Sugar-mimic glycosidase inhibitors: natural occurrence, biological activity and prospects for therapeutic application

Asano, Naoki; Nash, Robert J.; Molyneux, Russell J.; Fleet, George W. J.

doi:10.1016/s0957-4166(00)00113-0

Cited by 1,020 publications

(438 citation statements)

References 60 publications

Supporting

Mentioning

426

Contrasting

Unclassified

Order By: Relevance

“…Perhaps these alkaloids can interact with barrier function and sites, thus being able to enter the brain and contact the fetus. Hydrophilic compounds can cross these barriers at high concentrations and accumulate in subcellular compartments with a low pH (Asano et al, 2000). Swainsonine may be actively accumulated in liver and kidney because of the extensive sugar activity present in these organs (Bowen et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

“…Swainsonine is an indolizidine alkaloid and inhibits the action of the enzymes lysosomal α-mannosidase and Golgi α-mannosidase-II, resulting in lysosomal accumulation of incompletely processed oligosaccharides and alteration of the synthesis, processing and transport of glycoproteins (Stegelmeier et al, 1995). Calystegines are nortropanic alkaloids and inhibits the activity of glucosidases, galactosidases and xylosidases, lysosomal enzymes which act on oligosaccharide metabolism (Asano et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Rats offspring exposed to Ipomoea Carnea and handling during gestation: neurochemical evaluation

Schwarz

Hosomi

Flório

et al. 2007

Braz. arch. biol. technol.

View full text Add to dashboard Cite

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Rats offspring exposed to Ipomoea Carnea and handling during gestation: neurochemical evaluation

Schwarz

Hosomi

Flório

et al. 2007

Braz. arch. biol. technol.

View full text Add to dashboard Cite

show abstract

“…The production of extracellular glycosidases as well as proteolytic enzymes (BALASUBRAMANIAM et al 2005;LUAN et al 2005;MERTOVÁ et al 2002) that are released from plant cells might be of some importance for biotechnological applications in the food and pharmaceutical research and industry (SHIBANO et al 2004;WILLITS et al 2004;ASANO et al 2000;EL ASHRY et al 2000a,b,c;WATSON et al 2001). These enzymes are generally present in plants.…”

Section: Resultsmentioning

confidence: 99%

“…The data indicate a 91.5-92.0% intracellular and 8.0-8.5% extracellular distribution of the enzyme activity tested. The intracellular specific enzyme activity is 1.72-1.84 times higher.The production of extracellular glycosidases as well as proteolytic enzymes (BALASUBRAMANIAM et al 2005;LUAN et al 2005;MERTOVÁ et al 2002) that are released from plant cells might be of some importance for biotechnological applications in the food and pharmaceutical research and industry (SHIBANO et al 2004;WILLITS et al 2004;ASANO et al 2000; EL ASHRY et al 2000a,b,c;WATSON et al It is a very well-known fact that glycosidase inhibitors such as many mono-and bicyclic polyhydroxylated pyrrolides, piperidines and azepines (referred to as iminosugars or azasugars) have the potential as antiviral, anticancer and antidiabetic agents. Some of these inhibitors have already been put on the market for treatment of diabetes.…”

mentioning

confidence: 99%

Identification of sucrase activity in cell suspension and culture medium of melon

Stano¹,

Mičieta²,

Barth³

et al. 2005

Hort. Sci. (Prague)

