Functional Regulation of Sugar Assimilation by N-Glycan-specific Interaction of Pancreatic α-Amylase with Glycoproteins of Duodenal Brush Border Membrane

Asanuma-Date, Kimie; Hirano, Yuki; Le, Na; Sano, Kotone; Kawasaki, Nana; Hashii, Noritaka; Hiruta, Yoko; Nakayama, Kenichi; Umemura, Masayuki; Ishikawa, Kazuhiko; Sakagami, Hiromi; Ogawa, Haruko

doi:10.1074/jbc.m111.314658

Cited by 23 publications

(39 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Human pancreatic ␣-amylase was expressed in yeast and purified as described previously (11). Rabbit anti-␣-amylase IgGs to human pancreatic ␣-amylase (K50894R) were purchased from Biomeda Corp. (Foster City, CA).…”

Section: Methodsmentioning

confidence: 99%

“…Immunohistostaining and Microscopy-For the immunoperoxidase technique, deparaffinized and rehydrated tissue sections were treated as described previously (11). Examination was performed using a box-type fluorescence microscope, FSX100 (Olympus Optical Co., Ltd., Tokyo, Japan).…”

Section: Methodsmentioning

confidence: 99%

“…The fresh duodenum sections were soaked in 10 M pig pancreatic ␣-amylase contained in 1 mM phenylmethylsulfonyl fluoride in PBS (pH 7.2) and incubated at 4°C or 37°C for 0 -60 min with gentle agitation. After incubation, the tissues were fixed in 4% paraformaldehyde/PBS, and paraffin-embedded sections were prepared (11).…”

Section: Methodsmentioning

confidence: 99%

“…The carbohydrate-binding activity of pancreatic ␣-amylase, which is common to pigs and humans (11), allows it to interact with N-glycans on the duodenal BBM. This increases glucose production up to 240% through the cooperation of sucrase-isomaltase and ␣-amylase at a wide range of concentrations; however, glucose uptake by SGLT1 is inhibited at high ␣-amylase concentrations in the intestine (11). Therefore, we hypothesized that this process may be an innate regulatory mechanism in the intestinal lumen to suppress the sudden elevation of glucose absorption and maintain blood glucose homeostasis.…”

mentioning

confidence: 99%

See 3 more Smart Citations

Pancreatic α-Amylase Controls Glucose Assimilation by Duodenal Retrieval through N-Glycan-specific Binding, Endocytosis, and Degradation

Date

Satoh

Iida

et al. 2015

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Pancreatic α-Amylase Controls Glucose Assimilation by Duodenal Retrieval through N-Glycan-specific Binding, Endocytosis, and Degradation

Date

Satoh

Iida

et al. 2015

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…The first interaction (Ptf1a and Amy1a) affects carbohydrate metabolism, since Ptf1a encodes a protein that is a component of the transcription factor complex (21,22), and Amy1a encodes an amylase isoenzyme produced by the pancreas, which catalyzes the first step in the digestion of dietary starch and glycogen. However, its role in the genesis of hypertension is not clear at present (23,24). On the other hand, the interaction between Ptger4 and Ncf2 is expected to affect blood pressure, as Ncf2 was functionally involved in 'blood pressure' (Table V, G-2).…”

Section: Interactions Among Shr-specific Genes and Candidate Genes Rmentioning

confidence: 99%

Analysis of genes causing hypertension and stroke in spontaneously hypertensive rats: Gene expression profiles in the brain

