Linked Life Data

1834987

Source:http://linkedlifedata.com/resource/pubmed/id/1834987

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1991-11-25
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0031-6768
pubmed:author
pubmed:issnType
Print
pubmed:volume
418
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
523-30
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle.
pubmed:affiliation
Department of Physiology and Biophysics, University of Lund, Sweden.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, Non-U.S. Gov't