View full text Add to dashboard Cite

ABSTRACT:The activity of (soluble acid) sucrase was detected in a culture medium of the cell suspension culture of watermelon (Citrullus vulgaris L.). A simple and rapid procedure for the identification and determination of extracellular sucrase from a culture medium of watermelon cell suspension cultures is described. Sucrose was used as a substrate for the determination of extracellular and intracellular activities of the enzyme. Intracellular activity was estimated from the cell suspension. The results show a 91.5-92.0% intracellular and 8.0-8.5% extracellular distribution of sucrase activity. The described method enables to carry out a rapid, simple and specific detection of extracellular sucrase in plants. 105 lus vulgaris cv. Samara as previously described by TILEMANN et al. (2003).Identification and determination of intra-and extracellular sucraseUsing sucrose as a substrate the intra-and extracellular activity of soluble acid sucrase was identified. Eight days old cell suspension cultures were used to determine the intracellular enzyme activity. The cells (5 g) were filtered and washed twice with 1,000 ml of distilled water. Soluble proteins were extracted by grinding the cells in a pre-cooled mortar using a ratio 1:2 (g/ml) of cells and Mc Ilvaine buffer pH 4.5 at 4°C. The homogenate was filtered through two layers of nylon cloth and centrifuged at 15,000 g at 4°C. For determinations of extracellular enzyme activity the cultivation medium (without cells) was used after centrifugation (15,000 g, 10 min at 4°C). Enzyme assayEnzyme activity was determined by a modified method of RUBIO et al. (2002) using sucrose as a substrate. The reaction mixture contained a suitable amount of enzyme (0.2-0.4 ml) and 0.4 mM sucrose in Mc Ilvaine buffer pH 4.5 in a final volume of 2 ml. Enzyme activity was determined at 30°C for 30 to 60 min. The control contained temperature-inactivated enzyme (100°C, 10 min). The enzyme activity was expressed in katals. Proteins were determined by the method of BRADFORD (1976) using bovine serum albumin as a standard protein. The glucose content released by the enzyme was determined by the method of TRINDER (1969). RESULTS AND DISCUSSIONSynthetic chromogenic substrates are very suitable for biochemical and histochemical studies of hydrolytic enzymes. In the last decades, several methods for the determination of hydrolytic enzymes have been developed. Various naturally occurring chromogenic substrates may be used for these purposes (KIM et al. 2002;MIČIETA et al. 2002). p-nitrophenyl-β-Dfructofuranoside and naphthyl-β-D-fructofuranoside were not synthesised and only a natural substrate -sucrose was used for the study of sucrase.Therefore only sucrose was used to study the activity of intracellular and extracellular (acid soluble) sucrase. The highest specific activity of the studied enzyme was recorded on day 8 of cultivation (Table 2) in undifferentiated cells. Homogenised cell suspension cultures and culture medium alone after 8-day cultivation were used to assay the activity of intrac...

show abstract

“…The inhibitory effect of swainsonine on the class II enzyme had been described previously 89 . The bicyclic derivative of 1-deoxymannojirimycin, castanospermine, an indolizine alkaloid isolated from the seeds of the Australian chest nut tree Castanosperum australe 104 , inhibits the ER glucosidase enzymes, and as a result, further glycan processing 105 .…”

Section: High Mannose Speciesmentioning

confidence: 99%

Tailoring recombinant protein quality by rational media design

Brühlmann

Jordan

Hemberger³

et al. 2015

Biotechnology Progress

View full text Add to dashboard Cite

Clinical efficacy and safety of recombinant proteins are closely associated with their structural characteristics. The major quality attributes comprise glycosylation, charge variants (oxidation, deamidation, and C‐ & N‐terminal modifications), aggregates, low‐molecular‐weight species (LMW), and misincorporation of amino acids in the protein backbone. Cell culture media design has a great potential to modulate these quality attributes due to the vital role of medium in mammalian cell culture. The purpose of this review is to provide an overview of the way both classical cell culture medium components and novel supplements affect the quality attributes of recombinant therapeutic proteins expressed in mammalian hosts, allowing rational and high‐throughput optimization of mammalian cell culture media. A selection of specific and/or potent inhibitors and activators of oligosaccharide processing as well as components affecting multiple quality attributes are presented. Extensive research efforts in this field show the feasibility of quality engineering through media design, allowing to significantly modulate the protein function. © 2015 American Institute of Chemical Engineers Biotechnol. Prog., 31:615–629, 2015

show abstract

Sugar-mimic glycosidase inhibitors: natural occurrence, biological activity and prospects for therapeutic application

Cited by 1,020 publications

References 60 publications

Rats offspring exposed to Ipomoea Carnea and handling during gestation: neurochemical evaluation

Rats offspring exposed to Ipomoea Carnea and handling during gestation: neurochemical evaluation

Identification of sucrase activity in cell suspension and culture medium of melon

Tailoring recombinant protein quality by rational media design

Contact Info

Product

Resources

About