2015
DOI: 10.1074/jbc.m114.594937
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Pancreatic α-Amylase Controls Glucose Assimilation by Duodenal Retrieval through N-Glycan-specific Binding, Endocytosis, and Degradation

Abstract: Background: Secreted pancreatic ␣-amylase binds to N-glycans of the duodenal brush-border membrane (BBM) and inhibits glucose uptake by SGLT1 at high doses. Results: Enterocytes endocytosed and degraded the ␣-amylase in lysosomes about 30 min after BBM binding. Conclusion: N-Glycan recognition and subsequent internalization of ␣-amylase suppressed and then gradually allowed duodenal glucose absorption. Significance: A newly revealed mechanism regulates postprandial intestinal glucose uptake.

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Cited by 45 publications
(39 citation statements)
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“…Alpha-amylase activities of rats in the diabetic control groups increased significantly (p≤0.05) when compared to those in the normal group which is consistent with the reports of Date et al, [26] showing that induction of diabetes caused damage on the pancreas leading to the release of α-amylase in pancreatic juice thereby metabolizing carbohydrate (maltose) to glucose resulting to rise in blood glucose level. Treatment with aqueous extract of Citrullus lanatus seeds significantly (p≤0.05) reduced α-amylase activities in all the treated groups.…”
Section: Discussionsupporting
confidence: 89%
“…Alpha-amylase activities of rats in the diabetic control groups increased significantly (p≤0.05) when compared to those in the normal group which is consistent with the reports of Date et al, [26] showing that induction of diabetes caused damage on the pancreas leading to the release of α-amylase in pancreatic juice thereby metabolizing carbohydrate (maltose) to glucose resulting to rise in blood glucose level. Treatment with aqueous extract of Citrullus lanatus seeds significantly (p≤0.05) reduced α-amylase activities in all the treated groups.…”
Section: Discussionsupporting
confidence: 89%
“…Salivary amylase passing through the stomach in substrate bound form comes into contact with a very low level of pancreatic enzyme proteolytic activity in the intestine of bariatric pigs and thus it is not destroyed. This hypothesis is supported by recent experiments by Date et al 55 , 56 as well as by some earlier findings 65 .…”
Section: Pancreatic Enzymes In Glycaemic Controlsupporting
confidence: 79%
“…Taking into account other studies where reduced blood amylase concentrations were associated with glucose intolerance, we speculate that the mechanism behind these findings is based on the specific signal transduction of enteral or parenteral amylase or amylase-derived components/peptides, which interact with the glycoconjugates—possibly receptors on the apical or basolateral surface of the enterocyte 48 . Pancreatic amylase has been reported to bind to N -glycans in intestinal brush border membrane and inhibit intestinal glucose absorption by SGLT1 55 , 56 . Furthermore, amylase and/or amylase derivatives could enhance glucose uptake in insulin-independent tissues such as enterocytes via GLUT1 or GLUT2, and in this case could serve as a defensive mechanism against the development of hyperglycemia.…”
Section: Pancreatic Enzymes In Glycaemic Controlmentioning
confidence: 99%
“…In animals, α-amylases (α-1,4 glucan-4-gluconohydrolase, EC 3.2.1.1) have a central role in the initial steps of the digestion of key glycogenic substrates such as dietary starch and dietary and/or storage glycogen (Singh and Kayastha, 2014;Date et al, 2015). However, in spite of their inherent physiological importance, the current knowledge about forms, modulation by environmental factors, and biochemical features of amylase in the hepatopancreas (the main site of digestive enzyme synthesis and of digestion and absorption of nutrients and storage of energy substrates) of groups of ecological importance such as intertidal euryhaline crabs is still scarce and fragmentary (Blandamer and Beechey, 1966;Van Wormhoudt et al, 1995;Asaro et al, 2011;Zeng et al, 2010).…”
Section: Introductionmentioning
confidence: 99%