1211-P: No Significant Change of Glucagon Level by Empagliflozin in Diabetic Mice

Diabetes ◽  
2019 ◽  
Vol 68 (Supplement 1) ◽  
pp. 1211-P
Author(s):  
HIROMI SHIMODA ◽  
YUSUKE SEINO ◽  
TATSUHITO HIMENO ◽  
RIEKO INOUE ◽  
MIKIO MOTEGI ◽  
...  
2011 ◽  
Vol 81 (1) ◽  
pp. 34-42 ◽  
Author(s):  
Joel Deneau ◽  
Taufeeq Ahmed ◽  
Roger Blotsky ◽  
Krzysztof Bojanowski

Type II diabetes is a metabolic disease mediated through multiple molecular pathways. Here, we report anti-diabetic effect of a standardized isolate from a fossil material - a mineraloid leonardite - in in vitro tests and in genetically diabetic mice. The mineraloid isolate stimulated mitochondrial metabolism in human fibroblasts and this stimulation correlated with enhanced expression of genes coding for mitochondrial proteins such as ATP synthases and ribosomal protein precursors, as measured by DNA microarrays. In the diabetic animal model, consumption of the Totala isolate resulted in decreased weight gain, blood glucose, and glycated hemoglobin. To our best knowledge, this is the first description ever of a fossil material having anti-diabetic activity in pre-clinical models.


Author(s):  
Cynthia L. Ogden ◽  
Margaret D. Carroll ◽  
Margaret A. McDowell ◽  
Katherine M. Flegal

1992 ◽  
Vol 67 (01) ◽  
pp. 060-062 ◽  
Author(s):  
J Harsfalvi ◽  
E Tarcsa ◽  
M Udvardy ◽  
G Zajka ◽  
T Szarvas ◽  
...  

Summaryɛ(γ-glutamyl)lysine isodipeptide has been detected in normal human plasma by a sensitive HPLC technique in a concentration of 1.9-3.6 μmol/1. Incubation of in vitro clotted plasma at 37° C for 12 h resulted in an increased amount of isodipeptide, and there was no further significant change when streptokinase was also present. Increased in vivo isodipeptide concentrations were also observed in hypercoagulable states and during fibrinolytic therapy.


1961 ◽  
Vol 06 (03) ◽  
pp. 498-503 ◽  
Author(s):  
W Doleschel ◽  
W Auerswald

SummaryDuring “spontaneous” activation of a human euglobulin preparation in suitably spaced samples — while plasminogen became progressively converted into piasmin — the proactivator content was tested by addition of equal amounts of streptokinase and evaluation of the lytic activities on heated and normal bovine fibrin plates. Indepedently of the decreasing content of plasminogen the proactivator which could be activated by streptokinase showed no significant change of concentration. These observation indicate that plasminogen is not acting as proactivator and that there exists a separate proactivator-activator system of the fibrinolytic mechanism in human serum.


Sign in / Sign up

Export Citation Format

Share Document