Literature DB >> 8814556

A study on the mechanism of phalloidin-induced tension changes in skinned rabbit psoas muscle fibres.

A E Bukatina1, F Fuchs, S C Watkins.   

Abstract

The time course of phalloidin induced changes in isometric tension of partially activated skinned rabbit psoas fibres was studied as a function of both phalloidin concentration and time of pre-incubation with phalloidin. Upon addition of phalloidin to non-pretreated (control) fibres there was a fall in tension followed by an increase in tension. The latency of both parts of the response was inversely related to the phalloidin concentration in the range 40-130 microM phalloidin. By preincubating the fibres with phalloidin for varying periods of time it was possible to obtain responses which appeared to represent later portions of the control response. Thus after pre-treatment with 40 microM phalloidin in either rigor or relaxing solution for 5 min (the time corresponding to minimal tension in the control response) the tension response resembled that of the control, beginning from the vicinity of the minimum. The pattern of staining of the fibres by rhodamine-phalloidin was analysed by laser confocal microscopy to relate the mechanical response to phalloidin localization. If fibres were treated with rhodamine-phalloidin for 20-25 min there was a labelling of the I-Z-I segment with intense peaks of fluorescence at the Z-line and the ends of the I filaments. If fibres were pre-incubated for 5 min with phalloidin and then labelled with rhodamine-phalloidin the fluorescence at the Z-line and at the ends of the I filaments was suppressed and the peak of the fluorescence intensity was shifted toward the middle part of the I filament. The data indicate that the decrease in tension caused by phalloidin was associated with binding of phalloidin to the pointed ends of actin filament and the Z-line region, whereas the increase in tension occurred when phalloidin was bound along entire length of the actin filament.

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Year:  1996        PMID: 8814556     DOI: 10.1007/bf00240934

Source DB:  PubMed          Journal:  J Muscle Res Cell Motil        ISSN: 0142-4319            Impact factor:   2.698


  22 in total

1.  Interaction of actin with phalloidin: polymerization and stabilization of F-actin.

Authors:  P Dancker; I Löw; W Hasselbach; T Wieland
Journal:  Biochim Biophys Acta       Date:  1975-08-19

Review 2.  The cytoskeletal lattice of muscle cells.

Authors:  J V Small; D O Fürst; L E Thornell
Journal:  Eur J Biochem       Date:  1992-09-15

3.  Atomic model of the actin filament.

Authors:  K C Holmes; D Popp; W Gebhard; W Kabsch
Journal:  Nature       Date:  1990-09-06       Impact factor: 49.962

4.  Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells.

Authors:  A Fabiato; F Fabiato
Journal:  J Physiol (Paris)       Date:  1979

5.  Thin filament activation by phalloidin in skinned cardiac muscle.

Authors:  A E Bukatina; F Fuchs; P W Brandt
Journal:  J Mol Cell Cardiol       Date:  1995-06       Impact factor: 5.000

6.  The binding of fluorescent phallotoxins to actin in myofibrils.

Authors:  D Szczesna; S S Lehrer
Journal:  J Muscle Res Cell Motil       Date:  1993-12       Impact factor: 2.698

7.  Transient kinetic analysis of rhodamine phalloidin binding to actin filaments.

Authors:  E M De La Cruz; T D Pollard
Journal:  Biochemistry       Date:  1994-12-06       Impact factor: 3.162

8.  Effect of phalloidin on the ATPase activity of striated muscle myofibrils.

Authors:  A E Bukatina; F Fuchs
Journal:  J Muscle Res Cell Motil       Date:  1994-02       Impact factor: 2.698

9.  Phalloidin-induced actin polymerization in the cytoplasm of cultured cells interferes with cell locomotion and growth.

Authors:  J Wehland; M Osborn; K Weber
Journal:  Proc Natl Acad Sci U S A       Date:  1977-12       Impact factor: 11.205

10.  Calmodulin-sensitive interaction of human nebulin fragments with actin and myosin.

Authors:  D D Root; K Wang
Journal:  Biochemistry       Date:  1994-10-25       Impact factor: 3.162

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  14 in total

1.  F-actin stabilization increases tension cost during contraction of permeabilized airway smooth muscle in dogs.

Authors:  K A Jones; W J Perkins; R R Lorenz; Y S Prakash; G C Sieck; D O Warner
Journal:  J Physiol       Date:  1999-09-01       Impact factor: 5.182

2.  Familial hypertrophic cardiomyopathy can be characterized by a specific pattern of orientation fluctuations of actin molecules .

Authors:  J Borejdo; D Szczesna-Cordary; P Muthu; N Calander
Journal:  Biochemistry       Date:  2010-06-29       Impact factor: 3.162

3.  Simultaneous measurement of rotations of myosin, actin and ADP in a contracting skeletal muscle fiber.

Authors:  A A Shepard; D Dumka; I Akopova; J Talent; J Borejdo
Journal:  J Muscle Res Cell Motil       Date:  2005-02-09       Impact factor: 2.698

4.  Application of surface plasmon coupled emission to study of muscle.

Authors:  J Borejdo; Z Gryczynski; N Calander; P Muthu; I Gryczynski
Journal:  Biophys J       Date:  2006-07-14       Impact factor: 4.033

5.  Decreasing photobleaching by silver island films: application to muscle.

Authors:  P Muthu; I Gryczynski; Z Gryczynski; J Talent; I Akopova; K Jain; J Borejdo
Journal:  Anal Biochem       Date:  2007-04-12       Impact factor: 3.365

6.  Cross-bridge kinetics in myofibrils containing familial hypertrophic cardiomyopathy R58Q mutation in the regulatory light chain of myosin.

Authors:  P Mettikolla; N Calander; R Luchowski; I Gryczynski; Z Gryczynski; J Zhao; D Szczesna-Cordary; J Borejdo
Journal:  J Theor Biol       Date:  2011-06-24       Impact factor: 2.691

7.  A single-fiber in vitro motility assay. In vitro sliding velocity of F-actin vs. unloaded shortening velocity in skinned muscle fibers.

Authors:  E Thedinga; N Karim; T Kraft; B Brenner
Journal:  J Muscle Res Cell Motil       Date:  1999-11       Impact factor: 2.698

8.  Kinetics of a single cross-bridge in familial hypertrophic cardiomyopathy heart muscle measured by reverse Kretschmann fluorescence.

Authors:  Prasad Mettikolla; Nils Calander; Rafal Luchowski; Ignacy Gryczynski; Zygmunt Gryczynski; Julian Borejdo
Journal:  J Biomed Opt       Date:  2010 Jan-Feb       Impact factor: 3.170

9.  Dethiophalloidin increases Ca2+ responsiveness of skinned cardiac muscle.

Authors:  A E Bukatina; R D Kirkpatrick; K B Campbell
Journal:  J Muscle Res Cell Motil       Date:  1998-06       Impact factor: 2.698

10.  Single molecule kinetics in the familial hypertrophic cardiomyopathy D166V mutant mouse heart.

Authors:  Priya Muthu; Prasad Mettikolla; Nils Calander; Rafal Luchowski; Ignacy Gryczynski; Zygmunt Gryczynski; Danuta Szczesna-Cordary; J Borejdo
Journal:  J Mol Cell Cardiol       Date:  2009-11-13       Impact factor: 5.000

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