Literature DB >> 1864461

Simultaneous maturation of transverse tubules and sarcoplasmic reticulum during muscle differentiation in the mouse.

C Franzini-Armstrong1.   

Abstract

The development and maturation of transverse (T) tubules and sarcoplasmic reticulum (SR) have been studied in pre- and postnatal mouse muscle, using selective "staining" of these membrane systems. As previously reported in the literature, orderly transverse orientation of the T tubules occurs late in development and early T-SR junctions (triads and dyads) are located at random along the T tubules in a predominantly longitudinal orientation. We find that initial appearance of transverse tubules occurs fairly abruptly, and that all early T tubules have a longitudinal orientation. Transverse orientation of the T tubule network, location of triads at the A-I junction, and development of differentiated regions of the SR are coordinated events which occur gradually over a period of about 3 weeks for leg muscle.s The timing of triad development coincides with that reported for the increase in slow calcium current and dihydropyridine binding. Differences in T tubule patterns between muscle fibers of EDL and soleus are apparent only at relatively late stages.

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Mesh:

Year:  1991        PMID: 1864461     DOI: 10.1016/0012-1606(91)90237-w

Source DB:  PubMed          Journal:  Dev Biol        ISSN: 0012-1606            Impact factor:   3.582


  62 in total

1.  Differential response of the membrane systems involved in excitation-contraction coupling to early and later postnatal denervation in rat skeletal muscle.

Authors:  H Takekura; N Kasuga
Journal:  J Muscle Res Cell Motil       Date:  1999-04       Impact factor: 2.698

2.  Functional expression of the L-type calcium channel in mice skeletal muscle during prenatal myogenesis.

Authors:  C Strube; Y Tourneur; C Ojeda
Journal:  Biophys J       Date:  2000-03       Impact factor: 4.033

3.  Expression of L-type calcium channels associated with postnatal development of skeletal muscle function in mouse.

Authors:  S Mänttäri; A Pyörnilä; R Harjula; M Järvilehto
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

Review 4.  Organization of junctional sarcoplasmic reticulum proteins in skeletal muscle fibers.

Authors:  Virginia Barone; Davide Randazzo; Valeria Del Re; Vincenzo Sorrentino; Daniela Rossi
Journal:  J Muscle Res Cell Motil       Date:  2015-09-15       Impact factor: 2.698

5.  Ca2+/CaM-dependent inactivation of the skeletal muscle L-type Ca2+ channel (Cav1.1).

Authors:  Katarina Stroffekova
Journal:  Pflugers Arch       Date:  2007-09-26       Impact factor: 3.657

6.  Assembly of transverse tubule architecture in the middle and myotendinous junctional regions in developing rat skeletal muscle fibers.

Authors:  Susumu Yamashita; Kelly F McGrath; Atsumu Yuki; Hiroyuki Tamaki; Norikatsu Kasuga; Hiroaki Takekura
Journal:  J Muscle Res Cell Motil       Date:  2007-07-04       Impact factor: 2.698

7.  Regulated expression and temporal induction of the tail-anchored sarcolemmal-membrane-associated protein is critical for myoblast fusion.

Authors:  Rosa M Guzzo; Jeffery Wigle; Maysoon Salih; Edwin D Moore; Balwant S Tuana
Journal:  Biochem J       Date:  2004-08-01       Impact factor: 3.857

8.  Three-dimensional electron microscopy reveals new details of membrane systems for Ca2+ signaling in the heart.

Authors:  Takeharu Hayashi; Maryann E Martone; Zeyun Yu; Andrea Thor; Masahiro Doi; Michael J Holst; Mark H Ellisman; Masahiko Hoshijima
Journal:  J Cell Sci       Date:  2009-04-01       Impact factor: 5.285

9.  Membrane localization, Caveolin-3 association and rapid actions of vitamin D receptor in cardiac myocytes.

Authors:  Guisheng Zhao; Robert U Simpson
Journal:  Steroids       Date:  2009-12-14       Impact factor: 2.668

10.  Age-dependent chloride channel expression in skeletal muscle fibres of normal and HSA(LR) myotonic mice.

Authors:  Marino DiFranco; Carl Yu; Marbella Quiñonez; Julio L Vergara
Journal:  J Physiol       Date:  2012-12-17       Impact factor: 5.182

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