Literature DB >> 3100573

The effect of calcium on the aggregation of chicken gizzard thin filaments.

W Lehman.   

Abstract

Electron microscopy demonstrates that thin filaments isolated from chicken gizzard smooth muscle in the absence of Ca2+ are aggregated into networks. In contrast, thin filaments isolated in the presence of Ca2+ are dissociated from each other. Electron microscopy also reveals that the respective state of aggregation in each type of preparation is reversible and dependent on Ca2+ concentration. Corresponding viscosity measurements indicate that network formation is associated with an increase in thin filament viscosity. We propose that thin filament aggregation in vivo may be responsible for the tension maintenance of smooth muscle during relaxation.

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Year:  1986        PMID: 3100573     DOI: 10.1007/bf01753570

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


  26 in total

1.  Crosslinking of actin filaments is caused by caldesmon aggregates, but not by its dimers.

Authors:  K Sobue; K Takahashi; T Tanaka; K Kanda; N Ashino; S Kakiuchi; K Maruyama
Journal:  FEBS Lett       Date:  1985-03-11       Impact factor: 4.124

2.  A Ca2+-dependent actin modulator from vertebrate smooth muscle.

Authors:  H Hinssen; J V Small; A Sobieszek
Journal:  FEBS Lett       Date:  1984-01-23       Impact factor: 4.124

3.  Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner.

Authors:  A Bretscher; K Weber
Journal:  Cell       Date:  1980-07       Impact factor: 41.582

4.  Role of Ca2+ and myosin light chain phosphorylation in regulation of smooth muscle.

Authors:  M O Aksoy; R A Murphy; K E Kamm
Journal:  Am J Physiol       Date:  1982-01

5.  Methods to characterize actin filament networks.

Authors:  T D Pollard; J A Cooper
Journal:  Methods Enzymol       Date:  1982       Impact factor: 1.600

Review 6.  The filamins: properties and functions.

Authors:  R R Weihing
Journal:  Can J Biochem Cell Biol       Date:  1985-06

7.  Caldesmon association with smooth muscle thin filaments isolated in the presence and absence of calcium.

Authors:  W Lehman
Journal:  Biochim Biophys Acta       Date:  1986-01-23

8.  Bundling of actin filaments by aorta caldesmon is not related to its regulatory function.

Authors:  C J Moody; S B Marston; C W Smith
Journal:  FEBS Lett       Date:  1985-10-21       Impact factor: 4.124

9.  Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon.

Authors:  P K Ngai; M P Walsh
Journal:  J Biol Chem       Date:  1984-11-25       Impact factor: 5.157

10.  Calcium-dependent interaction of actin filaments with actin binding protein in the presence of calmodulin and caldesmon.

Authors:  K Maruyama; K Morimoto; Y Kijima; K Sobue; S Kakiuchi
Journal:  J Biochem       Date:  1985-05       Impact factor: 3.387

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  3 in total

Review 1.  Calponin (CaP) as a latch-bridge protein--a new concept in regulation of contractility in smooth muscles.

Authors:  Pawel T Szymanski
Journal:  J Muscle Res Cell Motil       Date:  2004       Impact factor: 2.698

2.  Interaction of calponin with actin and its functional implications.

Authors:  J Kołakowski; R Makuch; D Stepkowski; R Dabrowska
Journal:  Biochem J       Date:  1995-02-15       Impact factor: 3.857

3.  Caldesmon and the structure of smooth muscle thin filaments: electron microscopy of isolated thin filaments.

Authors:  C Moody; W Lehman; R Craig
Journal:  J Muscle Res Cell Motil       Date:  1990-04       Impact factor: 2.698

  3 in total

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