scholarly journals The inhibition of glucosylceramide β-glucosidase and other acid hydrolases by nucleic acids

1988 ◽  
Vol 254 (1) ◽  
pp. 297-300 ◽  
Author(s):  
A Sano ◽  
N S Radin
Keyword(s):  
Absorption Spectrum ◽  
Nucleic Acids ◽  
Protein Content ◽  
Inhibitory Activity ◽  
Inhibitory Effect ◽  
Inhibitory Effects ◽  
Acid Hydrolases ◽  
Activator Protein ◽  
Excess Amount ◽  
Beta Glucosidase

During the isolation of the activator protein for glucosylceramide beta-glucosidase, we found that certain column fractions contained an inhibitor of the enzyme. After separation from the activator protein by a DEAE-Sephacel column, the inhibitor was purified further with a Spehadex G-75 column. The u.v. absorption spectrum of the purified material was similar to that of nucleic acids and the protein content of the purified material was negligible. Furthermore the purified inhibitor reacted with orcinol but not with diphenylamine, and its inhibitory activity was completely destroyed by treatment with RNAases. It seems likely that the purified inhibitor was tRNA. Authentic RNA, tRNA and DNA had similar inhibitory effects on beta-glucosidase (Ki 17 micrograms/ml for tRNA, noncompetitive toward the substrate). The inhibitory effect of nucleic acids was not fully overcome by an excess amount of the activator protein, but phosphatidylserine could restore the activity to normal. Tests with several other hydrolases revealed that the inhibitory effect of nucleic acids was fairly general.

Growth-Inhibiting Properties of Xylem Exudate From Vitis vinifera

1995 ◽  
Vol 22 (1) ◽  
pp. 7 ◽  
Author(s):  
JA Campbell ◽  
BR Loveys ◽  
VWK Lee ◽  
S Strother
Keyword(s):  
Vitis Vinifera ◽  
Inhibitory Activity ◽  
Lemna Minor ◽  
Growth Inhibitor ◽  
Inhibitory Effect ◽  
Vitis Vinifera L ◽  
Inhibitory Effects ◽  
Inhibitor Activity ◽  
Xylem Exudate ◽  
Growth Inhibiting

An inhibitory effect on the growth of Lemna minor L. cultures has been demonstrated in xylem exudate from Vitis vinifera L. var. Waltham Cross bled from canes cut near the time of budburst. Most inhibitory activity was detected up to the time of maximal daily exudation, which corresponded closely with budburst. After this time the inhibitory activity rapidly disappeared. A similar pattern occurred in each of the 3 years of the study, 1988-1990. Using ultrafiltration, it was shown that most of the growth inhibitor activity of the crude exudate was located in the 0.5-10 kDa fraction. This fraction exhibited a seasonal variation in its bioactivity similar to that ofthe crude exudate samples. The 0.5-10 kDa fraction was found to contain abscisic acid but not in a sufficient quantity to account for the inhibitory effects. When chromatographically separated fractions corresponding to oligosaccharides were pooled, biological activity equivalent to that of the crude exudate was retained, which provides evidence that the inhibitor is possibly an oligosaccharide.

scholarly journals Melanogenesis Inhibitory Activity of Diterpenoid and Triterpenoid Constituents from the Aerial Part of Isodon trichocarpus

2017 ◽  
Vol 12 (8) ◽  
pp. 1934578X1701200
Author(s):  
Yoshiaki Manse ◽  
Kiyofumi Ninomiya ◽  
Akane Okazaki ◽  
Eriko Okada-Nishida ◽  
Takahiro Imagawa ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Aerial Part ◽  
Methanol Extract ◽  
Inhibitory Effect ◽  
B16 Melanoma ◽  
Related Protein ◽  
Inhibitory Effects

A methanol extract from the aerial part of Isodon trichocarpus (Labiatae) demonstrated inhibitory effects on melanogenesis in theophylline-stimulated murine B16 melanoma 4A5 cells (IC50 = 1.6 μg/mL). From the extract, nine diterpenoids (1–9) and four triterpenoids (10–13) were isolated. Among the isolates, enmein (1, IC50 = 0.22 μM), isodocarpin (2, 0.19 μM), nodosin (4, 0.46 μM), and oridonin (6, 0.90 μM) showed an inhibitory effect without notable cytotoxicity at the effective concentrations. These diterpenoids (1, 2, 4, and 6) inhibited the expression of tyrosinase, tyrosine-related protein (TRP)-1, and TRP-2 mRNA, which could be the mechanism of melanogenesis inhibitory activity.

