennifer M. Thompson, Joe V. Chakkalakal, and Bernard J. Jasmin. "Increased expression of utrophin in a slow vs. a fast muscle involves posttranscriptional events." American Journal of Physiology-Cell Physiology 281, no. 4 (October 1, 2001): C1300—C1309. http://dx.doi.org/10.1152/ajpcell.2001.281.4.c1300.

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In addition to showing differences in the levels of contractile proteins and metabolic enzymes, fast and slow muscles also differ in their expression profile of structural and synaptic proteins. Because utrophin is a structural protein expressed at the neuromuscular junction, we hypothesize that its expression may be different between fast and slow muscles. Western blots showed that, compared with fast extensor digitorum longus (EDL) muscles, slow soleus muscles contain significantly more utrophin. Quantitative RT-PCR revealed that this difference is accompanied by a parallel increase in the e

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13

Bonet-Kerrache, Armelle, Mathieu Fortier, Franck Comunale, and Cécile Gauthier-Rouvière. "The GTPase RhoA increases utrophin expression and stability, as well as its localization at the plasma membrane." Biochemical Journal 391, no. 2 (October 10, 2005): 261–68. http://dx.doi.org/10.1042/bj20050024.

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The Rho family of small GTPases are signalling molecules involved in cytoskeleton remodelling and gene transcription. Their activities are important for many cellular processes, including myogenesis. In particular, RhoA positively regulates skeletal-muscle differentiation. We report in the present study that the active form of RhoA increases the expression of utrophin, the autosomal homologue of dystrophin in the mouse C2C12 and rat L8 myoblastic cell lines. Even though this RhoA-dependent utrophin increase is higher in proliferating myoblasts, it is maintained during myogenic differentiation.

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14

Deconinck, Anne E., Allyson C. Potter, Jonathon M. Tinsley, Sarah J. Wood, Ruth Vater, Carol Young, Laurent Metzinger, Angela Vincent, Clarke R. Slater, and Kay E. Davies. "Postsynaptic Abnormalities at the Neuromuscular Junctions of Utrophin-deficient Mice." Journal of Cell Biology 136, no. 4 (February 24, 1997): 883–94. http://dx.doi.org/10.1083/jcb.136.4.883.

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Utrophin is a dystrophin-related cytoskeletal protein expressed in many tissues. It is thought to link F-actin in the internal cytoskeleton to a transmembrane protein complex similar to the dystrophin protein complex (DPC). At the adult neuromuscular junction (NMJ), utrophin is precisely colocalized with acetylcholine receptors (AChRs) and recent studies have suggested a role for utrophin in AChR cluster formation or maintenance during NMJ differentiation. We have disrupted utrophin expression by gene targeting in the mouse. Such mice have no utrophin detectable by Western blotting or immunocy

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15

Rybakova, Inna N., Jitandrakumar R. Patel, Kay E. Davies, Peter D. Yurchenco, and James M. Ervasti. "Utrophin Binds Laterally along Actin Filaments and Can Couple Costameric Actin with Sarcolemma When Overexpressed in Dystrophin-deficient Muscle." Molecular Biology of the Cell 13, no. 5 (May 2002): 1512–21. http://dx.doi.org/10.1091/mbc.01-09-0446.

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Dystrophin is widely thought to mechanically link the cortical cytoskeleton with the muscle sarcolemma. Although the dystrophin homolog utrophin can functionally compensate for dystrophin in mice, recent studies question whether utrophin can bind laterally along actin filaments and anchor filaments to the sarcolemma. Herein, we have expressed full-length recombinant utrophin and show that the purified protein is fully soluble with a native molecular weight and molecular dimensions indicative of monomers. We demonstrate that like dystrophin, utrophin can form an extensive lateral association wi

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16

Yamane, Akira, Satonari Akutsu, Thomas G. H. Diekwisch, and Ryoichi Matsuda. "Satellite cells and utrophin are not directly correlated with the degree of skeletal muscle damage in mdx mice." American Journal of Physiology-Cell Physiology 289, no. 1 (July 2005): C42—C48. http://dx.doi.org/10.1152/ajpcell.00577.2004.

