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2 edition of Amino acid, peptide and drug transport across monolayers of human intestinal (CAC0-2) cells in vitro. found in the catalog.

Amino acid, peptide and drug transport across monolayers of human intestinal (CAC0-2) cells in vitro.

Paul Leslie Nicklin

Amino acid, peptide and drug transport across monolayers of human intestinal (CAC0-2) cells in vitro.

by Paul Leslie Nicklin

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  • 39 Currently reading

Published by Aston University. Department of Pharmaceutical Sciences. in Birmingham .
Written in English


Edition Notes

Thesis(PhD) - Aston University, 1993.

ID Numbers
Open LibraryOL13907830M

Most common amino acid metabolism disease Cystine stones form in the bladder and kidneys Patients with this disorder lack a transporter in the proximal tubule of the kidney that absorbs cystine from the urine stream to put it back into the blood. As a result, cystine levels in the urine are much higher and crystals/stones form. John Jones provides an excellent, easy to read introduction to amino acid and peptide synthesis aimed at second and final year students. The text begins with a brief survey of the role and diversity of amino acids, peptides, and proteins in nature, and goes on to describe and explain the principal methods of chemical by:

In fact, amino acid ester prodrugs significantly improve the cellular uptake of the parent drugs via peptide transport mechanism, though there is no peptide bond in their structures. The fact that some epithelial cancer cells are rich in these transporters allows their use for the delivery of peptidomimetic anticancer agents [ 4, 76, 77, 78 ].Cited by: 2.   In the present chapter, the kinetics of drug transport and transport via drug transporters is described. The most common cell culture model for studying intestinal transport, i.e. the Caco-2 cell model is described in detail, and protocols for culturing and Cited by: 1.

Transportan is a 27 amino acid-long peptide containing 12 functional amino acids from the amino terminus of the neuropeptide galanin and mastoparan in the carboxyl terminus, connected via a lysine. Transportan is a cell-penetrating peptide as judged by indirect immunofluorescence using N epsilonbiotinyl-transportan.5/5(2). We recently showed that the transport of various FA across confluent layers of HBMEC was, in part, mediated by fatty acid transport proteins (FATPs) [5,6]. Knock down of FATP-1 and CD36 resulted in reduced FA transport. In addition, transport appeared to be dependent upon fatty acyl chain length and degree of by: 7.


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Amino acid, peptide and drug transport across monolayers of human intestinal (CAC0-2) cells in vitro by Paul Leslie Nicklin Download PDF EPUB FB2

The transport of acidic amino acids and their analogues across monolayers of human intestinal absorptive (Caco-2) cells in vitro. Nicklin PL(1), Irwin WJ, Hassan IF, Mackay M, Dixon HB. Author information: (1)Pharmaceutical Sciences Institute, Aston Cited by: The X − AG system, a sodium-dependent, acidic amino-acid transport system has been implicated in the transport of l-aspartate and l-glutamate across monolayers of human Caco-2 cells, an in vitro model of intestinal system, which shares many properties with the l-glutamate carrier present in the human jejunum, is highly saturable (> 95% at 50 μM), vectorial (apical-to Cited by: Transport of cephalexin and glycylsarcosine across MDCK and Caco-2 cell monolayers was quantified using LC-LC/MS.

Glycylsarcosine, p-aminohippuric acid (PAH), and tetraethylammonium chloride (TEA. The transport of lysine across monolayer of human cultured intestinal cells (Caco-2) depends on Na(+)-dependent and Na(+)-independent mechanism of different plasma membrane domain November This review is limited to progress made in drug transport via PepT1 over the past two years.

Previous detailed reviews on the topic of proton-coupled peptide transporters and their transport of drugs are by Brandsch [1, 2], Anderson and Thwaites [], Cao et al.

[] and Cited by: Some oligopeptides can be absorbed by Caco-2 cell monolayers intact. A recent study has reported that tight junctions were the major transport mechanism for Gln-Ile-Gly-Leu-Phe (QIGLF), a peptide derived from egg white ovalbumin with angiotensin converting enzyme (ACE)-inhibitory activity, across Caco-2 cell monolayers [].The transport of the peptide Val-Leu-Pro-Val-Pro (VLPVP), investigated Author: Huijuan Zhang, Yawen Duan, Yulin Feng, Jing Wang.

Relevance of different methods of studying amino acid/peptide transport to enteral nutrition Technique Advantages Disadvantages Examples, references Oral tolerance test Easy to administer in health and disease.

Antibiotic substrates can be proxy for peptide transport Extensive intestinal metabolism of amino acid invalidates results (e.g. Mechanisms of Transport of Amino Acids Across Membranes E J Collarini, and and D L Oxender Annual Review of Nutrition Cell And Membrane Physiology Joseph F.

