4-Hydroxyisoleucine: a novel amino acid potentiator of insulin secretion

Diabetes ◽  
1998 ◽  
Vol 47 (2) ◽  
pp. 206-210 ◽  
Author(s):  
Y. Sauvaire ◽  
P. Petit ◽  
C. Broca ◽  
M. Manteghetti ◽  
Y. Baissac ◽  
...  
Keyword(s):  
2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Nana Kobayashi ◽  
Shogo Okazaki ◽  
Oltea Sampetrean ◽  
Junichiro Irie ◽  
Hiroshi Itoh ◽  
...  

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Nana Kobayashi ◽  
Shogo Okazaki ◽  
Oltea Sampetrean ◽  
Junichiro Irie ◽  
Hiroshi Itoh ◽  
...  

2020 ◽  
Vol 167 (6) ◽  
pp. 587-596 ◽  
Author(s):  
Kento Maeda ◽  
Masayoshi Tasaki ◽  
Yukio Ando ◽  
Kazuaki Ohtsubo

Abstract Maintenance of cell surface residency and function of glycoproteins by lectins are essential for regulating cellular functions. Galectins are β-galactoside-binding lectins and form a galectin-lattice, which regulates stability, clustering, membrane sub-domain localization and endocytosis of plasmalemmal glycoproteins. We have previously reported that galectin-2 (Gal-2) forms a complex with cationic amino acid transporter 3 (CAT3) in pancreatic β cells, although the biological significance of the molecular interaction between Gal-2 and CAT3 has not been elucidated. In this study, we demonstrated that the structure of N-glycan of CAT3 was either tetra- or tri-antennary branch structure carrying β-galactosides, which works as galectin-ligands. Indeed, CAT3 bound to Gal-2 using β-galactoside epitope. Moreover, the disruption of the glycan-mediated bindings between galectins and CAT3 significantly reduced cell surface expression levels of CAT3. The reduced cell surface residency of CAT3 attenuated the cellular arginine uptake activities and subsequently reduced nitric oxide production, and thus impaired the arginine-stimulated insulin secretion of pancreatic β cells. These results indicate that galectin-lattice stabilizes CAT3 by preventing endocytosis to sustain the arginine-stimulated insulin secretion of pancreatic β cells. This provides a novel cell biological insight into the endocrinological mechanism of nutrition metabolism and homeostasis.


Jurnal Kimia ◽  
2016 ◽  
Author(s):  
Dita Rizkiyanti ◽  
Ni Made Suaniti ◽  
Ketut Ratnayani

Seeds are a source of high protein when compared with other parts of the plant. Compared to soy bean, the use of winged bean seeds, tamarind seeds, moringa seeds as protein sources are still very limited. Protein composed of several amino acids bond together to form a polypeptide. Some amino acids have been investigated to act as stimulating insulin secretion, namely, arginine, alanine, phenylalanine, isoleucine, and lysine. The aim of this study was to determine the potential content of amino acids stimulating the secretion of insulin in winged bean seeds, tamarind seeds, and moringa seeds. Based on the total content of amino acids in each seeds, the results showed that moringa seeds have the highest levels of total amino acids stimulating insulin secretion (16.4%), followed by winged bean seeds (16.2%), and tamarind seeds (12.1%). But if seen by the levels of each amino acid, the winged bean seeds on average had the highest amino acid content. The highest levels of arginine, alanine, phenylalanine, isoleucine, and leucine were found in winged bean seeds, while only one specific amino acid i.e. lysine was found to be the highest level on moringa seeds. It can be concluded that the most potential seeds as a source of amino acids stimulating insulin was the winged bean seeds, that will be useful in the prevention or treatment of diabetes mellitus.