Enhanced Inhibition of Escherichia coli O157:H7 by Lysozyme and Chelators

2003 ◽  
Vol 66 (10) ◽  
pp. 1783-1789 ◽  
Author(s):  
J. S. BOLAND ◽  
P. M. DAVIDSON ◽  
J. WEISS
Keyword(s):  
Escherichia Coli ◽  
Inhibitory Activity ◽  
Chelating Agents ◽  
Inhibitory Effect ◽  
Escherichia Coli O157 ◽  
Inhibitory Effects ◽  
Antimicrobial Spectrum ◽  
E Coli ◽  
Dilution Assay ◽  
Microbroth Dilution

This study examined the effects of three chelating agents (EDTA, disodium pyrophosphate [DSPP], and pentasodium tripolyphosphate [PSTPP]) on the inhibition of the growth of Escherichia coli O157:H7 by lysozyme. The objective of this study was to identify replacement chelators that exhibit synergistic properties similar to those of EDTA. The inhibitory effects of EDTA at 300 to 1,500 μg/ml and of DSPP and PSTPP at 3,000 to 15,000 μg/ml in combination with lysozyme at 200 to 600 μg/ml for up to 48 h at pHs of 6.0, 7.0, and 8.0 on four strains of E. coli O157:H7 was studied with the use of a microbroth dilution assay. The addition of EDTA enhanced lysozyme's inhibitory effect on strains of E. coli O157:H7. EDTA at ≥300 μg/ml combined with lysozyme at 200 to 600 μg/ml was sufficient to inhibit the growth of the strains at pHs of 6.0 and 8.0. At pH 7.0, lysozyme at 200 to 600 μg/ml and EDTA concentrations of ≥1,000 μg/ml were effective in inhibiting three of the four strains. DSPP at pH 6.0 was inhibitory at ≥10,000 μg/ml when combined with lysozyme at 200 to 300 μg/ml. In contrast, PSTPP increased the inhibitory activity of lysozyme more effectively at pH 8.0. Lysozyme at 200 to 600 μg/ml was effective against two strains of E. coli O157:H7 when used in conjunction with PSTPP at ≥5,000 μg/ml. The remaining strains were inhibited by PSTPP at ≥10,000 μg/ml. Our results indicate that inhibition occurred with each lysozyme-chelator combination, but the concentrations of phosphates required to increase the antimicrobial spectrum of lysozyme against E. coli O157:H7 were higher than the EDTA concentrations required to achieve the same effect.

Receptor-mediated glucocorticoid inhibition of cell proliferation in mouse growth cartilage in vitro

1985 ◽  
Vol 108 (3) ◽  
pp. 343-350 ◽  
Author(s):  
Michael Silbermann ◽  
Gila Maor
Keyword(s):  
Protein Content ◽  
Inhibitory Effect ◽  
Inhibitory Effects ◽  
Glucocorticoid Treatment ◽  
Growth Inhibitory ◽  
Insoluble Material ◽  
Cartilage Cells ◽  
Specific Receptors ◽  
Inhibition Of Dna Synthesis

