Transport of neutral and cationic amino acids across the brush-border membrane of the rabbit ileum

Munck, B. G.

doi:10.1007/bf01868733

Cited by 49 publications

(20 citation statements)

References 28 publications

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“…However, in some studies a cationic amino acid transport activity has been described resembling system y ϩ in nonepithelial cells (357). A number of studies clearly established the presence of a Na ϩ -independent transporter for neutral and cationic amino acids (226,228,229,264). As a result, this transporter has been classified as system b 0,ϩ to indicate its similarity to the system defined in mouse blastocysts (388).…”

Section: Transport Of Cationic Amino Acids and Cystine Across The Apimentioning

confidence: 97%

“…System B 0,ϩ is defined as a Na ϩ -dependent high-affinity transporter for neutral and cationic amino acids and was first described in mouse blastocysts (389). A transporter with very similar properties was functionally detected in rabbit distal ileum (226). In an attempt to identify novel neurotransmitter transporters, Sloan and Mager (348) cloned a cDNA from human mammary gland that encoded a transporter of 634 amino acids which had significant sequence homology to brain glycine transporters GLYT1 and GLYT2 (348).…”

Section: The System B 0ϩ Neutral and Cationic Amino Acid Transportermentioning

confidence: 98%

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Amino Acid Transport Across Mammalian Intestinal and Renal Epithelia

Bröer

2008

Physiological Reviews

811

671

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The transport of amino acids in kidney and intestine is critical for the supply of amino acids to all tissues and the homeostasis of plasma amino acid levels. This is illustrated by a number of inherited disorders affecting amino acid transport in epithelial cells, such as cystinuria, lysinuric protein intolerance, Hartnup disorder, iminoglycinuria, dicarboxylic aminoaciduria, and some other less well-described disturbances of amino acid transport. The identification of most epithelial amino acid transporters over the past 15 years allows the definition of these disorders at the molecular level and provides a clear picture of the functional cooperation between transporters in the apical and basolateral membranes of mammalian epithelial cells. Transport of amino acids across the apical membrane not only makes use of sodium-dependent symporters, but also uses the proton-motive force and the gradient of other amino acids to efficiently absorb amino acids from the lumen. In the basolateral membrane, antiporters cooperate with facilitators to release amino acids without depleting cells of valuable nutrients. With very few exceptions, individual amino acids are transported by more than one transporter, providing backup capacity for absorption in the case of mutational inactivation of a transport system.

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Section: Transport Of Cationic Amino Acids and Cystine Across The Apimentioning

confidence: 97%

Section: The System B 0ϩ Neutral and Cationic Amino Acid Transportermentioning

confidence: 98%

Amino Acid Transport Across Mammalian Intestinal and Renal Epithelia

Bröer

2008

Physiological Reviews

811

671

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“…The neutral amino acids enter the rabbit jejunal brush border membrane vesicles via three transport routes: non-saturable simple diffusion, Na'hdependent carriers and Na+ -dependent carriers (Stevens et al, 1982(Stevens et al, , 1984Munck, 1985;Harig, 1989). T w o groups of experiments were carried out to determine which L-threonine systems of transport could be affected by EM.…”

Section: Discussionmentioning

confidence: 99%

“…Early results seem to indicate that EM could decrease the L-threonine transport across the mucosal border. It has been demonstrated that .neutral amino acids are transported across the brush border by both Na+dependent and Na+-independent systems of transport (Stevens et al, 1982(Stevens et al, , 1984Munck, 1985;Harig el al., 1989).…”

Section: Effect Of E?ythromycin C M L-threonine Transportmentioning

confidence: 99%

Effect of erythromycin on L‐threonine transport in rabbit jejunum in vitro

Navarro¹,

Arruebo²,

Sorribas³

et al. 1992

Vet Pharm & Therapeutics

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Several antibiotics characterized by different molecular structures are known to affect some intestinal activities. Some of them have been described as inhibitors of the intestinal sugar and amino acid transport with different mechanisms. Erythromycin (EM) is a macrolide antibiotic acting as a motilin agonist and thus stimulating the gastrointestinal motor activity. Since several substances which increase the motor activity of the gastrointestinal tract may produce effects on the intestinal absorption of nutrients, the present study has been carried out to determine whether erythromycin affects the L-threonine intestinal absorption. The results obtained indicate that erythromycin diminishes the L-threonine intestinal transport, probably at the mucosal border level. Two groups of experiments carried out, with Na(+)-deprived medium and ouabain-enriched medium, might indicate that erythromycin action could be due to either a direct or an indirect action on the Na(+)-dependent L-threonine transport located in the brush border.

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“…Food protein is an essential nutrient needed by the human body for growth and maintenance. Traditionally, it is believed that food proteins are digested in the gastrointestinal tract by enzymes to amino acids, dipeptides, and tripeptides and then absorbed into the enterocyte across the brush‐border membrane via multiple amino acid and peptide transport systems . The absorption of peptides is more efficient than free amino acids .…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of cow's milk proteins from the rat intestinal lymph using a proteomic strategy

Wei

Jia

et al. 2013

Proteomics

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Food proteins were considered to be absorbed into the body after being digested to amino acids, dipeptides, and tripeptides. However, there are studies indicating that some proteins can pass through the intestinal epithelium under normal physiological conditions, perhaps not in sufficient quantities to be of nutritional importance, but in quantities that may be antigenically or biologically active. In the present study, rat intestinal lymph samples were collected using a modified lymph fistula rat model in fasting and cow's milk postprandial states. Low molecular weight proteins were enriched by ultrafiltration and differential solubilization, separated by 1D-SDS-PAGE, digested in-gel based on molecular weight, and identified using nano-LC-MS/MS. In the postprandial rat intestinal lymph, nine bovine-specific proteins (false discovery rate ≤1%) were identified in different molecular weight regions. Most proteins identified in lymph were highly abundant proteins in the milk, such as β-lactoglobulin and caseins. Seven of the nine identified bovine-specific proteins are allergens in milk. This strategy can be used to search for proteins that can enter the intestinal lymph and analyze their common features. Understanding the common features of these proteins might help to develop protein drugs taken orally, so that therapeutic proteins might embody fusion domains for cross-barrier transport or translocation.

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Transport of neutral and cationic amino acids across the brush-border membrane of the rabbit ileum

Cited by 49 publications

References 28 publications

Amino Acid Transport Across Mammalian Intestinal and Renal Epithelia

Amino Acid Transport Across Mammalian Intestinal and Renal Epithelia

Effect of erythromycin on L‐threonine transport in rabbit jejunum in vitro

Identification and characterization of cow's milk proteins from the rat intestinal lymph using a proteomic strategy

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