Hoffman Annual Review of Physiology A Cellular Model for Active Sodium Absorption by Mammalian Colon S G SchultzCited by:   The intestinal epithelium is the primary site of absorption of nutrients such as amino acids. The asymmetric distribution of the amino acid carrier systems between the apical (AP) 3 and basolateral (BL) membranes of the intestinal cells contributes to their absorption.

The intestinal transport of amino acids has been investigated in various animal models that involve membrane by: Although other peptide transporters such as PHT1/2 (peptide‐histidine transporters) and POT (oligopeptide transporters) are also expressed in the small intestine, PepT1 is reported to be mainly involved in the transport of small peptides, as it is expressed in a comparatively larger amount at the jejunal region (Herrera‐Ruiz et al., ).

Annu Rev Physiol. ; Molecular and integrative physiology of intestinal peptide transport. Daniel H(1). Author information: (1)Molecular Nutrition Unit, Technical University of Munich, D Freising-Weihenstephan, Germany.

[email protected] Intestinal protein digestion generates a huge variety and quantity of short chain peptides that are absorbed into intestinal epithelial Cited by:   The intestinal peptide transport system has broad substrate specificities.

In addition to its physiological function of absorbing di- and tripeptides resulting from the digestion of dietary proteins, this transport system also absorbs some orally administered peptidomimetic drugs, including β-lactam antibiotics, angiotensin converting enzyme inhibitors, renin inhibitors, bestatin, thrombin Cited by: Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1 Anna-Maria Näßl Vollständiger Abdruck der von der Fakultät Wissenschaftszentrum Weihenstephan für Ernährung, Landnutzung und Umwelt der Technischen Universität München zur Erlangung des akademischen Grades eines Doktors der Naturwissenschaften.

This study evaluated the effect of three levels of digestible amino acids (DAA;and % of Cobb recommendations) on mRNA abundance of peptide (PepT1) and amino acid (AA) transporters in day-old broilers during prestarter period. Jejunal mRNA levels of the PepT1 and b0,+AT increased as DAA level increased from to %.

The expression of CAT1 mRNA in the Cited by: 6. Amino acid transport disorders are medical conditions associated with a failure of amino acids to be absorbed from the kidney or intestine. An example is Hartnup disease. Reference [ edit ]Specialty: Nephrology.

The human orthologue of the H + ‐coupled amino acid transporter (hPAT1) was cloned from the human intestinal cell line Caco‐2 and its functional characteristics evaluated in a mammalian cell heterologous expression system.

The cloned hPAT1 consists of amino acids and exhibits 85 % identity with rat PAT1. Among the various human tissues examined by Northern blot, PAT1 mRNA Cited by: PEPT1 (peptide transporter 1) Aliases: HPECT1, HPEPT1 Gene name: Solute carrier family 15 member 1 (SLC15A1) Summary.

Human peptide transporter 1 (PEPT1) is an uptake transporter primarily responsible for the absorption of dietary di- and tripeptides from the small intestinal lumen. the human small intestine [ The uptake of amino acids, for example, from the intestinal lumen is well characterized with saturable sys- tems both in the brush border and basolateral membranes [ 9, The peptide transport sys- tem, on the other hand, is not as well charac-File Size: KB.

a-Amino- isobutyric acid has been studied extensively (l-4). In the present investigation, we examined the suitability of oc-amino- isobutyric acid (2) as well as that of a new model amino acid, 1-aminocyclopentane-I-carboxylic acid, for the study of amino acid transport across the intestine.

In doing so, we encountered. For example, there is a section on the enzyme-catalysed synthesis of peptides, with suitable examples, an area often neglected in texts describing peptide synthesis.

This modern text will be of value in the amino acid, peptide and protein field, to advanced undergraduates, graduate students and Author: G. Barrett, D. Elmore.

The objective of this paper was to investigate the effects of terminal amino acids on the transport of oligopeptides across the Caco-2 cell monolayer. Ala-based tetra- and pentapeptides were designed, and the N- or C-terminal amino acid residues were replaced by different amino acids.

The results showed that the oligopeptides had a wide range of transport permeability across the Caco-2 cell Cited by: 4. Addition of amino acids and peptides to Fe uptake solutions.

Immediately prior to each experiment, each amino acid and peptide was dissolved in HBSS buffered with 10 mmol PIPES/L, pHat a concentration of 10 mmol/L. A μL volume of the appropriate amino acid or peptide was then added to a mL aliquot of each Fe uptake by: Regulation of Amino Acid Transport Systems by Amino Acid Depletion and Supplementation in Monolayer Cultures of Rat Hepatocytes” (Received for publication, J ) Darshan S.

Kelley and Van R. Potter From the McArdle Laboratory for Cancer Research, University of Wisconsin, Madison, Wisconsin