Abstract. The growth hormone of neonatal facial cartilage from ICR mice is inhibited by glucocorticoid treatment in vitro. A reduction of the overall tissue weight is accompanied by a substantial decrease in the protein content of the tissue. For the first 48 h in culture, hormone-treated cartilage undergoes a complete standstill in protein gain, and only thereafter the protein content increases, yet is markedly smaller than that of control specimens. Further, a significant reduction in the DNA content is seen already by 24 h, a feature that intensifies by 48 h. A slight recovery takes place thereafter. The reduction in DNA concentration is accompanied by a significant decrease in [3H]thymidine incorporation in acid-insoluble material. The inhibition of DNA synthesis by triamcinolone acetonide is protein- and RNA-synthesis-dependent. Autoradiographic examinations reveal that young cartilage cells are heavily labelled with [3H]dexamethasone and that this labelling is specific. To further substantiate the involvement of glucocorticoid-specific receptors in the latter's inhibitory effects, tissues were treated with cortexolone, this apparently 'masking' the cytosolic receptors for glucocorticoids, and thereby succeeded to eliminate the growth-inhibitory effect of triamcinolone. These results provide evidence for a receptor-mediated set of responses to glucocorticoids in these cartilage cells.

scholarly journals Cholinesterase and microbial inhibitory activities of Tetrapleura tetraptera

2012 ◽  
Vol 4 (2) ◽  
pp. 156-163
Author(s):  
N. E. Okoronkwo ◽  
J. O. Echeme
Keyword(s):  
Inhibitory Activity ◽  
Water Extract ◽  
Antimicrobial Activities ◽  
Inhibitory Effect ◽  
Klebsiella Pneumonia ◽  
Inhibitory Effects ◽  
Continuous Increase ◽  
Water Extracts ◽  
Tetrapleura Tetraptera ◽  
Inhibitory Activities

The cholinesterase and microbial inhibitory activities of different parts of Tetrapleura tetraptera plant were evaluated due to their local applications. The cholinesterase results revealed that the extracts showed some levels of inhibitory effects depending on the solvents used. Tetrapleura tetraptera leaves had better inhibitory effects with maximum inhibitory activity of 70.0% at a concentration of 1.00mg/l for the water extract. Tetrapleura tetraptera bark showed highest inhibitory effect of 71.05% and (84.34%) for the ethanol and chloroform extracts at concentrations of 0.5mg/l and 1.0 mg/l respectively. While for petroleum ether, T. tetraptera bark recorded 74.34% inhibitory effect at concentration of 2.0 mg/l and also showed continuous increase in inhibitory activity as the concentration increases for aqueous methanol. The results of the antimicrobial activities showed that among all the test organisms, theethanol and water extracts of the leaves, stem, bark and root of the plants had promising activity against Escherichia coli, Staphylococcus aureus, Proteus mirabilis, Pseudomonas aeruginosa and Klebsiella pneumonia bacteria and Aspergillus fumigatus and Rhizopus species fungi. There was no activity shown by the ethanol and water extracts ofthe parts of the plants with Fugarium oxysporum, Penicillium chrysogenum and Mucor species fungi. The bacteria strains were more sensitive to the tested extracts than the fungi strains.

Inhibitory effects of bioaccessible anthocyanins and procyanidins from apple, red grape, cinnamon on α-amylase, α-glucosidase and lipase

2020 ◽  
pp. 1-9
Author(s):  
Pınar Ercan ◽  
Sedef Nehir El
Keyword(s):  
Inhibitory Activity ◽  
Digestive Enzymes ◽  
Positive Control ◽  
Anthocyanin Content ◽  
Inhibitory Effects ◽  
Total Anthocyanin ◽  
Total Anthocyanin Content ◽  
Before And After ◽  
Red Grape

