Evidence for the involvement of plasma-membrane-bound nitrate reductase in signal transduction during blue-light stimulation of nitrate uptake in Chlorella saccharophila

Planta ◽  
1995 ◽  
Vol 197 (4) ◽  
Author(s):  
Christine St�hr ◽  
Ulrich Glogau ◽  
Michael M�tschke ◽  
Rudolf Tischner
Keyword(s):  
Signal Transduction ◽  
Plasma Membrane ◽  
Nitrate Reductase ◽  
Blue Light ◽  
Nitrate Uptake ◽  
Light Stimulation ◽  
Chlorella Saccharophila ◽  
Membrane Bound ◽  
Stimulation Of

Evidence for a plasma-membrane-bound nitrate reductase involved in nitrate uptake of Chlorella sorokiniana

Planta ◽  
1989 ◽  
Vol 178 (1) ◽  
pp. 19-24 ◽  
Author(s):  
R. Tischner ◽  
M. R. Ward ◽  
R. C. Huffaker
Keyword(s):  
Plasma Membrane ◽  
Nitrate Reductase ◽  
Nitrate Uptake ◽  
Chlorella Sorokiniana ◽  
Membrane Bound

Characterization of the plasma-membrane-bound nitrate reductase in Chlorella saccharophila (Kr�ger) Nadson

Planta ◽  
1993 ◽  
Vol 191 (1) ◽  
Author(s):  
Christine St�hr ◽  
Rudolf Tischner ◽  
MichaelR. Ward
Keyword(s):  
Plasma Membrane ◽  
Nitrate Reductase ◽  
Chlorella Saccharophila ◽  
Membrane Bound

Phosphorylation of liver plasma membrane-bound calmodulin

1988 ◽  
Vol 66 (8) ◽  
pp. 922-927 ◽  
Author(s):  
Shobha Ghosh ◽  
Jon G. Church ◽  
Basil D. Roufogalis ◽  
Antonio Villalobo
Keyword(s):  
Plasma Membrane ◽  
Calcium Ion ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein Band ◽  
Bovine Brain ◽  
Antibody Treatment ◽  
Liver Plasma Membrane ◽  
Phosphate Donor ◽  
Membrane Bound ◽  
Stimulation Of

In highly purified rat liver plasma membrane preparations, membrane-bound calmodulin was phosphorylated by a membrane-bound protein kinase using [γ-32P] ATP as phosphate donor. Maximum phosphorylation of calmodulin occurred in the absence of calcium ion, but was significantly decreased in its presence. Plasma membrane-bound calmodulin was identified by the following criteria: (i) extraction from the membrane by EGTA, (ii) stimulation of the activity of the Ca2+-calmodulin-dependent enzyme, (3′:5′ AMP)-phosphodiesterase, by the EGTA extract, and (iii) electrophoretic comigration of EGTA-extracted protein with standard bovine brain calmodulin, both in the presence and the absence of Ca2+. Phosphorylation of the plasma membrane-bound calmodulin was shown by electrophoretic comigration of the 32P-labelled molecule with bovine brain calmodulin, the absence of phosphorylation of this protein band in calmodulin-depleted membranes, and a Western blot of the phosphorylated band using a calmodulin antibody. Treatment of plasma membrane preparations with sheep anticalmodulin serum prevented the phosphorylation of the calmodulin band. Phosphocalmodulin, which could be partially extracted from the membrane by EGTA, comigrated with bovine brain calmodulin in polyacrylamide gel electrophoresis.

scholarly journals Integrin-associated protein: a 50-kD plasma membrane antigen physically and functionally associated with integrins.

1990 ◽  
Vol 111 (6) ◽  
pp. 2785-2794 ◽  
Author(s):  
E Brown ◽  
L Hooper ◽  
T Ho ◽  
H Gresham
Keyword(s):  
Signal Transduction ◽  
Plasma Membrane ◽  
Synthetic Peptides ◽  
Plasma Membranes ◽  
Protein A ◽  
Hematopoietic Cells ◽  
Cell Types ◽  
Cell Biol ◽  
Leukocyte Response ◽  
Stimulation Of

Phagocytosis by monocytes or neutrophils can be enhanced by interaction with several proteins or synthetic peptides containing the Arg-Gly-Asp sequence. Recently we showed that an mAb, B6H12, specifically inhibited this enhancement of neutrophil phagocytosis by inhibiting Arg-Gly-Asp binding to the leukocyte response integrin (Gresham, H. D., J. L. Goodwin, P. M. Allen, D. C. Anderson, and E. J. Brown. 1989. J. Cell Biol. 108:1935-1943). Now, we have purified the antigen recognized by B6H12 to homogeneity. Surprisingly, it is a 50-kD molecule that is expressed on the plasma membranes of all hematopoietic cells, including erythrocytes, which express no known integrins. On platelets and placenta, but not on erythrocytes, this protein is associated with an integrin that can be recognized by an anti-beta 3 antibody. In addition, both the anti-beta 3 and several mAbs recognizing the 50-kD protein inhibit Arg-Gly-Asp stimulation of phagocytosis. These data demonstrate an association between integrins and the 50-kD protein on several cell types. For this reason, we call it Integrin-associated Protein (IAP). We hypothesize that IAP may play a role in signal transduction for enhanced phagocytosis by Arg-Gly-Asp ligands.

Kinetic characterization of succinate-dependent plasma membrane-bound nitrate reductase in tobacco roots 1

1999 ◽  
Vol 105 (4) ◽  
pp. 609-614 ◽  
Author(s):  
Stefanie Wienkoop ◽  
Wolfram R Ullrich ◽  
Christine Stöhr
Keyword(s):  
Plasma Membrane ◽  
Nitrate Reductase ◽  
Kinetic Characterization ◽  
Membrane Bound ◽  
Tobacco Roots
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