Literature DB >> 8312480

The fastest contracting muscles of nonmammalian vertebrates express only one isoform of the ryanodine receptor.

J O'Brien1, G Meissner, B A Block.   

Abstract

The skeletal muscles of chickens, frogs, and fish have been reported to express two isoforms (alpha and beta) of the sarcoplasmic reticulum calcium release channel (ryanodine receptor or RYR), while mammals express only one. We have studied patterns of RYR isoform expression in skeletal muscles from a variety of fish, reptiles, and birds with immunological techniques. Immunoblot analysis with a monoclonal antibody that recognizes both nonmammalian RYR isoforms and a polyclonal antibody specific to the alpha isoform show two key results: (a) two reptilian orders share with mammals the pattern of expressing only the alpha (skeletal) RYR isoform in skeletal muscle; and (b) certain functionally specialized muscles of fish and birds express only the alpha RYR isoforms. While both isoforms are expressed in the body musculature of fish and birds, the alpha isoform is expressed alone in extraocular muscles and swimbladder muscles. The appearance of the alpha RYR isoform alone in the extraocular muscles and a fast-contracting sonic muscle in fish (toadfish swimbladder muscle) provides evidence that this isoform is selectively expressed when rapid contraction is required. The functional and phylogenetic implications of expression of the alpha isoform alone are discussed in the context of the mechanism and evolution of excitation-contraction coupling.

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Year:  1993        PMID: 8312480      PMCID: PMC1225982          DOI: 10.1016/S0006-3495(93)81303-1

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  42 in total

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Authors:  C B Stewart
Journal:  Nature       Date:  1993-02-18       Impact factor: 49.962

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Authors:  T Murayama; Y Ogawa
Journal:  J Biochem       Date:  1992-10       Impact factor: 3.387

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  24 in total

1.  Differential effects of contractile potentiators on action potential-induced Ca2+ transients of frog and mouse skeletal muscle fibres.

Authors:  Caputo Carlo; Bolaños Pura; Ramos Magaly; DiFranco Marino
Journal:  J Muscle Res Cell Motil       Date:  2016-09-02       Impact factor: 2.698

Review 2.  Comparison of properties of Ca2+ release channels between rabbit and frog skeletal muscles.

Authors:  Y Ogawa; T Murayama; N Kurebayashi
Journal:  Mol Cell Biochem       Date:  1999-01       Impact factor: 3.396

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Authors:  F Protasi; H Takekura; Y Wang; S R Chen; G Meissner; P D Allen; C Franzini-Armstrong
Journal:  Biophys J       Date:  2000-11       Impact factor: 4.033

4.  Type 3 ryanodine receptors of skeletal muscle are segregated in a parajunctional position.

Authors:  Edward Felder; Clara Franzini-Armstrong
Journal:  Proc Natl Acad Sci U S A       Date:  2002-01-29       Impact factor: 11.205

Review 5.  The role of skeletal-muscle-based thermogenic mechanisms in vertebrate endothermy.

Authors:  Leslie A Rowland; Naresh C Bal; Muthu Periasamy
Journal:  Biol Rev Camb Philos Soc       Date:  2014-11-25

Review 6.  Ryanodine receptors: structure, expression, molecular details, and function in calcium release.

Authors:  Johanna T Lanner; Dimitra K Georgiou; Aditya D Joshi; Susan L Hamilton
Journal:  Cold Spring Harb Perspect Biol       Date:  2010-10-20       Impact factor: 10.005

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Authors:  J O'Brien; H H Valdivia; B A Block
Journal:  Biophys J       Date:  1995-02       Impact factor: 4.033

8.  Simulation of Ca2+ movements within the sarcomere of fast-twitch mouse fibers stimulated by action potentials.

Authors:  Stephen M Baylor; Stephen Hollingworth
Journal:  J Gen Physiol       Date:  2007-09       Impact factor: 4.086

9.  Chicken skeletal muscle ryanodine receptor isoforms: ion channel properties.

Authors:  A L Percival; A J Williams; J L Kenyon; M M Grinsell; J A Airey; J L Sutko
Journal:  Biophys J       Date:  1994-11       Impact factor: 4.033

10.  Ca2+ modulation of sarcoplasmic reticulum Ca2+ release in rat skeletal muscle fibers.

Authors:  O Delbono
Journal:  J Membr Biol       Date:  1995-07       Impact factor: 1.843

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