Abstract. The goals of this study were to determine and evaluate the bioaccessibility of total anthocyanin and procyanidin in apple (Amasya, Malus communis), red grape (Papazkarası, Vitis vinifera) and cinnamon (Cassia, Cinnamomum) using an in vitro static digestion system based on human gastrointestinal physiologically relevant conditions. Also, in vitro inhibitory effects of these foods on lipid (lipase) and carbohydrate digestive enzymes (α-amylase and α-glucosidase) were performed with before and after digested samples using acarbose and methylumbelliferyl oleate (4MUO) as the positive control. While the highest total anthocyanin content was found in red grape (164 ± 2.51 mg/100 g), the highest procyanidin content was found in cinnamon (6432 ± 177.31 mg/100 g) (p < 0.05). The anthocyanin bioaccessibilities were found as 10.2 ± 1%, 8.23 ± 0.64%, and 8.73 ± 0.70% in apple, red grape, and cinnamon, respectively. The procyanidin bioaccessibilities of apple, red grape, and cinnamon were found as 17.57 ± 0.71%, 14.08 ± 0.74% and 18.75 ± 1.49%, respectively. The analyzed apple, red grape and cinnamon showed the inhibitory activity against α-glucosidase (IC50 544 ± 21.94, 445 ± 15.67, 1592 ± 17.58 μg/mL, respectively), α-amylase (IC50 38.4 ± 7.26, 56.1 ± 3.60, 3.54 ± 0.86 μg/mL, respectively), and lipase (IC50 52.7 ± 2.05, 581 ± 54.14, 49.6 ± 2.72 μg/mL), respectively. According to our results apple, red grape and cinnamon have potential to inhibit of lipase, α-amylase and α-glucosidase digestive enzymes.

In Vitro Effects of Ethanol on Rabbit Platelet Aggregation, Secretion of Granule Contents, and Cyclic AMP Levels in the Presence of Prostacyclin

1989 ◽  
Vol 61 (02) ◽  
pp. 254-258 ◽  
Author(s):  
Margaret L Rand ◽  
Peter L Gross ◽  
Donna M Jakowec ◽  
Marian A Packham ◽  
J Fraser Mustard
Keyword(s):  
Cyclic Amp ◽  
Inhibitory Effect ◽  
Rabbit Platelet ◽  
Inhibitory Effects ◽  
Low Concentrations ◽  
Rabbit Platelets ◽  
High Concentrations ◽  
In Vitro Effects ◽  
Aggregation Of Platelets

SummaryEthanol, at physiologically tolerable concentrations, inhibits platelet responses to low concentrations of collagen or thrombin, but does not inhibit responses of washed rabbit platelets stimulated with high concentrations of ADP, collagen, or thrombin. However, when platelet responses to high concentrations of collagen or thrombin had been partially inhibited by prostacyclin (PGI2), ethanol had additional inhibitory effects on aggregation and secretion. These effects were also observed with aspirin- treated platelets stimulated with thrombin. Ethanol had no further inhibitory effect on aggregation of platelets stimulated with ADP, or the combination of ADP and epinephrine. Thus, the inhibitory effects of ethanol on platelet responses in the presence of PGI2 were very similar to its inhibitory effects in the absence of PGI2, when platelets were stimulated with lower concentrations of collagen or thrombin. Ethanol did not appear to exert its inhibitory effects by increasing cyclic AMP above basal levels and the additional inhibitory effects of ethanol in the presence of PGI2 did not appear to be brought about by further increases in platelet cyclic AMP levels.

Inhibition of ADP-Induced Responses in Human Platelets by Agents Elevating the Cyclic AMP Level: Comparison of Aggregation and Shape Change

1984 ◽  
Vol 52 (03) ◽  
pp. 333-335 ◽  
Author(s):  
Vider M Steen ◽  
Holm Holmsen
Keyword(s):  
Inhibitory Action ◽  
Human Platelet ◽  
Platelet Rich Plasma ◽  
Shape Change ◽  
Inhibitory Effect ◽  
Human Platelets ◽  
Inhibitory Effects ◽  
Early Step ◽  
Stimulus Response ◽  
Sequential Relationship

SummaryThe inhibitory effect of cAMP-elevating agents on shape change and aggregation in human platelets was studied to improve the understanding of the sequential relationship between these two responses.Human platelet-rich plasma was preincubated for 2 min at 37° C with prostaglandin E1 or adenosine, agents known to elevate the intracellular level of cAMP. Their inhibitory effects on ADP-induced shape change and aggregation were determined both separately and simultaneously. The dose-inhibition patterns for shape change and aggregation were similar for both PGE1 and adenosine. There was no distinct difference between the inhibitory action of these two inhibitors.These observations suggest that elevation of the intracellular concentration of cAMP interferes with an early step in the stimulus-response coupling that is common for aggregation and shape change.

