Proteome analysis of migrating versus nonmigrating rat heart endothelial cells reveals distinct expression patterns
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Proteome analysis of migrating versus nonmigrating rat heart endothelial cells reveals distinct expression patterns. / Obermeyer, Natalie; Janson, Nina; Bergmann, Juliane; Buck, Friedrich; Ito, Wulf D.
in: ENDOTHELIUM-J ENDOTH, Jahrgang 10, Nr. 3, 2003, S. 167-178.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Proteome analysis of migrating versus nonmigrating rat heart endothelial cells reveals distinct expression patterns
AU - Obermeyer, Natalie
AU - Janson, Nina
AU - Bergmann, Juliane
AU - Buck, Friedrich
AU - Ito, Wulf D
PY - 2003
Y1 - 2003
N2 - Migration of endothelial cells plays an important role during angiogenesis and the late remodeling phase of arteriogenesis. To investigate mechanisms responsible for cell migration, the authors subcloned a rat heart endothelial cell line (RHE) into a migrating and a nonmigrating cell line (RHE-A and RHE-neg, respectively). Both cell lines form cobblestone patterns in confluent cultures similar to the originating cell line, but RHE-neg cells grow in dense cell islets of several layers whereas RHE-A cells grow in a less dense monolayer. Both cell lines show the same expression pattern of known endothelial cell surface antigens (e.g., FIK-1). The authors used two-dimensional gel electrophoresis technique to look for differentially regulated proteins with possible functional importance for cell migration. The analysis of the cytosolic fraction as well as the membrane fraction revealed differences in the protein expression patterns of RHE-neg and RHE-A cells. Regulated spots were isolated and analyzed by mass spectrometry (MS/MS technique), leading to the identification of proteins potentially responsible for endothelial cell migration, e.g., the intermediate filament vimentin that was exclusively expressed in RHE-A cells. The authors thus have generated a reproducible model that allows the analysis of the proteome responsible for endothelial cell migration.
AB - Migration of endothelial cells plays an important role during angiogenesis and the late remodeling phase of arteriogenesis. To investigate mechanisms responsible for cell migration, the authors subcloned a rat heart endothelial cell line (RHE) into a migrating and a nonmigrating cell line (RHE-A and RHE-neg, respectively). Both cell lines form cobblestone patterns in confluent cultures similar to the originating cell line, but RHE-neg cells grow in dense cell islets of several layers whereas RHE-A cells grow in a less dense monolayer. Both cell lines show the same expression pattern of known endothelial cell surface antigens (e.g., FIK-1). The authors used two-dimensional gel electrophoresis technique to look for differentially regulated proteins with possible functional importance for cell migration. The analysis of the cytosolic fraction as well as the membrane fraction revealed differences in the protein expression patterns of RHE-neg and RHE-A cells. Regulated spots were isolated and analyzed by mass spectrometry (MS/MS technique), leading to the identification of proteins potentially responsible for endothelial cell migration, e.g., the intermediate filament vimentin that was exclusively expressed in RHE-A cells. The authors thus have generated a reproducible model that allows the analysis of the proteome responsible for endothelial cell migration.
KW - Animals
KW - Antigens, Surface/metabolism
KW - Biomarkers
KW - Cell Division/physiology
KW - Cell Line
KW - Cell Movement/physiology
KW - Electrophoresis, Gel, Two-Dimensional
KW - Endothelial Cells/immunology
KW - Keratins/metabolism
KW - Mass Spectrometry
KW - Neovascularization, Physiologic/physiology
KW - Organ Specificity
KW - Proteome/chemistry
KW - Rats
KW - Vimentin/metabolism
U2 - 10.1080/10623320390233481
DO - 10.1080/10623320390233481
M3 - SCORING: Journal article
C2 - 13129820
VL - 10
SP - 167
EP - 178
JO - ENDOTHELIUM-J ENDOTH
JF - ENDOTHELIUM-J ENDOTH
SN - 1062-3329
IS - 3
ER -