Yoshida

Watanabe

Yamanishi

et al. 2014

International Journal of Molecular Medicine

View full text Add to dashboard Cite

Abstract. Spontaneously hypertensive rats (SHR) and strokeprone SHR (SHRSP) are frequently used as rat models not only of essential hypertension and stroke, but also of attention-deficit hyperactivity disorder (ADHD). Normotensive Wistar-Kyoto rats (WKY) are used as the control rats in these cases. An increasing number of studies has demonstrated the critical role of the central nervous system in the development and maintenance of hypertension. In a previous study, we analyzed the gene expression profiles in the adrenal glands of SHR. Thus, in this study, we analyzed gene expression profiles in the brains of SHR in order to identify the genes responsible for causing hypertension and stroke, as well as those involved in ADHD. Using genome-wide microarray technology, we examined the gene expression profiles in the brains of 3 rat strains (SHR, SHRSP and WKY) when the rats were 3 and 6 weeks of age, a period in which the rats are considered to be in a prehypertensive state. Gene expression profiles in the brain were compared between SHR and WKY, and between SHRSP and SHR. A total of 179 genes showing a >4-or <-4-fold change in expression were isolated, and candidate genes were selected using two different web tools: the first tool was the Database for Annotation, Visualization and Integrated Discovery (DAVID), which was used to search for significantly enriched genes, and categorized them using Gene Ontology (GO) terms, and the second was the network explorer of Ingenuity Pathway Analysis (IPA), which was used to search for interaction networks among SHR-and SHRSP-specific genes. The IPA of SHR-specific genes revealed that prostaglandin E receptor 4 (Ptger4) is one of the candidate genes responsible for causing hypertension in SHR, and that albumin (Alb) and chymase 1 (Cma1) are also responsible for causing hypertension in SHR in the presence of angiotensinogen (Agt). Similar analyses of SHRSP-specific genes revealed that the angiotensin II receptorassociated gene (Agtrap) interacts with the FBJ osteosarcoma oncogene (Fos), and with the angiotensin II receptor type-1b (Agtr1b). As Agtrap and Agtr1b not only participate in the 'uptake of norepinephrine' and 'blood pressure', but also in the 'behavior' of SHRSP at 6 weeks of age, our data demonstrate a close association between hypertension and ADHD.

show abstract

α‐Amylase expressed in human small intestinal epithelial cells is essential for cell proliferation and differentiation

Date

Yamazaki

Toyoda

et al. 2019

J of Cellular Biochemistry

Self Cite

View full text Add to dashboard Cite

α‐Amylase, which plays an essential role in starch degradation, is expressed mainly in the pancreas and salivary glands. Human α‐amylase is also detected in other tissues, but it is unclear whether the α‐amylase is endogenously expressed in each tissue or mixed exogenously with one expressed by the pancreas or salivary glands. Furthermore, the biological significance of these α‐amylases detected in tissues other than the pancreas and salivary glands has not been elucidated. We discovered that human α‐amylase is expressed in intestinal epithelial cells and analyzed the effects of suppressing α‐amylase expression. α‐Amylase was found to be expressed at the second‐highest messenger RNA level in the duodenum in human normal tissues after the pancreas. α‐Amylase was detected in the cell extract of Caco‐2 intestinal epithelial cells but not secreted into the culture medium. The amount of α‐amylase expressed increased depending on the length of the culture of Caco‐2 cells, suggesting that α‐amylase is expressed in small intestine epithelial cells rather than the colon because the cells differentiate spontaneously upon reaching confluence in culture to exhibit the characteristics of small intestinal epithelial cells rather than colon cells. The α‐amylase expressed in Caco‐2 cells had enzymatic activity and was identified as AMY2B, one of the two isoforms of pancreatic α‐amylase. The suppression of α‐amylase expression by small interfering RNA inhibited cell differentiation and proliferation. These results demonstrate for the first time that α‐amylase is expressed in human intestinal epithelial cells and affects cell proliferation and differentiation. This α‐amylase may induce the proliferation and differentiation of small intestine epithelial cells, supporting a rapid turnover of cells to maintain a healthy intestinal lumen.

show abstract

Functional Regulation of Sugar Assimilation by N-Glycan-specific Interaction of Pancreatic α-Amylase with Glycoproteins of Duodenal Brush Border Membrane

Cited by 23 publications

References 53 publications

Pancreatic α-Amylase Controls Glucose Assimilation by Duodenal Retrieval through N-Glycan-specific Binding, Endocytosis, and Degradation

Pancreatic α-Amylase Controls Glucose Assimilation by Duodenal Retrieval through N-Glycan-specific Binding, Endocytosis, and Degradation

Analysis of genes causing hypertension and stroke in spontaneously hypertensive rats: Gene expression profiles in the brain

α‐Amylase expressed in human small intestinal epithelial cells is essential for cell proliferation and differentiation

Contact Info

Product

Resources

About