scholarly journals Dietary protein composition influences abundance of peptide and amino acid transporter messenger ribonucleic acid in the small intestine of 2 lines of broiler chicks

2010 ◽  
Vol 89 (8) ◽  
pp. 1663-1676 ◽  
Author(s):  
E.R. Gilbert ◽  
H. Li ◽  
D.A. Emmerson ◽  
K.E. Webb ◽  
E.A. Wong
PLoS ONE ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. e0128207 ◽  
Author(s):  
Guangran Li ◽  
Jianjun Li ◽  
Bie Tan ◽  
Jing Wang ◽  
Xiangfeng Kong ◽  
...  

2015 ◽  
Vol 1848 (5) ◽  
pp. 1157-1164 ◽  
Author(s):  
Laura A. Velázquez-Villegas ◽  
Adriana M. López-Barradas ◽  
Nimbe Torres ◽  
Rogelio Hernández-Pando ◽  
Juan Carlos León-Contreras ◽  
...  

PLoS ONE ◽  
2017 ◽  
Vol 12 (9) ◽  
pp. e0184845 ◽  
Author(s):  
Julia Jando ◽  
Simone M. R. Camargo ◽  
Brigitte Herzog ◽  
François Verrey

2020 ◽  
Vol 134 (21) ◽  
pp. 2823-2833 ◽  
Author(s):  
Simone M.R. Camargo ◽  
Raphael N. Vuille-dit-Bille ◽  
Chantal F. Meier ◽  
François Verrey

Abstract ACE2 is a type I membrane protein with extracellular carboxypeptidase activity displaying a broad tissue distribution with highest expression levels at the brush border membrane (BBM) of small intestine enterocytes and a lower expression in stomach and colon. In small intestinal mucosa, ACE2 mRNA expression appears to increase with age and to display higher levels in patients taking ACE-inhibitors (ACE-I). There, ACE2 protein heterodimerizes with the neutral amino acid transporter Broad neutral Amino acid Transporter 1 (B0AT1) (SLC6A19) or the imino acid transporter Sodium-dependent Imino Transporter 1 (SIT1) (SLC6A20), associations that are required for the surface expression of these transport proteins. These heterodimers can form quaternary structures able to function as binding sites for SARS-CoV-2 spike glycoproteins. The heterodimerization of the carboxypeptidase ACE2 with B0AT1 is suggested to favor the direct supply of substrate amino acids to the transporter, but whether this association impacts the ability of ACE2 to mediate viral infection is not known. B0AT1 mutations cause Hartnup disorder, a condition characterized by neutral aminoaciduria and, in some cases, pellagra-like symptoms, such as photosensitive rash, diarrhea, and cerebellar ataxia. Correspondingly, the lack of ACE2 and the concurrent absence of B0AT1 expression in small intestine causes a decrease in l-tryptophan absorption, niacin deficiency, decreased intestinal antimicrobial peptide production, and increased susceptibility to inflammatory bowel disease (IBD) in mice. Thus, the abundant expression of ACE2 in small intestine and its association with amino acid transporters appears to play a crucial role for the digestion of peptides and the absorption of amino acids and, thereby, for the maintenance of structural and functional gut integrity.


2009 ◽  
Vol 139 (9) ◽  
pp. 1677-1684 ◽  
Author(s):  
Juliana Pérez Laspiur ◽  
Jeanne L. Burton ◽  
Patty S. D. Weber ◽  
Julie Moore ◽  
Roy N. Kirkwood ◽  
...  

2019 ◽  
Vol 47 (2) ◽  
pp. 571-590 ◽  
Author(s):  
Kiran Javed ◽  
Stephen J. Fairweather

Abstract Amino acids are increasingly recognised as modulators of nutrient disposal, including their role in regulating blood glucose through interactions with insulin signalling. More recently, cellular membrane transporters of amino acids have been shown to form a pivotal part of this regulation as they are primarily responsible for controlling cellular and circulating amino acid concentrations. The availability of amino acids regulated by transporters can amplify insulin secretion and modulate insulin signalling in various tissues. In addition, insulin itself can regulate the expression of numerous amino acid transporters. This review focuses on amino acid transporters linked to the regulation of insulin secretion and signalling with a focus on those of the small intestine, pancreatic β-islet cells and insulin-responsive tissues, liver and skeletal muscle. We summarise the role of the amino acid transporter B0AT1 (SLC6A19) and peptide transporter PEPT1 (SLC15A1) in the modulation of global insulin signalling via the liver-secreted hormone fibroblast growth factor 21 (FGF21). The role of vesicular vGLUT (SLC17) and mitochondrial SLC25 transporters in providing glutamate for the potentiation of insulin secretion is covered. We also survey the roles SNAT (SLC38) family and LAT1 (SLC7A5) amino acid transporters play in the regulation of and by insulin in numerous affective tissues. We hypothesise the small intestine amino acid transporter B0AT1 represents a crucial nexus between insulin, FGF21 and incretin hormone signalling pathways. The aim is to give an integrated overview of the important role amino acid transporters have been found to play in insulin-regulated nutrient signalling.


Author(s):  
Stefano Maric ◽  
Pascal Flüchter ◽  
Laura Chiara Guglielmetti ◽  
Ralph Fabian Staerkle ◽  
Tom Sasse ◽  
...  

2018 ◽  
Vol 315 (5) ◽  
pp. G887-G895 ◽  
Author(s):  
C. Meier ◽  
S. M. Camargo ◽  
S. Hunziker ◽  
U. Moehrlen ◽  
S. J. Gros ◽  
...  

The expression of amino acid transporters in small intestine epithelia of human newborns has not been studied yet. It is further not known whether the maturation of imino acid (proline) transport is delayed as in the kidney proximal tubule. The possibility to obtain small intestinal tissue from patients undergoing surgery for jejunal or ileal atresia during their first days after birth was used to address these questions. As control, adult terminal ileum tissue was sampled during routine endoscopies. Gene expression of luminal imino and amino acid transporter SIT1 (SLC6A20) was approximately threefold lower in newborns versus adults. mRNA levels of all other luminal and basolateral amino acid transporters and accessory proteins tested were similar in newborn mucosa compared with adults. At the protein level, the major luminal neutral amino acid transporter B0AT1 (SLC6A19) and its accessory protein angiotensin-converting enzyme 2 were shown by immunofluorescence to be expressed similarly in newborns and in adults. SIT1 protein was not detectable in the small intestine of human newborns, in contrast to adults. The morphology of newborn intestinal mucosa proximal and distal to the obstruction was generally normal, but a decreased proliferation rate was visualized distally of the atresia by lower levels of the mitosis marker Ki-67. The mRNA level of the 13 tested amino acid transporters and accessory proteins was nonetheless similar, suggesting that the intestinal obstruction and interruption of amniotic fluid passage through the small intestinal lumen did not affect amino acid transporter expression. NEW & NOTEWORTHY System IMINO transporter SIT1 is not expressed in the small intestine of human newborns. This new finding resembles the situation in the proximal kidney tubule leading to iminoglycinuria. Lack of amniotic fluid passage in small intestinal atresia does not affect amino acid transporter expression distal to intestinal occlusion.


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