Evaluation of Apigenin Inhibiting Lactate Dehydrogenase Activity Based on CdTe Quantum Dots Fluorescence

2021 ◽  
Vol 17 (9) ◽  
pp. 1806-1811
Author(s):  
Xiangling Ren ◽  
Meijia Liu ◽  
Ming Tang ◽  
Longfei Tan ◽  
Changhui Fu ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Enzyme Inhibitors ◽  
Cell Metabolism ◽  
Critical Role ◽  
Enzyme Reaction ◽  
Sodium Oxalate ◽  
Lactate Dehydrogenase Activity ◽  
Metabolism Pathway ◽  
Metabolism Inhibition ◽  
Glycolysis Process

Lactate dehydrogenase (LDH) is one of key enzymes in glucose metabolism pathway, which plays a critical role in cell metabolism. Inhibition of LDH can inhibit glycolysis process, thereby inhibiting the occurrence and development of tumor cells. Two kinds of LDH inhibitors, apigenin and emodin, were obtained by testing the IC50 of several natural products in LDH enzyme reaction. The IC50 of apigenin was about 1/3 of LDH inhibitor sodium oxalate. A new method to evaluate the performance of LDH inhibitors based on CdTe QDs was established at the same time, which provides a new idea for research on LDH enzyme inhibitors.

Lactate dehydrogenase activity and its isoenzymes in concentric layers of adult bovine and calf lenses

1987 ◽  
Vol 6 (4) ◽  
pp. 555-560 ◽  
Author(s):  
David Sempol ◽  
Edurado Osinaga ◽  
Seymour Zigman ◽  
Israel Korc ◽  
Beatriz Korc ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Lactate Dehydrogenase Activity

Lactate Dehydrogenase Activity is Inhibited by Methylmalonate in vitro

2006 ◽  
Vol 31 (4) ◽  
pp. 541-548 ◽  
Author(s):  
Laura O. Saad ◽  
Sandra R. Mirandola ◽  
Evelise N. Maciel ◽  
Roger F. Castilho
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Lactate Dehydrogenase Activity

scholarly journals CSF Lactate Dehydrogenase Activity in Patients with Creutzfeldt-Jakob Disease Exceeds That in Other Dementias

2004 ◽  
Vol 17 (3) ◽  
pp. 204-206 ◽  
Author(s):  
H. Schmidt ◽  
M. Otto ◽  
P. Niedmann ◽  
L. Cepek ◽  
A. Schröter ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Lactate Dehydrogenase Activity ◽  
Csf Lactate ◽  
Jakob Disease

Improved column method for separating lactate dehydrogenase isoenzymes 1 and 2.

1978 ◽  
Vol 24 (3) ◽  
pp. 480-482 ◽  
Author(s):  
D W Mercer
Keyword(s):  
Myocardial Infarction ◽  
Acute Myocardial Infarction ◽  
Creatine Kinase ◽  
Heart Disease ◽  
Lactate Dehydrogenase ◽  
Sodium Chloride ◽  
Lactate Dehydrogenase Activity ◽  
Column Method ◽  
Creatine Kinase Mb ◽  
Lactate Dehydrogenase Isoenzymes

Abstract Lactate dehydrogenase (LD) isoenzymes 1 and 2 in human serum were separated on a column of diethylaminoethyl-Sephadex. Samples layered on mini-columns were eluted with buffered sodium chloride (100, 150, and 200 mmol/liter). Lactate dehydrogenase activity in column effluents was measured by the Wacker method, and their isoenzyme content was evaluated by electrophoresis on polyacrylamide gel. Results for column-fractionated LD-1 and LD-2 were expressed in two ways: LD-1/LD-2 ratios and total LD-1 + LD-2 activities. The former is a more specific indicator of myocardial infarction than the latter. Sera from 10 patients with acute myocardial infarction (increased creatine kinease isoenzyme MB activity) exhibited ratios in the range of 0.92 to 1.56, ratios for 10 patients without heart disease (normal creatine kinase MB) ranged from 0.33 to 0.69.

scholarly journals Mitochondrial fusion mediated by mitofusin 1 regulates macrophage mycobactericidal activity by enhancing autophagy

2021 ◽  
Author(s):  
Yuping Ning ◽  
Yi Cai ◽  
Youchao Dai ◽  
Fuxiang Li ◽  
Siwei Mo ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Life Cycle ◽  
Atp Synthase ◽  
Host Defense ◽  
Mitochondrial Dynamics ◽  
Critical Role ◽  
Mitochondrial Fusion ◽  
Atp Production ◽  
Metabolism Pathway ◽  
Mitofusin 1

Mitochondria as a highly dynamic organelle continuously changes morphology and position during its life cycle. Mitochondrial dynamics including fission and fusion play a critical role in maintaining functional mitochondria for ATP production, which is directly linked to host defense against Mtb infection. However, how macrophages regulate mitochondrial dynamics during Mycobacterium tuberculosis (Mtb) infection remains elusive. In this study, we found that Mtb infection induced mitochondrial fusion through enhancing the expression of mitofusin 1 ( MFN1 ), which resulted in increased ATP production. Silencing MFN1 inhibited mitochondrial fusion and subsequently reduced ATP production, which, in turn, severely impaired macrophages mycobactericidal activity by inhibiting autophagy. Impairment of mycobactericidal activity and autophagy was replicated using oligomycin, an inhibitor of ATP synthase. In summary, our study revealed MFN1-mediated mitochondrial fusion is essential for macrophages mycobactericidal activity through the regulation of ATP dependent autophagy. MFN1-mediated metabolism pathway might be targets for development of host direct therapy (HDT) strategy against TB.

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