The Inhibitory Effect of Heparin and Related Glycosaminoglycans on Neutrophil Chemotaxis

1984 ◽  
Vol 52 (02) ◽  
pp. 134-137 ◽  
Author(s):  
Yaacov Matzner ◽  
Gerard Marx ◽  
Ruth Drexler ◽  
Amiram Eldor
Keyword(s):  
Specific Binding ◽  
Anticoagulant Activity ◽  
Neutrophil Migration ◽  
Inhibitory Effect ◽  
Chemotactic Factor ◽  
Human Neutrophils ◽  
Boyden Chamber ◽  
Neutrophil Chemotaxis ◽  
Inhibitory Effects ◽  
Chemotactic Factors

SummaryClinical observations have shown that heparin has antiinflammatory activities. The effect of heparin on neutrophil chemotaxis was evaluated in vitro in the Boyden Chamber. This method enabled differentiation between the direct effects of heparin on neutrophil migration and locomotion, and its effects on chemotactic factors. Heparin inhibited both the random migration and directed locomotion of human neutrophils toward zymosan-activated serum (ZAS) and F-met-leu-phe (FMLP). Inhibition was found to be dependent on the concentrations of the heparin and of the chemotactic factors. No specific binding of heparin to the neutrophils could be demonstrated, and heparin’s inhibitory effects were eliminated by simple washing of the cells. When added directly to the chamber containing chemotactic factor, heparin inhibited the chemotactic activity of ZAS but not that of FMLP, suggesting a direct inhibitory effect against C5a, the principal chemotactic factor in ZAS.Experiments performed with low-molecular-weight heparin, N-desulfated heparin, dextran sulfate, chondroitin sulfate and dextran indicated that the inhibitory effects of heparin on neutrophil chemotaxis are not related to its anticoagulant activity, but probably depend on the degree of sulfation of the heparin molecule.

Inhibition of Yeast Growth by Tryptamine and Recovery with Tryptophan

2020 ◽  
Vol 16 (1) ◽  
pp. 48-52 ◽  
Author(s):  
Chandrika Kadkol ◽  
Ian Macreadie
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Carbon Source ◽  
Competitive Inhibition ◽  
Yeast Species ◽  
Inhibitory Effect ◽  
The Body ◽  
Inhibitory Effects ◽  
Trna Synthetases ◽  
Fermentative Growth ◽  
Biogenic Monoamine

Background: Tryptamine, a biogenic monoamine that is present in trace levels in the mammalian central nervous system, has probable roles as a neurotransmitter and/or a neuromodulator and may be associated with various neuropsychiatric disorders. One of the ways tryptamine may affect the body is by the competitive inhibition of the attachment of tryptophan to tryptophanyl tRNA synthetases. Methods: This study has explored the effects of tryptamine on growth of six yeast species (Saccharomyces cerevisiae, Candida glabrata, C. krusei, C. dubliniensis, C. tropicalis and C. lusitaniae) in media with glucose or ethanol as the carbon source, as well as recovery of growth inhibition by the addition of tryptophan. Results: Tryptamine was found to have an inhibitory effect on respiratory growth of all yeast species when grown with ethanol as the carbon source. Tryptamine also inhibited fermentative growth of Saccharomyces cerevisiae, C. krusei and C. tropicalis with glucose as the carbon source. In most cases the inhibitory effects were reduced by added tryptophan. Conclusion: The results obtained in this study are consistent with tryptamine competing with tryptophan to bind mitochondrial and cytoplasmic tryptophanyl tRNA synthetases in yeast: effects on mitochondrial and cytoplasmic protein synthesis can be studied as a function of growth with glucose or ethanol as a carbon source. Of the yeast species tested, there is variation in the sensitivity to tryptamine and the rescue by tryptophan. The current study suggests appropriate yeast strains and approaches for further studies.

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