Literature DB >> 20418783

In vitro analysis of rod composition and actin dynamics in inherited myopathies.

Aurélie Vandebrouck1, Ana Domazetovska, Nancy Mokbel, Sandra T Cooper, Biljana Ilkovski, Kathryn N North.   

Abstract

Rods are the pathological hallmark of nemaline myopathy, but they can also occur as a secondary phenomenon in other disorders, including mitochondrial myopathies such as complex I deficiency. The mechanisms of rod formation are not well understood, particularly when rods occur in diverse disorders with very different structural and metabolic defects. We compared the characteristics of rods associated with abnormalities in structural components of skeletal muscle thin filament (3 mutations in the skeletal actin gene ACTA1) with those of rods induced by the metabolic cell stress of adenosine triphosphate depletion. C2C12 and NIH/3T3 cell culture models and immunocytochemistry were used to study rod composition and conformation. Fluorescent recovery after photobleaching was used to measure actin dynamics inside the rods. We demonstrate that not all rods are the same. Rods formed under different conditions contain a unique fingerprint of actin-binding proteins (cofilin and alpha-actinin) and display differences in actin dynamics that are specific to the mutation, to the cellular location of the rods (intranuclear vs cytoplasmic), and/or to the underlying pathological process (i.e. mutant actin or adenosine triphosphate depletion). Thus, rods likely represent a common morphological end point of a variety of different pathological processes, either structural or metabolic.

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Year:  2010        PMID: 20418783     DOI: 10.1097/NEN.0b013e3181d892c6

Source DB:  PubMed          Journal:  J Neuropathol Exp Neurol        ISSN: 0022-3069            Impact factor:   3.685


  11 in total

1.  Binucleate germ cells in Caenorhabditis elegans are removed by physiological apoptosis.

Authors:  Stephan A Raiders; Michael D Eastwood; Meghan Bacher; James R Priess
Journal:  PLoS Genet       Date:  2018-07-19       Impact factor: 5.917

Review 2.  Nuclear actin and myosins at a glance.

Authors:  Primal de Lanerolle
Journal:  J Cell Sci       Date:  2012-11-01       Impact factor: 5.285

Review 3.  Dynamic regulation of sarcomeric actin filaments in striated muscle.

Authors:  Shoichiro Ono
Journal:  Cytoskeleton (Hoboken)       Date:  2010-11

4.  Imaging Intranuclear Actin Rods in Live Heat Stressed Drosophila Embryos.

Authors:  Natalie Biel; Lauren Figard; Anna Marie Sokac
Journal:  J Vis Exp       Date:  2020-05-15       Impact factor: 1.424

5.  Zebrafish models for nemaline myopathy reveal a spectrum of nemaline bodies contributing to reduced muscle function.

Authors:  Tamar E Sztal; Mo Zhao; Caitlin Williams; Viola Oorschot; Adam C Parslow; Aminah Giousoh; Michaela Yuen; Thomas E Hall; Adam Costin; Georg Ramm; Phillip I Bird; Elisabeth M Busch-Nentwich; Derek L Stemple; Peter D Currie; Sandra T Cooper; Nigel G Laing; Kristen J Nowak; Robert J Bryson-Richardson
Journal:  Acta Neuropathol       Date:  2015-05-01       Impact factor: 17.088

6.  The Effects of Disease Models of Nuclear Actin Polymerization on the Nucleus.

Authors:  Leonid A Serebryannyy; Michaela Yuen; Megan Parilla; Sandra T Cooper; Primal de Lanerolle
Journal:  Front Physiol       Date:  2016-10-07       Impact factor: 4.566

7.  Actin-Interacting Protein 1 Contributes to Intranuclear Rod Assembly in Dictyostelium discoideum.

Authors:  Hellen C Ishikawa-Ankerhold; Wioleta Daszkiewicz; Michael Schleicher; Annette Müller-Taubenberger
Journal:  Sci Rep       Date:  2017-01-11       Impact factor: 4.379

Review 8.  Nemaline myopathies: a current view.

Authors:  Caroline A Sewry; Jenni M Laitila; Carina Wallgren-Pettersson
Journal:  J Muscle Res Cell Motil       Date:  2019-06-21       Impact factor: 2.698

9.  Phenotypes of myopathy-related beta-tropomyosin mutants in human and mouse tissue cultures.

Authors:  Saba Abdul-Hussein; Karin Rahl; Ali-Reza Moslemi; Homa Tajsharghi
Journal:  PLoS One       Date:  2013-09-10       Impact factor: 3.240

10.  Phosphorylated cofilin-2 is more prone to oxidative modifications on Cys39 and favors amyloid fibril formation.

Authors:  Marcello Pignataro; Giulia Di Rocco; Lidia Lancellotti; Fabrizio Bernini; Khaushik Subramanian; Elena Castellini; Carlo Augusto Bortolotti; Daniele Malferrari; Daniele Moro; Giovanni Valdrè; Marco Borsari; Federica Del Monte
Journal:  Redox Biol       Date:  2020-08-25       Impact factor: 11.799

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