Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Friederike Pausch"'
Publikováno v:
Histochemistry and Cell Biology. 145:511-525
Activation of endothelial cells and recruitment of mural cells define critical steps during the formation of stable vascular elements. Both events are reflected by cocultures of endothelial cells and isolated murine pericyte-like cells and define a v
Publikováno v:
Histochemistry and Cell Biology. 145:527-529
Deletion of beta catenin in hypertrophic growth plate chondrocytes impairs trabecular bone formation
Autor:
Britta Schlund, Sonja Gebhard, Takako Hattori, Andreas Hess, Klaus von der Mark, Svitlana Golovchenko, Christine Hartmann, Matthias Gebhardt, Friederike Pausch
Publikováno v:
Bone. 55:102-112
In order to elucidate the role of β-catenin in hypertrophic cartilage zone of the growth plate, we deleted the β-catenin gene ctnnb1 specifically from hypertrophic chondrocytes by mating ctnnb1 fl/fl mice with BAC-Col10a1-Cre -deleter mice. Surp
Autor:
Michael R. Bösl, Benoit de Crombrugghe, Eva Bauer, Helga von der Mark, Britta Schlund, Takako Hattori, Sonja Gebhard, Cordula Surmann-Schmitt, Andreas Hess, Friederike Pausch, Catharina Müller, Klaus von der Mark
Publikováno v:
Development. 137:901-911
SOX9 is a transcription factor of the SRY family that regulates sex determination, cartilage development and numerous other developmental events. In the foetal growth plate, Sox9 is highly expressed in chondrocytes of the proliferating and prehypertr
Autor:
John F. Bateman, Friederike Pausch, Bent Brachvogel, Peter G. Farlie, Zhigang Zhou, Ernst Pöschl, Julia Etich, Trevor L. Cameron, Udo S. Gaipl, Klaus von der Mark
Publikováno v:
Experimental Cell Research. 313:2730-2743
Pericytes are closely associated with endothelial cells, contribute to vascular stability and represent a potential source of mesenchymal progenitor cells. Using the specifically expressed annexin A5-LacZ fusion gene (Anxa5-LacZ), it became possible
Autor:
Friederike Pausch, Wolfgang Baum, Klaus von der Mark, Udo S. Gaipl, Ernst Pöschl, Martin Herrmann, Franz Rödel, Ruediger B Mueller, Bent Brachvogel, Benjamin Frey, Luis E. Muñoz
Publikováno v:
Current Medicinal Chemistry. 14:271-277
Annexins are characterized by the ability to bind phospholipids of membranes in the presence of Ca2+. Annexin A5 represents a typical member of this protein family and is a natural occurring highly specific ligand for phosphatidylserine (PS). The exp
Autor:
Ahmed Sheriff, Friederike Pausch, Bent Brachvogel, Udo S. Gaipl, Luis E. Muñoz, Ernst Pöschl, Sandra Franz, Dorothee von Laer, Peter Kern, Christian Stach, Birgit Vogt, Martin Herrmann, Wolfgang Baum, Barbara G. Fürnrohr
Publikováno v:
Journal of Leukocyte Biology. 81:6-14
Apoptotic and necrotic cells expose phosphatidylserine (PS). This membrane modification ensures a swift recognition and uptake by phagocytes of the dying and dead cells. Annexin V (AxV) preferentially binds to anionic phospholipids and thereby, modul
Autor:
Friederike Pausch, Thomas Winkler, Bent Brachvogel, Ernst Pöschl, Rupert Hallmann, Klaus von der Mark, Ursula Schlötzer-Schrehardt, Clementine Hofmann, Helga Moch
Publikováno v:
Development. 132:2657-2668
The annexin A5 gene ( Anxa5 ) was recently found to be expressed in the developing and adult vascular system as well as the skeletal system. In this paper, the expression of an Anxa5 - lacZ fusion gene was used to define the onset of expression in th
Autor:
Rupert Hallmann, Olaf Wendler, Friederike Pausch, Lydia Sorokin, Britta Engelhardt, Michael Sixt
Publikováno v:
The Journal of Cell Biology
An active involvement of blood–brain barrier endothelial cell basement membranes in development of inflammatory lesions in the central nervous system (CNS) has not been considered to date. Here we investigated the molecular composition and possible
Autor:
Michael Frieser, Friederike Pausch, Stephan Kröger, E. Ohage, Rainer Deutzmann, Lydia Sorokin
Publikováno v:
Developmental Biology. 189:285-300
We have previously shown that mouse and bovine endothelial cells express a novel 400-kDa laminin alpha chain complexed to beta1 and gamma1 laminin chains. We describe here purification of this laminin isoform from the conditioned medium of a mouse pe