Xanthohumol, a Prenylated Chalcone from Beer Hops, Acts as an α-Glucosidase Inhibitor in Vitro

2014 ◽  
Vol 62 (24) ◽  
pp. 5548-5554 ◽  
Author(s):  
Ming Liu ◽  
Hua Yin ◽  
Ge Liu ◽  
Jianjun Dong ◽  
Zhonghua Qian ◽  
...  
Keyword(s):  
Glucosidase Inhibitor ◽  
Prenylated Chalcone

Critical Assessment of In Vitro Screening of α-Glucosidase Inhibitors from Plants with Acarbose as a Reference Standard

Planta Medica ◽  
2021 ◽  
Author(s):  
Neil Miller ◽  
Elizabeth Joubert
Keyword(s):  
Reference Standard ◽  
Screening Assay ◽  
Enzyme Preparations ◽  
Glucosidase Inhibitor ◽  
Biological Source ◽  
Oral Antidiabetic ◽  
Glucosidase Inhibitors ◽  
Plant Sources

AbstractPostprandial hyperglycemia is treated with the oral antidiabetic drug acarbose, an intestinal α-glucosidase inhibitor. Side effects of acarbose motivated a growing number of screening studies to identify novel α-glucosidase inhibitors derived from plant extracts and other natural sources. As “gold standard”, acarbose is frequently included as the reference standard to assess the potency of these candidate α-glucosidase inhibitors, with many outperforming acarbose by several orders of magnitude. The results are subsequently used to identify suitable compounds/products with strong potential for in vivo efficacy. However, most α-glucosidase inhibitor screening studies use enzyme preparations obtained from nonmammalian sources (typically Saccharomyces cerevisiae), despite strong evidence that inhibition data obtained using nonmammalian α-glucosidase may hold limited value in terms of identifying α-glucosidase inhibitors with actual in vivo hypoglycemic potential. The aim was to critically discuss the screening of novel α-glucosidase inhibitors from plant sources, emphasizing inconsistencies and pitfalls, specifically where acarbose was included as the reference standard. An assessment of the available literature emphasized the cruciality of stating the biological source of α-glucosidase in such screening studies to allow for unambiguous and rational interpretation of the data. The review also highlights the lack of a universally adopted screening assay for novel α-glucosidase inhibitors and the commercial availability of a standardized preparation of mammalian α-glucosidase.

scholarly journals Iminosugars With Endoplasmic Reticulum α-Glucosidase Inhibitor Activity Inhibit ZIKV Replication and Reverse Cytopathogenicity in vitro

2020 ◽  
Vol 11 ◽  
Author(s):  
Gitanjali Bhushan ◽  
Levina Lim ◽  
Ian Bird ◽  
Shubhada K. Chothe ◽  
Ruth H. Nissly ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Inhibitor Activity ◽  
Glucosidase Inhibitor

Development of diarylpentadienone analogues as alpha-glucosidase inhibitor: Synthesis, in vitro biological and in vivo toxicity evaluations, and molecular docking analysis

2020 ◽  
Vol 104 ◽  
pp. 104277
Author(s):  
Maryam Aisyah Abdullah ◽  
Yu-Ri Lee ◽  
Siti Nurulhuda Mastuki ◽  
Sze Wei Leong ◽  
Wan Norhamidah Wan Ibrahim ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Docking Analysis ◽  
In Vivo Toxicity ◽  
Glucosidase Inhibitor ◽  
Alpha Glucosidase ◽  
Molecular Docking Analysis

scholarly journals In vitro and in silico evaluations of diarylpentanoid series as α-glucosidase inhibitor

2018 ◽  
Vol 28 (3) ◽  
pp. 302-309 ◽  
Author(s):  
Sze Wei Leong ◽  
Faridah Abas ◽  
Kok Wai Lam ◽  
Khatijah Yusoff
Keyword(s):  
In Silico ◽  
Glucosidase Inhibitor

Xanthohumol Induces Apoptosis in B-CLL Mediated by Caspase 9 Following Downregulation of bcl-xL and mcl-1.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 5028-5028
Author(s):  
Barbara Vanhoecke ◽  
Sofie Lust ◽  
Ann Janssens ◽  
Jan Philippe ◽  
Marc Bracke ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Specific Inhibitor ◽  
Annexin V ◽  
Parp Cleavage ◽  
Cancer Cell Growth ◽  
Breast Cancer Cell Growth ◽  
Erk Phosphorylation ◽  
Prenylated Chalcone ◽  
Dose Dependent

