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Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle

Malmqvist, Ulf LU and Arner, Anders LU (1991) In Pflügers Archiv 418(6). p.523-530
Abstract
The relation between the isoform distribution of the myosin 17 kDa essential light chain (LC17) and the mechanical properties of smooth muscle was investigated. The relative content of the basic (LC17b) and acidic (LC17a) isoelectric variants of the 17 kDa myosin light chain was determined in different mammalian smooth muscle tissues. The relative content of LC17b varied between muscles: rabbit rectococcygeus 0%, rabbit trachea 5%, guinea-pig taenia coli 21%, rat uterus 38%, rabbit aorta 56% and rat aorta 60%. The rate of tension development was determined following photolysis of caged-adenosine triphosphate (ATP) in skinned fibres activated with thiophosphorylation of the regulatory light chains. The half-time for force development was... (More)
The relation between the isoform distribution of the myosin 17 kDa essential light chain (LC17) and the mechanical properties of smooth muscle was investigated. The relative content of the basic (LC17b) and acidic (LC17a) isoelectric variants of the 17 kDa myosin light chain was determined in different mammalian smooth muscle tissues. The relative content of LC17b varied between muscles: rabbit rectococcygeus 0%, rabbit trachea 5%, guinea-pig taenia coli 21%, rat uterus 38%, rabbit aorta 56% and rat aorta 60%. The rate of tension development was determined following photolysis of caged-adenosine triphosphate (ATP) in skinned fibres activated with thiophosphorylation of the regulatory light chains. The half-time for force development was 0.67 s in rabbit rectococcygeus, 1.6 s in rabbit trachea, 1.13 s in guinea-pig taenia coli and 1.38 s in rabbit aorta. The maximal shortening velocity (Vmax) was determined with the isotonic quick release technique in skinned fibre preparations activated with thiophosphorylation. Vmax was 0.25 muscle lengths per second (ML/s) in rabbit rectococcygeus, 0.24 ML/s in rabbit trachea, 0.17 ML/s in guinea-pig taenia coli, 0.11 ML/s in rat uterus and 0.03 ML/s in rabbit aorta. The range of variation in Vmax between muscles was larger than in the half-time for force development. The inverse relationship between Vmax and the relative content of LC17b in the investigated muscles suggests that the type of essential myosin light chain influences the Vmax in smooth muscle. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Myosin 17 kDa light chains, mooth muscle, Shortening velocity, Caged-ATP, Force development
in
Pflügers Archiv
volume
418
issue
6
pages
523 - 530
publisher
Springer
external identifiers
  • pmid:1834987
  • scopus:0025817957
ISSN
0031-6768
DOI
10.1007/BF00370566
language
English
LU publication?
yes
id
2a607028-4397-4af3-9e84-09b6862ea3fb (old id 1106037)
date added to LUP
2008-08-01 11:13:45
date last changed
2017-08-06 04:26:20
@article{2a607028-4397-4af3-9e84-09b6862ea3fb,
  abstract     = {The relation between the isoform distribution of the myosin 17 kDa essential light chain (LC17) and the mechanical properties of smooth muscle was investigated. The relative content of the basic (LC17b) and acidic (LC17a) isoelectric variants of the 17 kDa myosin light chain was determined in different mammalian smooth muscle tissues. The relative content of LC17b varied between muscles: rabbit rectococcygeus 0%, rabbit trachea 5%, guinea-pig taenia coli 21%, rat uterus 38%, rabbit aorta 56% and rat aorta 60%. The rate of tension development was determined following photolysis of caged-adenosine triphosphate (ATP) in skinned fibres activated with thiophosphorylation of the regulatory light chains. The half-time for force development was 0.67 s in rabbit rectococcygeus, 1.6 s in rabbit trachea, 1.13 s in guinea-pig taenia coli and 1.38 s in rabbit aorta. The maximal shortening velocity (Vmax) was determined with the isotonic quick release technique in skinned fibre preparations activated with thiophosphorylation. Vmax was 0.25 muscle lengths per second (ML/s) in rabbit rectococcygeus, 0.24 ML/s in rabbit trachea, 0.17 ML/s in guinea-pig taenia coli, 0.11 ML/s in rat uterus and 0.03 ML/s in rabbit aorta. The range of variation in Vmax between muscles was larger than in the half-time for force development. The inverse relationship between Vmax and the relative content of LC17b in the investigated muscles suggests that the type of essential myosin light chain influences the Vmax in smooth muscle.},
  author       = {Malmqvist, Ulf and Arner, Anders},
  issn         = {0031-6768},
  keyword      = {Myosin 17 kDa light chains,mooth muscle,Shortening velocity,Caged-ATP,Force development},
  language     = {eng},
  number       = {6},
  pages        = {523--530},
  publisher    = {Springer},
  series       = {Pflügers Archiv},
  title        = {Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle},
  url          = {http://dx.doi.org/10.1007/BF00370566},
  volume       = {418},
  year         = {1991},
}