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To determine whether muscle satellite cells and utrophin are correlated with the degree of damage in mdx skeletal muscles, we measured the area of the degenerative region as an indicator of myofiber degeneration in the masseter, gastrocnemius, soleus, and diaphragm muscles of mdx mice. Furthermore, we analyzed the expression levels of the paired box homeotic gene 7 ( pax7), m-cadherin (the makers of muscle satellite cells), and utrophin mRNA. We also investigated the immunolocalization of m-cadherin and utrophin proteins in the muscles of normal C57BL/10J (B10) and mdx mice. The expression lev

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17

Angus, Lindsay M., Joe V. Chakkalakal, Alexandre Méjat, Joe K. Eibl, Guy Bélanger, Lynn A. Megeney, Eva R. Chin, Laurent Schaeffer, Robin N. Michel та Bernard J. Jasmin. "Calcineurin-NFAT signaling, together with GABP and peroxisome PGC-1α, drives utrophin gene expression at the neuromuscular junction". American Journal of Physiology-Cell Physiology 289, № 4 (жовтень 2005): C908—C917. http://dx.doi.org/10.1152/ajpcell.00196.2005.

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We examined whether calcineurin-NFAT (nuclear factors of activated T cells) signaling plays a role in specifically directing the expression of utrophin in the synaptic compartment of muscle fibers. Immunofluorescence experiments revealed the accumulation of components of the calcineurin-NFAT signaling cascade within the postsynaptic membrane domain of the neuromuscular junction. RT-PCR analysis using synaptic vs. extrasynaptic regions of muscle fibers confirmed these findings by showing an accumulation of calcineurin transcripts within the synaptic compartment. We also examined the effect of c

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18

Grady, R. Mark, John P. Merlie, and Joshua R. Sanes. "Subtle Neuromuscular Defects in Utrophin-deficient Mice." Journal of Cell Biology 136, no. 4 (February 24, 1997): 871–82. http://dx.doi.org/10.1083/jcb.136.4.871.

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Utrophin is a large cytoskeletal protein that is homologous to dystrophin, the protein mutated in Duchenne and Becker muscular dystrophy. In skeletal muscle, dystrophin is broadly distributed along the sarcolemma whereas utrophin is concentrated at the neuromuscular junction. This differential localization, along with studies on cultured cells, led to the suggestion that utrophin is required for synaptic differentiation. In addition, utrophin is present in numerous nonmuscle cells, suggesting that it may have a more generalized role in the maintenance of cellular integrity. To test these hypot

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19

Wells, William A. "Sticky utrophin messages." Journal of Cell Biology 154, no. 6 (September 10, 2001): 1098. http://dx.doi.org/10.1083/jcb1546iti4.

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20

Fulmer, Tim. "Biglycan meets utrophin." Science-Business eXchange 4, no. 5 (February 2011): 122. http://dx.doi.org/10.1038/scibx.2011.122.

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21

Peters, Matthew F., Hélène M. Sadoulet-Puccio, R. Mark Grady, Neal R. Kramarcy, Louis M. Kunkel, Joshua R. Sanes, Robert Sealock та Stanley C. Froehner. "Differential Membrane Localization and Intermolecular Associations of α-Dystrobrevin Isoforms in Skeletal Muscle". Journal of Cell Biology 142, № 5 (7 вересня 1998): 1269–78. http://dx.doi.org/10.1083/jcb.142.5.1269.

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α-Dystrobrevin is both a dystrophin homologue and a component of the dystrophin protein complex. Alternative splicing yields five forms, of which two predominate in skeletal muscle: full-length α-dystrobrevin-1 (84 kD), and COOH-terminal truncated α-dystrobrevin-2 (65 kD). Using isoform-specific antibodies, we find that α-dystrobrevin-2 is localized on the sarcolemma and at the neuromuscular synapse, where, like dystrophin, it is most concentrated in the depths of the postjunctional folds. α-Dystrobrevin-2 preferentially copurifies with dystrophin from muscle extracts. In contrast, α-dystrobre

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22

Peter, Angela K., Jamie L. Marshall, and Rachelle H. Crosbie. "Sarcospan reduces dystrophic pathology: stabilization of the utrophin–glycoprotein complex." Journal of Cell Biology 183, no. 3 (November 3, 2008): 419–27. http://dx.doi.org/10.1083/jcb.200808027.