Abstract Introduction Xanthohumol is a hop-derived prenylated chalcone with structural similarities to flavopiridol. It has documented impact on breast cancer cell growth and invasiveness in vitro. Based on these observations, lymphocytes from patients with 20 B-CLL were cultured in the presence of xanthohumol in vitro. Methods Xanthohumol was dissolved in DMSO and used at concentrations up to 50 μM. B-CLL cells were cultured in RPMI 1640–10% FBS in vitro. Apoptosis, cell cycle analysis and bcl-2 expression was assessed by flow cytometry. PARP, Erk1/2, p38, Akt, JNK, p70S6K, and P-p38, P-Akt, P-JNK, and P-p70S6K, caspase 3, 8 and 9, and bcl-XL and mcl-1 were assessed by Western Blot. Results After 24h, xanthohumol induced dose-dependent killing of B-CLL cells at a LD50 (24h) of 24.4 ± 6.6 μM, independently of known adverse prognostic factors such as Ig mutation status, ZAP-70, and cytogenetic abnormalities including 17p-loss of p53. Cell death was associated with PARP cleavage and Annexin V positivity, suggestive of an apoptotic mechanism. Apoptosis was accompanied by cleavage of procaspase-9 but not of procaspase-8. Among bcl-2 family members tested, there was a decrease in bcl-2, bcl-xL and mcl-1 expression. The effects of xanthohumol on the major signal transduction pathways showed no effect on Jnk, Akt, p38 and Erk phosphorylation, but stimulation of p70S6K phosphorylation which could not be inhibited by rapamycin, a specific inhibitor of mTOR. Conclusion Xanthohumol has antitumor activity on B-CLL cells in vitro that appears to be independent both of DNA-damage and of Zap-70 effects on signal transduction.

ChemInform Abstract: Synthesis from D-Lyxonolactone of 1,4-Dideoxy-1,4-imino-L-arabinitol, a Glucosidase Inhibitor with in vitro Antiviral Activity.

ChemInform ◽  
2010 ◽  
Vol 24 (34) ◽  
pp. no-no
Author(s):  
J. R. BEHLING ◽  
A. L. CAMPBELL ◽  
K. A. BABIAK ◽  
J. S. NG ◽  
J. MEDICH ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Glucosidase Inhibitor

scholarly journals COMPARISON OF α –GLUCOSIDASE INHIBITORY ACTIVITY OF Moringa oleifera ETHANOLIC EXTRACT

2021 ◽  
Vol 9 (Spl-2-ICOPMES_2020) ◽  
pp. S269-S273
Author(s):  
Rizky Rahmwaty Alami ◽  
◽  
Herlina Rante ◽  
Yulia Yusrini Djabir ◽  
◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Moringa Oleifera ◽  
Ethanolic Extract ◽  
Ethanol Extract ◽  
Positive Control ◽  
Glucosidase Inhibitor ◽  
Plant Samples

The purpose of this research was to determine the α-glucosidase enzyme inhibitory activity of Moringa oleifera plant samples collected from the three geographical areas viz., Saragi, Bacuhau, and Batumatongka of Southeast Sulawesi Indonesia. Ethanol extract of Moringa leaves was prepared by the maceration method using 95% ethanol. The estimation of α –glucosidase inhibitory activity of this extract was performed in vitro. The results of the study showed that ethanolic extract of three Moringa samples i.e. Sarangi, Bacuhau, and Batumatongka had the IC50value of 18.62, 10.18, 10.58 ppm, respectively while IC50value for the acarbose positive control was reported 11.54ppm. From the results of this study, it can be concluded that ethanolic extract of Moringa could inhibit α –glucosidase and this potential was similar to the commercial α –glucosidase inhibitor acarbose.

scholarly journals Biosynthesis of inositol trisphosphate receptors: selective association with the molecular chaperone calnexin

