Comparison of Normal and Thrombasthenic Human Blood Platelets

Author(s):  
N. F. Rodman ◽  
J. C. Painter ◽  
R. G. Mason

The ultrastructure of normal human blood platelets in the resting state has been described in detail. Platelets recovered from citrated plasma of a patient with Glanzmann's thrombopathy or thrombasthenia have a similar appearance (Fig. 1). These anucleate cells are usually disc shaped and hence are round or oval, depending upon the plane of sectioning. They have randomly dispersed cytoplasmic organelles and microtubules which are typically arranged in a marginal band.Platelet responses to several agglutinating agents and the relation of platelets to fibrin during clotting have been reported. On exposure to thrombin, to ADP, or to collagen, normal and thrombasthenic platelets undergo similar early morphologic changes. Pseudopods form and organelles move toward platelet centers, with microtubules being outermost of the closely packed, centrally apposed organelles. A peripheral rim of cytoplasm is essentially organelle-free except for an occasional mitochondrion or vacuole and except for microtubules which sometimes extend outward into pseudopods. Following these early, preagglutination changes normal platelets agglutinate in response to each of the 3 agglutinating agents, whether in autologous plasma or in salt solution after repeated washings. Thrombasthenic platelets in autologous plasma fail to agglutinate in response to thrombin or to ADP and agglutinate only minimally on exposure to finely divided collagen.

1975 ◽  
Vol 33 (02) ◽  
pp. 341-353
Author(s):  
W Schneider ◽  
R Gross

SummaryTwo MDH isoenzymes were detected in the homogenate of normal human blood platelets. According to their properties the cationic isoenzyme is compartmentalized in the mitochondria, the anionic one belongs to the cytoplasma. In spite of the few mitochondria in human blood platelets the proportion of the cationic enzyme is relatively high.Both of these enzymes could belong to a transfer system for malate transport across the mitochondrial membrane. As human blood platelets do not contain creatine phosphate a system like that could be of significance for platelet function.


1974 ◽  
Vol 52 (2) ◽  
pp. 245-251 ◽  
Author(s):  
LISA AHTEE ◽  
D.J. BOULLIN ◽  
M.K. PAASONEN

Blood ◽  
1978 ◽  
Vol 52 (1) ◽  
pp. 57-67 ◽  
Author(s):  
LC Andersson ◽  
CG Gahmberg

Abstract We labeled surface glycoproteins of normal human blood platelets, granulocytes, monocytes, T and B lymphocytes, and null cells by the galactose oxidase-NaB3H4 and periodate-NaB3H4 labeling techniques. The labeled glycoproteins were observed by fluorography after separation by polyacrylamide slab gel electrophoresis. All major types of human leukocytes showed different and characteristic surface glycoprotein patterns. These patterns evidently also include common components.


Blood ◽  
1958 ◽  
Vol 13 (8) ◽  
pp. 773-777 ◽  
Author(s):  
J. GUREVITCH ◽  
D. NELKEN ◽  
D. DANON

Abstract Phase contrast and electron microscopic studies on the morphologic changes of platelets in various hypotonic salt solutions are presented.


1960 ◽  
Vol 8 (1) ◽  
pp. 61-67 ◽  
Author(s):  
G. Adolph Ackerman

Endogenous and succinic dehydrogenase activity was demonstrated in the living cells of normal human blood and bone marrow using a buffered nitro BT-succinate incubating solution. With this technique dehydrogenase activity was localized primarily in the granular leukocytes and the sites of enzymatic activity appeared to be non-mitochondrial. The addition of a non-ionic surface active agent to the incubating solution resulted in marked differences in the cellular and intracellular localization of dehydrogenase activity. With this method it was possible to demonstrate dehydrogenase activity in the mitochondria of most of the formed elements of the blood and bone marrow, including developing granulocytes and erythroid cells, agranulocytes, and blood platelets. Mature erythrocytes also exhibited a minimal dehydrogenase reaction with this procedure. This investigation indicated that in order adequately to demonstrate and evaluate dehydrogenase activity in the cells of the blood and bone marrow it was necessary to have increased cellular and mitochondrial permeability, as well as partially viable cells with an intact dehydrogenase system.


Blood ◽  
1978 ◽  
Vol 52 (1) ◽  
pp. 57-67 ◽  
Author(s):  
LC Andersson ◽  
CG Gahmberg

We labeled surface glycoproteins of normal human blood platelets, granulocytes, monocytes, T and B lymphocytes, and null cells by the galactose oxidase-NaB3H4 and periodate-NaB3H4 labeling techniques. The labeled glycoproteins were observed by fluorography after separation by polyacrylamide slab gel electrophoresis. All major types of human leukocytes showed different and characteristic surface glycoprotein patterns. These patterns evidently also include common components.


1972 ◽  
Vol 27 (01) ◽  
pp. 121-133 ◽  
Author(s):  
P Massini ◽  
E. F Lüscher

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.


1968 ◽  
Vol 20 (03/04) ◽  
pp. 301-313 ◽  
Author(s):  
W Schneider ◽  
K Schumacher ◽  
B Thiede ◽  
R Gross

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.


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