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Mutations in the dystrophin gene cause Duchenne muscular dystrophy and result in the loss of dystrophin and the entire dystrophin–glycoprotein complex (DGC) from the sarcolemma. We show that sarcospan (SSPN), a unique tetraspanin-like component of the DGC, ameliorates muscular dystrophy in dystrophin-deficient mdx mice. SSPN stabilizes the sarcolemma by increasing levels of the utrophin–glycoprotein complex (UGC) at the extrasynaptic membrane to compensate for the loss of dystrophin. Utrophin is normally restricted to the neuromuscular junction, where it replaces dystrophin to form a functiona

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23

Onori, Annalisa, Agata Desantis, Serena Buontempo, Maria Grazia Di Certo, Maurizio Fanciulli, Luisa Salvatori, Claudio Passananti, and Nicoletta Corbi. "The artificial 4-zinc-finger protein Bagly binds human utrophin promoter A at the endogenous chromosomal site and activates transcription." Biochemistry and Cell Biology 85, no. 3 (June 2007): 358–65. http://dx.doi.org/10.1139/o07-015.

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Our aim is to upregulate the expression of the dystrophin-related gene utrophin in Duchenne muscular dystrophy, in this way complementing the lack of dystrophin function. To achieve utrophin upregulation, we designed and engineered synthetic zinc-inger based transcription factors. We have previously shown that the artificial 3-zinc-finger protein Jazz, fused with the appropriate effector domain, is able to drive the transcription of a test gene from utrophin promoter A. Here we report a novel artificial 4-zinc-finger protein, Bagly, which binds with optimized affinity–specificity to a 12 bp DN

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24

Porter, J. D., J. A. Rafael, R. J. Ragusa, J. K. Brueckner, J. I. Trickett, and K. E. Davies. "The sparing of extraocular muscle in dystrophinopathy is lost in mice lacking utrophin and dystrophin." Journal of Cell Science 111, no. 13 (July 1, 1998): 1801–11. http://dx.doi.org/10.1242/jcs.111.13.1801.

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The extraocular muscles are one of few skeletal muscles that are structurally and functionally intact in Duchenne muscular dystrophy. Little is known about the mechanisms responsible for differential sparing or targeting of muscle groups in neuromuscular disease. One hypothesis is that constitutive or adaptive properties of the unique extraocular muscle phenotype may underlie their protection in dystrophinopathy. We assessed the status of extraocular muscles in the mdx mouse model of muscular dystrophy. Mice showed mild pathology in accessory extraocular muscles, but no signs of pathology were

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25

Perronnet, Caroline, and Cyrille Vaillend. "Dystrophins, Utrophins, and Associated Scaffolding Complexes: Role in Mammalian Brain and Implications for Therapeutic Strategies." Journal of Biomedicine and Biotechnology 2010 (2010): 1–19. http://dx.doi.org/10.1155/2010/849426.

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Two decades of molecular, cellular, and functional studies considerably increased our understanding of dystrophins function and unveiled the complex etiology of the cognitive deficits in Duchenne muscular dystrophy (DMD), which involves altered expression of several dystrophin-gene products in brain. Dystrophins are normally part of critical cytoskeleton-associated membrane-bound molecular scaffolds involved in the clustering of receptors, ion channels, and signaling proteins that contribute to synapse physiology and blood-brain barrier function. The utrophin gene also drives brain expression

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26

&NA;. "Utrophin in muscular dystrophy." Inpharma Weekly &NA;, no. 1071 (January 1997): 7. http://dx.doi.org/10.2165/00128413-199710710-00015.

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27

Campbell, Kevin P., and Rachelle H. Crosbie. "Utrophin to the rescue." Nature 384, no. 6607 (November 1996): 308–9. http://dx.doi.org/10.1038/384308a0.

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28

Tanihata, Jun, Naoki Suzuki, Yuko Miyagoe-Suzuki, Kazuhiko Imaizumi, and Shin'ichi Takeda. "Downstream utrophin enhancer is required for expression of utrophin in skeletal muscle." Journal of Gene Medicine 10, no. 6 (2008): 702–13. http://dx.doi.org/10.1002/jgm.1190.

