scholarly journals The Interactions of Hepatocyte Growth Factor/Scatter Factor and Its NK1 and NK2 Variants with Glycosaminoglycans Using a Modified Gel Mobility Shift Assay

2004 ◽  
Vol 279 (42) ◽  
pp. 43560-43567 ◽  
Author(s):  
Malcolm Lyon ◽  
Jon A. Deakin ◽  
Daniel Lietha ◽  
Ermanno Gherardi ◽  
John T. Gallagher
1995 ◽  
Vol 270 (2) ◽  
pp. 830-836 ◽  
Author(s):  
Antje Plaschke-Schlütter ◽  
Jürgen Behrens ◽  
Ermanno Gherardi ◽  
Walter Birchmeier

1997 ◽  
Vol 185 (12) ◽  
pp. 2121-2131 ◽  
Author(s):  
Robbert van der Voort ◽  
Taher E.I. Taher ◽  
Robert M.J. Keehnen ◽  
Lia Smit ◽  
Martijn Groenink ◽  
...  

T cell–dependent humoral immune responses are initiated by the activation of naive B cells in the T cell areas of the secondary lymphoid tissues. This primary B cell activation leads to migration of germinal center (GC) cell precursors into B cell follicles where they engage follicular dendritic cells (FDC) and T cells, and differentiate into memory B cells or plasma cells. Both B cell migration and interaction with FDC critically depend on integrin-mediated adhesion. To date, the physiological regulators of this adhesion were unkown. In the present report, we have identified the c-met–encoded receptor tyrosine kinase and its ligand, the growth and motility factor hepatocyte growth factor/scatter factor (HGF/SF), as a novel paracrine signaling pathway regulating B cell adhesion. We observed that c-Met is predominantly expressed on CD38+CD77+ tonsillar B cells localized in the dark zone of the GC (centroblasts). On tonsil B cells, ligation of CD40 by CD40-ligand, induces a transient strong upregulation of expression of the c-Met tyrosine kinase. Stimulation of c-Met with HGF/SF leads to receptor phosphorylation and, in addition, to enhanced integrin-mediated adhesion of B cells to both VCAM-1 and fibronectin. Importantly, the c-Met ligand HGF/SF is produced at high levels by tonsillar stromal cells thus providing signals for the regulation of adhesion and migration within the lymphoid microenvironment.


2001 ◽  
Vol 159 (2) ◽  
pp. 579-590 ◽  
Author(s):  
Glenn A. Gmyrek ◽  
Marc Walburg ◽  
Craig P. Webb ◽  
Hsiao-Man Yu ◽  
Xueke You ◽  
...  

1994 ◽  
Vol 103 (3) ◽  
pp. 306-309 ◽  
Author(s):  
Toshimasa Jindo ◽  
Ryoji Tsuboi ◽  
Ryusuke Imai ◽  
Kenji Takamori ◽  
Jeffrey S Rubin ◽  
...  

2000 ◽  
Vol 14 (2) ◽  
pp. 319-332 ◽  
Author(s):  
Gerd Lindner ◽  
Andreas Menrad ◽  
Ermanno Gherardi ◽  
Glenn Merlino ◽  
Pia Welker ◽  
...  

1999 ◽  
Vol 251 (1) ◽  
pp. 3-15 ◽  
Author(s):  
Steven M. DeLuca ◽  
Jacquelyn Gerhart ◽  
Eric Cochran ◽  
Eileen Simak ◽  
Jennifer Blitz ◽  
...  

1995 ◽  
Vol 42 (2) ◽  
pp. 171-176
Author(s):  
R Rzepecki ◽  
E Markiewicz ◽  
J Szopa

The nuclear matrices from White bush (Cucurbita pepo var. patisonina) cell nuclei have been isolated using three methods: I, standard procedure involving extraction of cell nuclei with 2 M NaCl and 1% Triton X-100; II, the same with pre-treatment of cell nuclei with 0.5 mM CuSO4 (stabilisation step); and III, method with extraction by lithium diiodosalicylate (LIS), and compared the polypeptide pattern. The isolated matrices specifically bind SAR DNA derived from human beta-interferon gene in the exogenous SAR binding assay and in the gel mobility shift assay. Using IgG against the 32 kDa endonuclease we have found in the DNA-protein blot assay that this protein is one of the proteins binding SAR DNA. We have identified three proteins with molecular mass of 65 kDa, 60 kDa and 32 kDa which are responsible for SAR DNA binding in the gel mobility shift assay experiments.


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