UNIVERSI
TÄ
TS-
BIBLIOTHEK
P
ADERBORN
Anmelden
Menü
Menü
Start
Hilfe
Blog
Weitere Dienste
Neuerwerbungslisten
Fachsystematik Bücher
Erwerbungsvorschlag
Bestellung aus dem Magazin
Fernleihe
Einstellungen
Sprache
Deutsch
Deutsch
Englisch
Farbschema
Hell
Dunkel
Automatisch
Sie befinden Sich nicht im Netzwerk der Universität Paderborn. Der Zugriff auf elektronische Ressourcen ist
gegebenenfalls
nur via VPN oder Shibboleth (DFN-AAI) möglich.
mehr Informationen...
Universitätsbibliothek
Katalog
Suche
Details
Zur Ergebnisliste
Ergebnis 11 von 53
Datensatz exportieren als...
BibTeX
Intracellular interaction of myosin light chain kinase with macrophage migration inhibition factor (MIF) in endothelium
Journal of cellular biochemistry, 2005-07, Vol.95 (4), p.849-858
Wadgaonkar, Raj
Dudek, Steven M.
Zaiman, Ari L.
Linz-McGillem, Laura
Verin, Alexander D.
Nurmukhambetova, Saule
Romer, Lewis H.
Garcia, Joe G.N.
2005
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Wadgaonkar, Raj
Dudek, Steven M.
Zaiman, Ari L.
Linz-McGillem, Laura
Verin, Alexander D.
Nurmukhambetova, Saule
Romer, Lewis H.
Garcia, Joe G.N.
Titel
Intracellular interaction of myosin light chain kinase with macrophage migration inhibition factor (MIF) in endothelium
Ist Teil von
Journal of cellular biochemistry, 2005-07, Vol.95 (4), p.849-858
Ort / Verlag
Hoboken: Wiley Subscription Services, Inc., A Wiley Company
Erscheinungsjahr
2005
Quelle
Wiley Online Library All Journals
Beschreibungen/Notizen
The endothelial cell Ca2+/calmodulin (CaM)‐dependent myosin light chain kinase isoform (EC MLCK) is a multifunctional contractile effector involved in vascular barrier regulation, leukocyte diapedesis, apoptosis, and angiogenesis. The EC MLCK isoform and its splice variants contain a unique N‐terminal sequence not present in the smooth muscle MLCK isoform (SM MLCK), which allows novel upregulation of MLCK activation by signaling cascades including p60src. The yeast two‐hybrid assay system using the entire EC MLCK1 N‐terminus (922 aa) as bait, identified additional stable MLCK binding partners including the 12 KDa macrophage migration inhibitory factor (MIF). This finding was confirmed by cross immunoprecipitation assays under non‐denaturing conditions and by GST pull down experiments using GST‐N‐terminal MLCK (#1–923) and MLCK N‐terminal deletion mutants in TNFα‐ and thrombin‐stimulated endothelium. This EC MLCK–MIF interaction was shown biochemically and by immunofluorescent microscopy to be enhanced in TNFα‐ and thrombin‐stimulated endothelium, both of which induce increased MLCK activity. Thrombin induced the colocalization of an epitope‐tagged, full‐length MIF fusion protein with phosphorylated MLC along peripheral actin stress fibers. Together these studies suggest that the novel interaction between MIF and MLCK may have important implications for the regulation of both non‐muscle cytoskeletal dynamics as well as pathobiologic vascular events that involve MLCK. © 2005 Wiley‐Liss, Inc.
Sprache
Englisch
Identifikatoren
ISSN: 0730-2312
eISSN: 1097-4644
DOI: 10.1002/jcb.20472
Titel-ID: cdi_proquest_miscellaneous_67920710
Format
–
Schlagworte
actin
,
Actins - metabolism
,
Amino Acid Sequence
,
Binding Sites
,
Cells, Cultured
,
cytoskeleton
,
Endothelium - metabolism
,
Humans
,
Macrophage Migration-Inhibitory Factors - chemistry
,
Macrophage Migration-Inhibitory Factors - genetics
,
Macrophage Migration-Inhibitory Factors - metabolism
,
Molecular Sequence Data
,
Myosin-Light-Chain Kinase - chemistry
,
Myosin-Light-Chain Kinase - genetics
,
Myosin-Light-Chain Kinase - metabolism
,
Protein Binding
,
Protein Structure, Tertiary
,
Saccharomyces cerevisiae
,
thrombin
,
TNF
,
Two-Hybrid System Techniques
,
Umbilical Cord - metabolism
,
yeast two-hybrid screening
Weiterführende Literatur
Empfehlungen zum selben Thema automatisch vorgeschlagen von
bX