Diabetes ◽  
1998 ◽  
Vol 47 (2) ◽  
pp. 206-210 ◽  
Author(s):  
Y. Sauvaire ◽  
P. Petit ◽  
C. Broca ◽  
M. Manteghetti ◽  
Y. Baissac ◽  
...  
Keyword(s):  

Diabetes Care ◽  
2003 ◽  
Vol 26 (3) ◽  
pp. 625-630 ◽  
Author(s):  
L. J.C. van Loon ◽  
M. Kruijshoop ◽  
P. P.C.A. Menheere ◽  
A. J.M. Wagenmakers ◽  
W. H.M. Saris ◽  
...  

2000 ◽  
Vol 28 (5) ◽  
pp. A196-A196
Author(s):  
A. Shine ◽  
N. H. Mc Clenaghan ◽  
P. Flatt ◽  
JPG Malthouse ◽  
C. Hewage ◽  
...  

2014 ◽  
Vol 307 (9) ◽  
pp. E800-E812 ◽  
Author(s):  
Veronika Leiss ◽  
Katarina Flockerzie ◽  
Ana Novakovic ◽  
Michaela Rath ◽  
Annika Schönsiegel ◽  
...  

Bordetella pertussis toxin (PTx), also known as islet-activating protein, induces insulin secretion by ADP-ribosylation of inhibitory G proteins. PTx-induced insulin secretion may result either from inactivation of Gαo proteins or from combined inactivation of Gαo, Gαi1, Gαi2, and Gαi3 isoforms. However, the specific role of Gαi2 in pancreatic β-cells still remains unknown. In global (Gαi2−/−) and β-cell-specific (Gαi2βcko) gene-targeted Gαi2 mouse models, we studied glucose homeostasis and islet functions. Insulin secretion experiments and intracellular Ca2+ measurements were used to characterize Gαi2 function in vitro. Gαi2−/− and Gαi2βcko mice showed an unexpected metabolic phenotype, i.e., significantly lower plasma insulin levels upon intraperitoneal glucose challenge in Gαi2−/− and Gαi2βcko mice, whereas plasma glucose concentrations were unchanged in Gαi2−/− but significantly increased in Gαi2βcko mice. These findings indicate a novel albeit unexpected role for Gαi2 in the expression, turnover, and/or release of insulin from islets. Detection of insulin secretion in isolated islets did not show differences in response to high (16 mM) glucose concentrations between control and β-cell-specific Gαi2-deficient mice. In contrast, the two- to threefold increase in insulin secretion evoked by l-arginine or l-ornithine (in the presence of 16 mM glucose) was significantly reduced in islets lacking Gαi2. In accord with a reduced level of insulin secretion, intracellular calcium concentrations induced by the agonistic amino acid l-arginine did not reach control levels in β-cells. The presented analysis of gene-targeted mice provides novel insights in the role of β-cell Gαi2 showing that amino acid-induced insulin-release depends on Gαi2.


2007 ◽  
Vol 282 (46) ◽  
pp. 33583-33592 ◽  
Author(s):  
Nidhi Ahuja ◽  
Bjoern Schwer ◽  
Stefania Carobbio ◽  
David Waltregny ◽  
Brian J. North ◽  
...  

Sirtuins are homologues of the yeast transcriptional repressor Sir2p and are conserved from bacteria to humans. We report that human SIRT4 is localized to the mitochondria. SIRT4 is a matrix protein and becomes cleaved at amino acid 28 after import into mitochondria. Mass spectrometry analysis of proteins that coimmunoprecipitate with SIRT4 identified insulindegrading enzyme and the ADP/ATP carrier proteins, ANT2 and ANT3. SIRT4 exhibits no histone deacetylase activity but functions as an efficient ADP-ribosyltransferase on histones and bovine serum albumin. SIRT4 is expressed in islets of Langerhans and colocalizes with insulin-expressing β cells. Depletion of SIRT4 from insulin-producing INS-1E cells results in increased insulin secretion in response to glucose. These observations define a new role for mitochondrial SIRT4 in the regulation of insulin secretion.


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