1999 ◽  
Vol 342 (1) ◽  
pp. 153-161 ◽  
Author(s):  
Suresh K. JOSEPH ◽  
Darren BOEHNING ◽  
Shaila BOKKALA ◽  
Richard WATKINS ◽  
Johan WIDJAJA
Keyword(s):  
Inositol Trisphosphate ◽  
Type I ◽  
Ip3 Receptors ◽  
Inositol Trisphosphate Receptor ◽  
Glucosidase Inhibitor ◽  
Glucosidase Inhibitors ◽  
Glycosylation Sites ◽  
Mechanism Of Interaction ◽  
Trisphosphate Receptor

A prominent labelled polypeptide having the same mobility as type-I inositol trisphosphate receptor (IP3R) was immunoprecipitated from WB-cell lysates by antibodies to calnexin, an ER integral membrane chaperone. The identity of this polypeptide was confirmed by re-immunoprecipitation of the radioactive polypeptides released from calnexin-antibody immunoprecipitates with type-I IP3R antibody. The interaction of calnexin with newly synthesized type-I IP3R was transient and inhibited by treatment of the cells with dithiothreitol or the glucosidase inhibitor N-methyldeoxynojirimicin. In similar experiments, there was no evidence for the binding of type-I IP3R to calreticulin, an ER luminal chaperone. Calnexin (but not calreticulin) associated with newly synthesized FLAG (DYKDDDDK epitope)-tagged type-III IP3R expressed in COS-7 cells. In order to further define the mechanism of interaction of nascent IP3R with chaperones, we have utilized an in vitro rabbit reticulocyte translation assay programmed with RNA templates encoding the six putative transmembrane (TM) domains of IP3Rs. In accordance with the known preference of calnexin for monoglucosylated oligosaccharide chains, calnexin antibody preferentially immunoprecipitated a proportion of glycosylated type-I translation product. Addition of glucosidase inhibitors prevented the association of calnexin with in vitro translated type-I TM construct. Using truncated RNA templates we found that calnexin did not associate with the first four TM domains but retained affinity for the construct encoding TM domains 5 and 6, which contains the glycosylation sites. We propose that calnexin is a key chaperone involved in the folding, assembly and oligomerization of newly synthesized IP3 receptors in the ER.

scholarly journals The regulation of lipogenesis in vivo in the lactating mammary gland of the rat during the starved-refed transition. Studies wtih acarbose, a glucosidase inhibitor

1987 ◽  
Vol 242 (1) ◽  
pp. 235-243 ◽  
Author(s):  
S W Mercer ◽  
D H Williamson
Keyword(s):  
Mammary Gland ◽  
Time Course ◽  
Chow Diet ◽  
Glucosidase Inhibitor ◽  
Lactating Mammary Gland ◽  
Phosphofructokinase Activity ◽  
Time Course Study ◽  
Fructose 1,6 Bisphosphate

Depression of carbohydrate digestion by oral administration of acarbose, a glucosidase inhibitor, led to a 75% inhibition of the re-activation of lipogenesis in vivo in the mammary gland of 18 h-starved lactating rats refed with 5 g of chow diet. Rates of [1-14C]glucose incorporation in vitro into lipid and CO2 in mammary-gland acini isolated from refed animals were elevated compared with acini from starved rats, but acarbose treatment completely prevented this stimulation. Gastric intubation of glucose led to a large stimulation of lipogenesis in the mammary gland of starved lactating rats, similar to that induced by refeeding with chow diet; this was dependent on the amount of glucose given and the time elapsed between glucose administration and injection of 3H2O for the measurement of lipogenesis. The switch-on of lipogenesis in the mammary gland of starved lactating rats, by refeeding or by intubation of glucose, was associated with a decrease in the ratio of [glucose 6-phosphate]/[fructose 1,6-bisphosphate] in the gland, indicative of an increase in phosphofructokinase activity. A time-course study revealed that the ratio decreased rapidly over the first 30 min of chow refeeding, after which a large surge in lipogenesis was seen. Acarbose, given 25 min after the onset of refeeding, led to a stepwise increase in the ratio, in parallel with the observed decrease in lipogenic activity. It is concluded that the control of lipogenesis in the mammary gland is closely linked to the availability of dietary carbohydrate. An important site of regulation of lipogenesis in the gland appears to be at the level of phosphofructokinase. A possible role of insulin in the regulation of phosphofructokinase activity, and the acute modulation of insulin-sensitivity in the gland during the starved-refed transition, are discussed.

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