scholarly journals Cyclic 3′,5′-adenosine monophosphate in human blood platelets. II. Effect of N6-2′-o-dibutyryl cyclic 3′,5′-adenosine monophosphate on platelet function

1972 ◽  
Vol 51 (7) ◽  
pp. 3f-3f
Keyword(s):  
Platelet Function ◽  
Human Blood ◽  
Blood Platelets ◽  
Adenosine Monophosphate ◽  
Human Blood Platelets

Cyclic 3′,5′-Adenosine Monophosphate in Human Blood Platelets

Nature ◽  
1969 ◽  
Vol 224 (5219) ◽  
pp. 609-610 ◽  
Author(s):  
EDWIN W. SALZMAN ◽  
LENA L. NERI
Keyword(s):  
Human Blood ◽  
Blood Platelets ◽  
Adenosine Monophosphate ◽  
Human Blood Platelets

scholarly journals Cyclic 3′,5′-adenosine monophosphate in human blood platelets

1971 ◽  
Vol 50 (1) ◽  
pp. 131-141 ◽  
Author(s):  
Edwin W. Salzman ◽  
Linda Levine
Keyword(s):  
Human Blood ◽  
Blood Platelets ◽  
Adenosine Monophosphate ◽  
Human Blood Platelets

scholarly journals Surface membrane clearing of receptor-ligand complexes in human blood platelets

1987 ◽  
Vol 87 (3) ◽  
pp. 465-472
Author(s):  
O. Behnke
Keyword(s):  
Human Blood ◽  
Blood Platelets ◽  
Surface Membrane ◽  
Adenosine Monophosphate ◽  
Membrane System ◽  
Intercellular Spaces ◽  
Platelet Antibodies ◽  
Internalization Process ◽  
Human Blood Platelets

Human blood platelets were challenged sequentially in vitro with polyclonal anti-platelet antibodies and cationized ferritin. Both ligands bound to the surface membrane and were sequestered by internalization into a surface-connected membrane system (SCS) with a cleared surface membrane as the eventual result. Patching and capping of bound antibody preceded internalization, and platelets cooperated in the clearing process by adhering to each other at capped areas and by mutual covering up, a process dubbed platelet hugging. The internalization process was repeated upon challenge with the second ligand, the two ligands being sequestered as separate deposits in the SCS, mirroring the two cycles of internalization. Platelets were activated during internalization process and tended to aggregate. In aggregates, surfaces exposed to the medium were cleared of ligand, which accumulated in the intercellular spaces and within the SCS of the aggregated platelets. Aggregation but not internalization and hugging was prevented by adenosine and adenosine monophosphate.

On the Mechanism by which Cell Contact Induces the Release Reaction of Blood Platelets; the Effect of Cationic Polymers

1972 ◽  
Vol 27 (01) ◽  
pp. 121-133 ◽  
Author(s):  
P Massini ◽  
E. F Lüscher
Keyword(s):  
Human Blood ◽  
Calcium Ions ◽  
Blood Platelets ◽  
Cell Contact ◽  
Second Phase ◽  
Cationic Polymers ◽  
Release Reaction ◽  
Per Se ◽  
Human Blood Platelets

SummaryHuman blood platelets are aggregated by the basic polymers polylysine and DEAE- dextran. Under certain conditions a second phase of aggregation, concomitant with the release reaction, is elicited. The presence of ADP, calcium ions and a plasmatic cofactor within the primary aggregates are necessary for the induction of the release reaction. These experiments demonstrate that cell contact per se does not lead to a release reaction ; in order to become effective it must take place in the presence of ADP.

Chromatographic Isolation of the LDH-Isoenzymes of Human Blood Platelets and an Investigation of Their Enzyme Kinetics

1968 ◽  
Vol 20 (03/04) ◽  
pp. 301-313 ◽  
Author(s):  
W Schneider ◽  
K Schumacher ◽  
B Thiede ◽  
R Gross
Keyword(s):  
Human Blood ◽  
Blood Platelets ◽  
Deae Cellulose ◽  
Order Reaction ◽  
Kinetic Properties ◽  
Ldh Isoenzymes ◽  
Kinetic Investigations ◽  
Substrate Concentrations ◽  
Chromatographic Isolation ◽  
Human Blood Platelets

SummaryThe LDH-isoenzymes of human blood platelets show a distinct predominance of the isoenzymes 2 and 3 upon chromatography on DEAE-cellulose. Small amounts of LDH-1 are also present, while only traces of LDH-4 and -5 can be detected.Enzyme kinetic investigations of the principal isoenzymes LDH-1, -2 and -3 clearly show that the differences in inhibition constants with pyruvate as substrate which are demonstrable at 25° largely disappear at 37°. On the other hand, the differences among the isoenzymes in their affinity for pyruvate and lactate as substrate as well as in with respect to the optimal substrate concentrations of pyruvate are more marked at 37° than at 25°. Also, the type of inhibition found with lactate as substrate is increasingly the expression of a higher order reaction in going from LDH-1 to LDH-3. A dependence of the LDH distribution pattern upon the metabolism of the cell is discussed. A comparison of our results with thrombocytes with those of other workers with erythrocytes and leucocytes makes it unlikely that the LDH pattern is directly dependent upon the existence of an oxidative metabolism. Rather, the redox potential of the cell could be of importance for the nature of the pattern of isoenzymes and for their differing kinetic properties.

Interaction of Vasopressin with Human Blood Platelets: Dependency on Mg2+

1986 ◽  
Vol 56 (03) ◽  
pp. 260-262 ◽  
Author(s):  
Isabella Roos ◽  
Fabrizia Ferracin ◽  
Alfred Pletscher
Keyword(s):  
Phosphatidic Acid ◽  
Human Blood ◽  
Arginine Vasopressin ◽  
Specific Binding ◽  
Blood Platelets ◽  
Bivalent Cations ◽  
Platelet Membranes ◽  
Maximal Rise ◽  
Human Blood Platelets ◽  
Stimulation Of

SummaryArginine-vasopressin (AVP) in the presence of Mg2+ but not in the absence of bivalent cations led to accumulation of [32P]-phosphatidic acid ([32P]-PA) in human blood platelets. Mg2+ also enhanced the specific binding of [3H]-AVP to intact platelets. The concentrations of the cation which enabled AVP to cause half maximal rise of [32P]-PA and those inducing half maximal [3H]-AVP-binding were of the same order. It is concluded that the stimulation of phosphatidyl inositide breakdown by AVP in presence of Mg2+ is at least partially due to a Mg2+-induced enhancement of specific AVP-binding to the platelet membranes.

Benzalkonium chloride interferes with energy production, secretion and morphology in human blood platelets

Platelets ◽  
1999 ◽  
Vol 10 (2) ◽  
pp. 97-104 ◽  
Author(s):  
Ø. Berg ◽  
A. M. Bakken ◽  
S. K. Steinsvåg ◽  
M. Farstad
Keyword(s):  
Human Blood ◽  
Benzalkonium Chloride ◽  
Energy Production ◽  
Blood Platelets ◽  
Human Blood Platelets
Sign in / Sign up

Export Citation Format

Share Document