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29

EBIHARA, SATORU, GHIABE-HENRI GUIBINGA, RENALD GILBERT, JOSEPHINE NALBANTOGLU, BERNARD MASSIE, GEORGE KARPATI, and BASIL J. PETROF. "Differential effects of dystrophin and utrophin gene transfer in immunocompetent muscular dystrophy (mdx) mice." Physiological Genomics 3, no. 3 (September 8, 2000): 133–44. http://dx.doi.org/10.1152/physiolgenomics.2000.3.3.133.

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Ebihara, Satoru, Ghiabe-Henri Guibinga, Renald Gilbert, Josephine Nalbantoglu, Bernard Massie, George Karpati, and Basil J. Petrof. Differential effects of dystrophin and utrophin gene transfer in immunocompetent muscular dystrophy (mdx) mice. Physiol Genomics 3: 133–144, 2000.—Duchenne muscular dystrophy (DMD) is a fatal disease caused by defects in the gene encoding dystrophin. Dystrophin is a cytoskeletal protein, which together with its associated protein complex, helps to protect the sarcolemma from mechanical stresses associated with muscle contraction. Gene therapy efforts aimed at supp

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Banks, Glen B., Jeffrey S. Chamberlain, and Guy L. Odom. "Microutrophin expression in dystrophic mice displays myofiber type differences in therapeutic effects." PLOS Genetics 16, no. 11 (November 11, 2020): e1009179. http://dx.doi.org/10.1371/journal.pgen.1009179.

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Gene therapy approaches for DMD using recombinant adeno-associated viral (rAAV) vectors to deliver miniaturized (or micro) dystrophin genes to striated muscles have shown significant progress. However, concerns remain about the potential for immune responses against dystrophin in some patients. Utrophin, a developmental paralogue of dystrophin, may provide a viable treatment option. Here we examine the functional capacity of an rAAV-mediated microutrophin (μUtrn) therapy in the mdx4cv mouse model of DMD. We found that rAAV-μUtrn led to improvement in dystrophic histopathology & mostly rest

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Jimenez-Mallebrera, Cecilia, Kay Davies, Wendy Putt, and Yvonne H. Edwards. "A study of short utrophin isoforms in mice deficient for full-length utrophin." Mammalian Genome 14, no. 1 (January 1, 2003): 47–60. http://dx.doi.org/10.1007/s00335-002-3044-z.

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Rafael, Jill A., Jonathon M. Tinsley, Allyson C. Potter, Anne E. Deconinck, and Kay E. Davies. "Skeletal muscle-specific expression of a utrophin transgene rescues utrophin-dystrophin deficient mice." Nature Genetics 19, no. 1 (May 1998): 79–82. http://dx.doi.org/10.1038/ng0598-79.

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33

Dove, Alan W. "Utrophin gets a new look." Journal of Cell Biology 157, no. 2 (April 15, 2002): 194. http://dx.doi.org/10.1083/jcb1572iti5.

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34

Sewry, C. A., K. J. Nowak, J. T. Ehmsen, and K. E. Davies. "A and B utrophin in human muscle and sarcolemmal A-utrophin associated with tumours." Neuromuscular Disorders 15, no. 11 (November 2005): 779–85. http://dx.doi.org/10.1016/j.nmd.2005.08.002.

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Costantini, Jennifer L., Samuel M. S. Cheung, Sen Hou, Hongzhao Li, Sam K. Kung, James B. Johnston, John A. Wilkins, Spencer B. Gibson, and Aaron J. Marshall. "TAPP2 links phosphoinositide 3-kinase signaling to B-cell adhesion through interaction with the cytoskeletal protein utrophin: expression of a novel cell adhesion-promoting complex in B-cell leukemia." Blood 114, no. 21 (November 19, 2009): 4703–12. http://dx.doi.org/10.1182/blood-2009-03-213058.

