Probing glycation potential of dietary sugars in human blood by an integrated in vitro approach

2020 ◽  
pp. 128951
Author(s):  
Nadezhda Frolova ◽  
Alena Soboleva ◽  
Viet Duc Nguyen ◽  
Ahyoung Kim ◽  
Christian Ihling ◽  
...  
Keyword(s):  
1974 ◽  
Vol 32 (02/03) ◽  
pp. 266-276
Author(s):  
Carl D. Jacobsen ◽  
John C. Hoak ◽  
Kenneth K. WU ◽  
Glenna L. Fry
Keyword(s):  

SummaryIn serum from patients with DIC at least 3 different FR-antigenic components could be found. It was difficult to demonstrate these components in the corresponding plasma samples. It is possible that a portion of these antigens formed as a result of in vitro clotting despite the presence of proteolytic inhibitors. These results suggest that the interpretation of “increased split products in serum” may be more complex than current concepts indicate.


1973 ◽  
Vol 30 (03) ◽  
pp. 494-498 ◽  
Author(s):  
G de Gaetano ◽  
J Vermylen

SummaryThrombelastograms of both native blood and re-calcified platelet-rich plasma samples taken from subjects given a single oral dose of aspirin (1 gram) were not significantly different from the pretreatment recordings. Aspirin also did not modify the thrombelastogram when preincubated in vitro with platelet-rich plasma at concentrations inhibiting the platelet “release reaction” by collagen. Thrombelastography therefore cannot evaluate the effect of aspirin on platelet function.


1973 ◽  
Vol 29 (03) ◽  
pp. 694-700 ◽  
Author(s):  
Paul L. Rifkin ◽  
Marjorie B. Zucker

SummaryDipyridamole (Persantin) is reported to prolong platelet survival and inhibit embolism in patients with prosthetic heart valves, but its mechanism of action is unknown. Fifty jxM dipyridamole failed to reduce the high percentage of platelets retained when heparinized human blood was passed through a glass bead column, but prolonged the inhibition of retention caused by disturbing blood in vitro. Possibly the prostheses act like disturbance. Although RA 233 was as effective as dipyridamole in inhibiting the return of retention, it was less effective in preventing the uptake of adenosine into erythrocytes, and more active in inhibiting ADP-induced aggregation and release. Thus there is no simple relation between these drug effects.


1963 ◽  
Vol 18 (5) ◽  
pp. 955-958 ◽  
Author(s):  
S. H. Blondheim ◽  
Gabriel Neumann ◽  
Edna Kott ◽  
Zena Ben-Ishai

The ability of human blood to acetylate p-aminobenzoic acid, determined in vitro, varied directly with the ambient temperature to which the subject was exposed before the blood was drawn. This was demonstrated by 135 determinations of the acetylating ability of the blood of 49 subjects performed over a period of 3 years, and also in acute experiments in which subjects were exposed to 6 and 37 C for up to 2 hr. Variations in the acetylating ability of blood may reflect the activity of metabolic mechanisms involved in thermal homeostasis. aromatic amines; p-aminobenzoic acid; cold; heat acclimatization; (blood) enzymes; weather; environment Submitted on September 11, 1962


1989 ◽  
Vol 7 (2) ◽  
pp. 123-128 ◽  
Author(s):  
Jerry L. Phllips ◽  
Rowena Schwartz ◽  
Daniel D. Von Hoff

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