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Myosin in Cultured Human Endothelial Cells
Author(s) -
Moore Anne,
Jafee Eric A.,
Becker Carl G.,
Nachman Ralph L.
Publication year - 1977
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1977.tb00564.x
Subject(s) - myosin , antiserum , endothelial stem cell , myosin light chain kinase , biology , microbiology and biotechnology , gel electrophoresis , sepharose , biochemistry , chemistry , antibody , enzyme , immunology , in vitro
Myosin was isolated from cultured human endothelial cells by extraction with 0.6 M KCl and chromatography on Sepharose 4B. The extracted endothelial cell protein was identified as myosin by the characteristic ATPase profile, that is, the ATPase was activated by Ca 2+ and EDTA and inhibited by Mg 2+ . On sodium dodecyl sulphate polyacrylamide gel electrophoresis, the endothelial cell myosin heavy chain migrated with a molecular weight of 200 000 as did rabbit uterine and human platelet myosin heavy chains. A crude preparation of the endothelial cell myosin reacted immunologically with an antiserum to platelet myosin, a smooth muscle type of myosin. In indirect immunofluorescence studies, antiserum to the purified endothelial cell myosin stained cultured endothelial cells in a fibrillar pattern. The fibrillar pattern was more intense when the endothelial cells were stained with antiserum to platelet myosin. The presence of myosin in the endothelial cell provides a basis for the contractility of these cells. This contractile property may plan an important role in the physiologic function of these cells.