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Abstract Tandem pleckstrin homology domain proteins (TAPPs) are recruited to the plasma membrane via binding to phosphoinositides produced by phosphoinositide 3-kinases (PI3Ks). Whereas PI3Ks are critical for B-cell activation, the functions of TAPP proteins in B cells are unknown. We have identified 40 potential interaction partners of TAPP2 in B cells, including proteins involved in cytoskeletal rearrangement, signal transduction and endocytic trafficking. The association of TAPP2 with the cytoskeletal proteins utrophin and syntrophin was confirmed by Western blotting. We found that TAPP2, s

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Zuellig, Richard A., Beat C. Bornhauser, Ralf Amstutz, Bruno Constantin, and Marcus C. Schaub. "Tissue Expression and Actin Binding of a Novel N-Terminal Utrophin Isoform." Journal of Biomedicine and Biotechnology 2011 (2011): 1–18. http://dx.doi.org/10.1155/2011/904547.

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Utrophin and dystrophin present two large proteins that link the intracellular actin cytoskeleton to the extracellular matrix via the C-terminal-associated protein complex. Here we describe a novel short N-terminal isoform of utrophin and its protein product in various rat tissues (N-utro, 62 kDa, amino acids 1–539, comprising the actin-binding domain plus the first two spectrin repeats). Using different N-terminal recombinant utrophin fragments, we show that actin binding exhibits pronounced negative cooperativity (affinity constantsK1=∼5×106andK2=∼1×105 M-1) and is Ca2+-insensitive. Expressi

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Nawrotzki, R., N. Y. Loh, M. A. Ruegg, K. E. Davies, and D. J. Blake. "Characterisation of alpha-dystrobrevin in muscle." Journal of Cell Science 111, no. 17 (September 1, 1998): 2595–605. http://dx.doi.org/10.1242/jcs.111.17.2595.

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Dystrophin-related and associated proteins are important for the formation and maintenance of the mammalian neuromuscular junction. Initial studies in the electric organ of Torpedo californica showed that the dystrophin-related protein dystrobrevin (87K) co-purifies with the acetylcholine receptors and other postsynaptic proteins. Dystrobrevin is also a major phosphotyrosine-containing protein in the postsynaptic membrane. Since inhibitors of tyrosine protein phosphorylation block acetylcholine receptor clustering in cultured muscle cells, we examined the role of alpha-dystrobrevin during syna

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Avila-Polo, R., E. Rivas, M. Cabrera-Serrano, P. Carbonell, I. Rojas-Marcos, Y. Morgado, E. Servian, M. Madruga, C. Marquez, and C. Paradas. "Utrophin immunohistochemical expression in neuromuscular disorders." Neuromuscular Disorders 26 (October 2016): S206. http://dx.doi.org/10.1016/j.nmd.2016.06.434.

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Nelson, Roxanne. "Utrophin therapy for Duchenne muscular dystrophy?" Lancet Neurology 3, no. 11 (November 2004): 637. http://dx.doi.org/10.1016/s1474-4422(04)00891-9.

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Belanto, J. J., T. L. Mader, M. D. Eckhoff, D. M. Strandjord, G. B. Banks, M. K. Gardner, D. A. Lowe, and J. M. Ervasti. "Microtubule binding distinguishes dystrophin from utrophin." Proceedings of the National Academy of Sciences 111, no. 15 (March 31, 2014): 5723–28. http://dx.doi.org/10.1073/pnas.1323842111.

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Karpati, George. "Utrophin muscles in on the action." Nature Medicine 3, no. 1 (January 1997): 22–23. http://dx.doi.org/10.1038/nm0197-22.

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Basu, Utpal, Olga Lozynska, Catherine Moorwood, Gopal Patel, Steve D. Wilton, and Tejvir S. Khurana. "Translational Regulation of Utrophin by miRNAs." PLoS ONE 6, no. 12 (December 27, 2011): e29376. http://dx.doi.org/10.1371/journal.pone.0029376.

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Santas, Amy J., Danielle L. Lavery, Chelsea F. Popowski, April Y. Hung, Ryan E. Hunt, Mary K. Richardson, and Kristin M. Braun. "Utrophin Expression is Prevalent in Epidermis." BIOS 81, no. 3 (September 2010): 67–75. http://dx.doi.org/10.1893/011.081.0301.

