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Title: Involvement of myosin light-chain kinase in endothelial cell retraction

Abstract

Permeabilized bovine pulmonary artery endothelial cell monolayers were used to investigate the mechanism of endothelial cell retraction. Postconfluent endothelial cells permeabilized with saponin retracted upon exposure to ATP and Ca{sup 2+}. Retraction was accompanied by thiophosphorylation of 19,000-Da myosin light chains when adenosine 5'-(gamma-({sup 35}S)thio)triphosphate was included in the medium. Both retraction and thiophosphorylation of myosin light chains exhibited a graded quantitative dependence on Ca{sup 2+}. When permeabilized monolayers were extracted in buffer D containing 100 mM KCl and 30 mM MgCl2 for 30 min, the cells failed to retract upon exposure to ATP and Ca{sup 2+}, and no thiophosphorylation of myosin light chains occurred. The ability both to retract and to thiophosphorylate myosin light chains was restored by the addition to the permeabilized, extracted cells of myosin light-chain kinase and calmodulin together but not by either alone. These studies indicate that endothelial cell retraction, as does smooth muscle contraction, depends on myosin light-chain kinase phosphorylation of myosin light chains.

Authors:
;  [1]
  1. Saint Louis Univ. School of Medicine, MO (USA)
Publication Date:
OSTI Identifier:
6968819
Resource Type:
Journal Article
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America; (USA)
Additional Journal Information:
Journal Volume: 87:1; Journal ID: ISSN 0027-8424
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; CELL MEMBRANES; PERMEABILITY; MYOSIN; PHOSPHORYLATION; PHOSPHOTRANSFERASES; ENZYME ACTIVITY; ATP; CALCIUM COMPOUNDS; CATTLE; ELECTROPHORESIS; ENDOTHELIUM; FLUORESCENCE; MOLECULAR WEIGHT; SULFUR 35; TRACER TECHNIQUES; ALKALINE EARTH METAL COMPOUNDS; ANIMAL TISSUES; ANIMALS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; BODY; CELL CONSTITUENTS; CHEMICAL REACTIONS; DAYS LIVING RADIOISOTOPES; DOMESTIC ANIMALS; ENZYMES; EVEN-ODD NUCLEI; GLOBULINS; ISOTOPE APPLICATIONS; ISOTOPES; LIGHT NUCLEI; LUMINESCENCE; MAMMALS; MEMBRANES; NUCLEI; NUCLEOTIDES; ORGANIC COMPOUNDS; PHOSPHORUS-GROUP TRANSFERASES; PROTEINS; RADIOISOTOPES; RUMINANTS; SULFUR ISOTOPES; TISSUES; TRANSFERASES; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Wysolmerski, R B, and Lagunoff, D. Involvement of myosin light-chain kinase in endothelial cell retraction. United States: N. p., 1990. Web. doi:10.1073/pnas.87.1.16.
Wysolmerski, R B, & Lagunoff, D. Involvement of myosin light-chain kinase in endothelial cell retraction. United States. https://doi.org/10.1073/pnas.87.1.16
Wysolmerski, R B, and Lagunoff, D. 1990. "Involvement of myosin light-chain kinase in endothelial cell retraction". United States. https://doi.org/10.1073/pnas.87.1.16.
@article{osti_6968819,
title = {Involvement of myosin light-chain kinase in endothelial cell retraction},
author = {Wysolmerski, R B and Lagunoff, D},
abstractNote = {Permeabilized bovine pulmonary artery endothelial cell monolayers were used to investigate the mechanism of endothelial cell retraction. Postconfluent endothelial cells permeabilized with saponin retracted upon exposure to ATP and Ca{sup 2+}. Retraction was accompanied by thiophosphorylation of 19,000-Da myosin light chains when adenosine 5'-(gamma-({sup 35}S)thio)triphosphate was included in the medium. Both retraction and thiophosphorylation of myosin light chains exhibited a graded quantitative dependence on Ca{sup 2+}. When permeabilized monolayers were extracted in buffer D containing 100 mM KCl and 30 mM MgCl2 for 30 min, the cells failed to retract upon exposure to ATP and Ca{sup 2+}, and no thiophosphorylation of myosin light chains occurred. The ability both to retract and to thiophosphorylate myosin light chains was restored by the addition to the permeabilized, extracted cells of myosin light-chain kinase and calmodulin together but not by either alone. These studies indicate that endothelial cell retraction, as does smooth muscle contraction, depends on myosin light-chain kinase phosphorylation of myosin light chains.},
doi = {10.1073/pnas.87.1.16},
url = {https://www.osti.gov/biblio/6968819}, journal = {Proceedings of the National Academy of Sciences of the United States of America; (USA)},
issn = {0027-8424},
number = ,
volume = 87:1,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 1990},
month = {Mon Jan 01 00:00:00 EST 1990}
}