Emiglitate - CAS 80879-63-6
Catalog number: 80879-63-6
Category: Inhibitor
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Molecular Formula:
Molecular Weight:
Emiglitate is an α-glucosidase inhibitor that is a powerful inhibitor of glucose-induced insulin release.But no development was reported for the treatment of Diabetes mellitus
BAY o 1248; EINECS 279-613-2;Emiglitatum [Latin]; Emiglitate; UNII-PF8AB2IBUM;1,5-Dideoxy-1,5-((2-(4-(ethoxycarbonyl)phenoxy)ethyl)imino)-D-glucitol
Soluble in DMSO
-20℃ Freezer
Diabetes mellitus
Quality Standard:
In-house standard
Shelf Life:
2 month in rt, long time
Canonical SMILES:
Current Developer:
Bayer; Mitsubishi Pharma Corporation
1.Modulation of islet G-proteins, alpha-glucosidehydrolase inhibition and insulin release stimulated by various secretagogues.
Salehi A;Lundquist I Biosci Rep. 1996 Feb;16(1):23-34.
Guanine nucleotide-binding proteins (G-proteins) are known to act as important modulators of insulin release from the islets of Langerhans. We have recently found that the deoxynojirimycin-derivative emiglitate, a recognized inhibitor of intestinal alpha-glucosidehydrolase activity, is a powerful inhibitor of glucose-induced insulin release. With the use of isolated mouse islets the present investigation was performed in a primary attempt to elucidate whether this inhibitory mechanism in some way was linked to the beta-cell G-protein system. Treatment of freshly isolated islets with pertussis toxin (PTX), which is known to inactivate the G (i)-proteins, abolished the inhibitory effect of the alpha(2)-adrenoceptor agonist clonidine on insulin release stimulated by the phosphodiesterase inhibitor IBMX in the presence of the protein kinase C activator TPA and even changed it into an increase. Emiglitate did not display any inhibitory action on insulin release induced by these secretagogues. Similarly, clonidine-induced inhibition of glucose stimulated insulin release was reversed by PTX. However, PTX did not influence the suppressive action of emiglitate on glucose-induced insulin secretion.
2.Islet glucan-1,4-alpha-glucosidase: differential influence on insulin secretion induced by glucose and isobutylmethylxanthine in mice.
Salehi A;Lundquist I J Endocrinol. 1993 Sep;138(3):391-400.
In previous in-vivo studies we have presented indirect evidence for the involvement of islet acid glucan-1,4-alpha-glucosidase (acid amyloglucosidase), a lysosomal glycogen-hydrolysing enzyme, in certain insulin secretory processes. In the present combined in-vitro and in-vivo investigation, we studied whether differential changes in islet acid amyloglucosidase activity were related to the insulin secretory response induced by two mechanistically different secretagogues, glucose and isobutylmethylxanthine (IBMX). It was observed that addition of the selective alpha-glucosidehydrolase inhibitor emiglitate (1 mmol/l) to isolated pancreatic islets resulted in a marked reduction of glucose-induced insulin release. This was accompanied by a pronounced suppression of islet activities of acid amyloglucosidase and acid alpha-glucosidase, whereas other lysosomal enzyme activities, such as acid phosphatase and N-acetyl-beta-D-glucosaminidase, were unaffected. Furthermore, islets first incubated with emiglitate in the presence of high (16.7 mmol/l) glucose released less insulin than untreated controls in response to glucose in a second incubation period in the absence of emiglitate. In contrast, IBMX-induced insulin release was not influenced by emiglitate although accompanied by a marked reduction of islet activities of all three alpha-glucosidehydrolases.
3.Effect of 1-desoxynojirimycin derivatives on small intestinal disaccharidase activities and on active transport in vitro.
Lembcke B;Fölsch UR;Creutzfeldt W Digestion. 1985;31(2-3):120-7.
The influence of two new 1-desoxynojirimycin derivatives, BAY m 1099 and BAY o 1248, on rat small intestinal disaccharidases (sucrase, maltase, isomaltase, glucoamylase, lactase, trehalase) and alkaline phosphatase activity has been investigated in vitro. Both compounds are very potent alpha-glucosidase inhibitors. Tested in the range of 0.1-5.0 micrograms/ml, inhibition is strongest on sucrase (up to 97.1%) and glucoamylase (up to 96.7%). BAY m 1099 also reduced (up to 56.4%) beta-galactosidase (lactase) activity. For both inhibitors a competitive type of sucrase inhibition was demonstrated (Lineweaver-Burk plot). Affinity versus sucrase was unusually tight. The Ki of BAY m 1099 versus sucrase amounted to 1.14 x 10(-7) M and of BAY o 1248 to 6.92 X 10(-8) M (Dixon plot). Both inhibitors did not impair active transport of L-leucine or methyl-alpha-D-glucoside into everted rings of rat jejunum in vitro.
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CAS 80879-63-6 Emiglitate

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