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Winder, S. J., T. J. Gibson, and J. Kendrick-Jones. "Dystrophin and utrophin: the missing links!" FEBS Letters 369, no. 1 (August 1, 1995): 27–33. http://dx.doi.org/10.1016/0014-5793(95)00398-s.

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Rigoletto, C., A. Prelle, P. Ciscato, M. Moggio, G. Comi, F. Fortunato, and G. Scarlato. "Utrophin expression during human fetal development." International Journal of Developmental Neuroscience 13, no. 6 (October 1995): 585–93. http://dx.doi.org/10.1016/0736-5748(95)00039-j.

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Tinsley, Jonathon M., and Kay E. Davies. "Utrophin: A potential replacement for dystrophin?" Neuromuscular Disorders 3, no. 5-6 (January 1993): 537–39. http://dx.doi.org/10.1016/0960-8966(93)90111-v.

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Winder, Steven J., Lance Hemmings, Sarah J. Bolton, Sutherland K. Maciver, Jon M. Tinsley, Kay E. Davies, David R. Critchley, and John Kendrick-Jones. "Calmodulin regulation of utrophin actin binding." Biochemical Society Transactions 23, no. 3 (August 1, 1995): 397S. http://dx.doi.org/10.1042/bst023397s.

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Ramachandran, Jayalakshmi, Joel S. Schneider, Pierre-Antoine Crassous, Ruifang Zheng, James P. Gonzalez, Lai-Hua Xie, Annie Beuve, Diego Fraidenraich, and R. Daniel Peluffo. "Nitric oxide signalling pathway in Duchenne muscular dystrophy mice: up-regulation of L-arginine transporters." Biochemical Journal 449, no. 1 (December 7, 2012): 133–42. http://dx.doi.org/10.1042/bj20120787.

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DMD (Duchenne muscular dystrophy) is an incurable rapidly worsening neuromuscular degenerative disease caused by the absence of dystrophin. In skeletal muscle a lack of dystrophin disrupts the recruitment of neuronal NOS (nitric oxide synthase) to the sarcolemma thus affecting NO (nitric oxide) production. Utrophin is a dystrophin homologue, the expression of which is greatly up-regulated in the sarcolemma of dystrophin-negative fibres from mdx mice, a mouse model of DMD. Although cardiomyopathy is an important cause of death, little is known about the NO signalling pathway in the cardiac musc

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Sekulic-Jablanovic, Marijana, Nina D. Ullrich, David Goldblum, Anja Palmowski-Wolfe, Francesco Zorzato, and Susan Treves. "Functional characterization of orbicularis oculi and extraocular muscles." Journal of General Physiology 147, no. 5 (April 11, 2016): 395–406. http://dx.doi.org/10.1085/jgp.201511542.

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The orbicularis oculi are the sphincter muscles of the eyelids and are involved in modulating facial expression. They differ from both limb and extraocular muscles (EOMs) in their histology and biochemistry. Weakness of the orbicularis oculi muscles is a feature of neuromuscular disorders affecting the neuromuscular junction, and weakness of facial muscles and ptosis have also been described in patients with mutations in the ryanodine receptor gene. Here, we investigate human orbicularis oculi muscles and find that they are functionally more similar to quadriceps than to EOMs in terms of excit

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Kachinsky, Amy M., Stanley C. Froehner, and Sharon L. Milgram. "A PDZ-containing Scaffold Related to the Dystrophin Complex at the Basolateral Membrane of Epithelial Cells." Journal of Cell Biology 145, no. 2 (April 19, 1999): 391–402. http://dx.doi.org/10.1083/jcb.145.2.391.

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Membrane scaffolding complexes are key features of many cell types, serving as specialized links between the extracellular matrix and the actin cytoskeleton. An important scaffold in skeletal muscle is the dystrophin-associated protein complex. One of the proteins bound directly to dystrophin is syntrophin, a modular protein comprised entirely of interaction motifs, including PDZ (protein domain named for PSD-95, discs large, ZO-1) and pleckstrin homology (PH) domains. In skeletal muscle, the syntrophin PDZ domain recruits sodium channels and signaling molecules, such as neuronal nitric oxide

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