Literature DB >> 12438018

Regulation of mammalian ryanodine receptors.

Gerhard Meissner1.   

Abstract

Ryanodine receptors (RyRs) are large, high conductance Ca2+ channels that control the level of intracellular Ca2+ by releasing Ca2+ from an intracellular compartment, the sarco/endoplasmic reticulum. Mammalian tissues express 3 closely related ryanodine receptors (RyRs) known as skeletal muscle (RyR1), cardiac muscle (RyR2) and brain (RyR3). The RyRs are isolated as 30S protein complexes comprised of four 560 kDa RyR2 subunits and four 12.6 kDa FK506 binding protein (FKBP12.6) subunits. Multiple endogenous effector molecules and posttranslational modifications regulate the RyRs. This chapter reviews the regulation of the mammalian RyRs by endogenous effector molecules.

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Year:  2002        PMID: 12438018     DOI: 10.2741/A899

Source DB:  PubMed          Journal:  Front Biosci        ISSN: 1093-4715


  76 in total

Review 1.  Nanospaces between endoplasmic reticulum and mitochondria as control centres of pancreatic β-cell metabolism and survival.

Authors:  James D Johnson; Michael J Bround; Sarah A White; Dan S Luciani
Journal:  Protoplasma       Date:  2011-11-22       Impact factor: 3.356

Review 2.  The voltage-dependent anion channel in endoplasmic/sarcoplasmic reticulum: characterization, modulation and possible function.

Authors:  V Shoshan-Barmatz; A Israelson
Journal:  J Membr Biol       Date:  2005-03       Impact factor: 1.843

Review 3.  Cardiac and skeletal muscle disorders caused by mutations in the intracellular Ca2+ release channels.

Authors:  Silvia G Priori; Carlo Napolitano
Journal:  J Clin Invest       Date:  2005-08       Impact factor: 14.808

Review 4.  Muscle channelopathies and critical points in functional and genetic studies.

Authors:  Karin Jurkat-Rott; Frank Lehmann-Horn
Journal:  J Clin Invest       Date:  2005-08       Impact factor: 14.808

5.  Modulation of sarcoplasmic reticulum Ca2+ release in skeletal muscle expressing ryanodine receptor impaired in regulation by calmodulin and S100A1.

Authors:  Naohiro Yamaguchi; Benjamin L Prosser; Farshid Ghassemi; Le Xu; Daniel A Pasek; Jerry P Eu; Erick O Hernández-Ochoa; Brian R Cannon; Paul T Wilder; Richard M Lovering; David Weber; Werner Melzer; Martin F Schneider; Gerhard Meissner
Journal:  Am J Physiol Cell Physiol       Date:  2011-02-02       Impact factor: 4.249

6.  Single channel properties of heterotetrameric mutant RyR1 ion channels linked to core myopathies.

Authors:  Le Xu; Ying Wang; Naohiro Yamaguchi; Daniel A Pasek; Gerhard Meissner
Journal:  J Biol Chem       Date:  2008-01-01       Impact factor: 5.157

7.  Silencing genes of sarcoplasmic reticulum proteins clarifies their roles in excitation-contraction coupling.

Authors:  Gerhard Meissner; Ying Wang; Le Xu; Jerry P Eu
Journal:  J Physiol       Date:  2009-07-01       Impact factor: 5.182

8.  Aldolase potentiates DIDS activation of the ryanodine receptor in rabbit skeletal sarcoplasmic reticulum.

Authors:  In-Ra Seo; Sang Hyun Moh; Eun Hui Lee; Gerhard Meissner; Do Han Kim
Journal:  Biochem J       Date:  2006-10-15       Impact factor: 3.857

9.  Evidence for the transport of glutathione through ryanodine receptor channel type 1.

Authors:  Gábor Bánhegyi; Miklós Csala; Gábor Nagy; Vincenzo Sorrentino; Rosella Fulceri; Angelo Benedetti
Journal:  Biochem J       Date:  2003-12-15       Impact factor: 3.857

10.  Multi-minicore disease and atypical periodic paralysis associated with novel mutations in the skeletal muscle ryanodine receptor (RYR1) gene.

Authors:  Haiyan Zhou; Suzanne Lillis; Ryan E Loy; Farshid Ghassemi; Michael R Rose; Fiona Norwood; Kerry Mills; Safa Al-Sarraj; Russell J M Lane; Lucy Feng; Emma Matthews; Caroline A Sewry; Stephen Abbs; Stefan Buk; Michael Hanna; Susan Treves; Robert T Dirksen; Gerhard Meissner; Francesco Muntoni; Heinz Jungbluth
Journal:  Neuromuscul Disord       Date:  2010-01-18       Impact factor: 4.296

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