Inhibition of human and mouse plasma membrane bound NTPDases by P2 receptor antagonists

2007 ◽  
Vol 74 (10) ◽  
pp. 1524-1534 ◽  
Author(s):  
Mercedes N. Munkonda ◽  
Gilles Kauffenstein ◽  
Filip Kukulski ◽  
Sébastien A. Lévesque ◽  
Charlène Legendre ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
P2 Receptor ◽  
Receptor Antagonists ◽  
Mouse Plasma ◽  
Membrane Bound ◽  
Human And Mouse

Exterior and Interior Events in Early Stage of Thrombin-induced Platelet Aggregation

1977 ◽  
Vol 38 (03) ◽  
pp. 0630-0639 ◽  
Author(s):  
Shuichi Hashimoto ◽  
Sachiko Shibata ◽  
Bonro Kobayashi
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Plasma Membrane ◽  
Platelet Aggregation ◽  
Early Stage ◽  
Adenyl Cyclase ◽  
Cellular Component ◽  
Primary Event ◽  
Rabbit Platelets ◽  
Membrane Bound

SummaryTreatment of washed rabbit platelets with 1 u/ml of thrombin at 37° C resulted in a disappearance from platelets of a protein with 250,000 dalton molecular weight which was shown to be originated from plasma membrane. Parallel loss of adenyl cyclase was noted, and both reactions were complete within 30 sec. From the patterns of disc electrophoretograms, the importance of quick suppression of thrombin action in demonstrating the primary event was stressed.Thrombin induced an apparent activation of membrane bound phosphodiesterase. This reaction was also complete within 30 sec. The cellular component which contained the enzyme activity was distinct from plasma membrane. Soluble phosphodiesterase was not influenced by thrombin at all.These reactions required intact platelet cells to react with thrombin, and no reaction was detected when subcellular preparations were treated with thrombin.Possibility of collaboration of changes in externally located synthetic enzyme with those in internally located degrading enzyme in the early phase of thrombin action on platelets was suggested.

scholarly journals PROBLEMS ASSOCIATED WITH THE DEMONSTRATION BY LEAD METHODS OF ADENOSINE TRIPHOSPHATASE ACTIVITY IN RESIDENT PERITONEAL MACROPHAGES AND EXUDATE MONOCYTES OF THE GUINEA PIG

1973 ◽  
Vol 21 (5) ◽  
pp. 488-498 ◽  
Author(s):  
R. E. POELMANN ◽  
W. T. DAEMS ◽  
E. J. VAN LOHUIZEN
Keyword(s):  
Plasma Membrane ◽  
Guinea Pig ◽  
Microscopic Study ◽  
Heterogeneous Nucleation ◽  
Adenosine Triphosphatase ◽  
Peritoneal Macrophages ◽  
Electron Microscopic ◽  
Adenosine Triphosphatase Activity ◽  
Eosinophilic Granulocytes ◽  
Membrane Bound

This cytochemical and electron microscopic study on peritoneal macrophages of the guinea pig has raised doubts concerning the validity of lead methods for the demonstration of plasma membrane-bound adenosine triphosphatase activity. The problems encountered are inherent in the use of lead ions as a capture reagent. The nonenzymatically formed precipitates reflect sites of heterogeneous nucleation specific for certain kinds of cells, e.g., resident peritoneal macrophages, eosinophilic granulocytes and, to a lesser degree, exudate monocytes. This type of precipitation is also catalyzed on the surface of nonbiologic matrices such as latex particles. Enzymatic processes may well occur, but they cannot be distinguished from nonenzymatic processes.

scholarly journals A constitutive, plasma-membrane bound β-glucosidase inTrichoderma reesei

1986 ◽  
Vol 34 (3) ◽  
pp. 291-295 ◽  
Author(s):  
Claudio Umile ◽  
Christian P. Kubicek
Keyword(s):  
Plasma Membrane ◽  
Membrane Bound

scholarly journals Very Cool Clathrin

2005 ◽  
Vol 13 (6) ◽  
pp. 3-7
Author(s):  
Stephen W. Carmichael
Keyword(s):  
Plasma Membrane ◽  
Coated Vesicles ◽  
Membrane Bilayer ◽  
Membrane Bound ◽  
Membranous Component

Clathrin-coated vesicles are the shuttle containers within cells. The vesicles carry lipids and proteins between membrane-bound compartments. Clathrin forms a cage-like structure around the membrane-bound vesicle that is pinched off from the plasma membrane (in endocytosis) or a membranous component of the cytoplasm. Clathrin recruits cargo that is within a vesicle through intermediary proteins known as adaptors that help select membrane-anchored protein and form an interface between the clathrin cage and the membrane bilayer.

scholarly journals A novel adenylylation process in liver plasma membrane-bound proteins

1990 ◽  
Vol 265 (33) ◽  
pp. 20653-20661
Author(s):  
E San José ◽  
A Benguría ◽  
A Villalobo
Keyword(s):  
Plasma Membrane ◽  
Liver Plasma Membrane ◽  
Membrane Bound

The heterotrimeric Gi(3) protein acts in slow but not in fast exocytosis of rat melanotrophs

1999 ◽  
Vol 112 (22) ◽  
pp. 4143-4150 ◽  
Author(s):  
M. Kreft ◽  
S. Gasman ◽  
S. Chasserot-Golaz ◽  
V. Kuster ◽  
M. Rupnik ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
G Proteins ◽  
Flash Photolysis ◽  
Secretory Granules ◽  
Secretory Activity ◽  
Α Subunit ◽  
Capacitance Measurements ◽  
Regulated Secretion ◽  
Kinetic Component ◽  
Membrane Bound

Besides having a role in signal transduction some trimeric G-proteins may be involved in a late stage of exocytosis. Using immunocytochemistry and confocal microscopy we found that Gi(3)-protein resides mainly in the plasma membrane, whereas Gi(1/2-)protein is preferentially associated with secretory granules. To study the function of trimeric Gi(3)- and Gi(1/2)-proteins, secretory responses in single rat melanotrophs were monitored by patch-clamp membrane capacitance measurements. We report here that mastoparan, an activator of trimeric G-proteins, enhances calcium-induced secretory activity in rat melanotrophs. The introduction of synthetic peptides corresponding to the C-terminal domain of the (α)-subunit of Gi(3)- and Gi(1/2)-proteins indicated that Gi(3)peptide specifically blocked the mastoparan-stimulated secretory activity, which indicates an involvement of a trimeric Gi(3)-protein in mastoparan-stimulated secretory activity. Flash photolysis of caged Ca(2+)-elicited biphasic capacitance increases consisting of a fast and a slower component. Injection of anti-Gi(3) antibodies selectively inhibited the slow but not the fast component of secretory activity in rat melanotrophs. We propose that the plasma membrane-bound Gi(3)-protein may be involved in regulated secretion by specifically controlling the slower kinetic component of exocytosis.

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