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Relevant bibliographies by topics / Oligopeptides transport systems

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Journal articles

Academic literature on the topic 'Oligopeptides transport systems'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Oligopeptides transport systems"

1

Chothe, Paresh, Nagendra Singh, and Vadivel Ganapathy. "Evidence for two different broad-specificity oligopeptide transporters in intestinal cell line Caco-2 and colonic cell line CCD841." American Journal of Physiology-Cell Physiology 300, no. 6 (2011): C1260—C1269. http://dx.doi.org/10.1152/ajpcell.00299.2010.

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Recently the existence of two different Na+-coupled oligopeptide transport systems has been described in mammalian cells. These transport systems are distinct from the previously known H+/peptide cotransporters PEPT1 and PEPT2, which transport only dipeptides and tripeptides. To date, the only peptide transport system known to exist in the intestine is PEPT1. Here we investigated the expression of the Na+-coupled oligopeptide transporters in intestinal cell lines, using the hydrolysis-resistant synthetic oligopeptides deltorphin II and [d-Ala2,d-Leu5]enkephalin (DADLE) as model substrates. Cac

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2

Verheul, Annette, Frank M. Rombouts, and Tjakko Abee. "Utilization of Oligopeptides by Listeria monocytogenes Scott A." Applied and Environmental Microbiology 64, no. 3 (1998): 1059–65. http://dx.doi.org/10.1128/aem.64.3.1059-1065.1998.

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ABSTRACT For effective utilization of peptides, Listeria monocytogenes possesses two different peptide transport systems. The first one is the previously described proton motive force (PMF)-driven di- and tripeptide transport system (A. Verheul, A. Hagting, M.-R. Amezaga, I. R. Booth, F. M. Rombouts, and T. Abee, Appl. Environ. Microbiol. 61:226–233, 1995). The present results reveal that L. monocytogenes possesses an oligopeptide transport system, presumably requiring ATP rather than the PMF as the driving force for translocation. Experiments to determine growth in a defined medium containing

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3

Hiron, Aurelia, Elise Borezée-Durant, Jean-Christophe Piard, and Vincent Juillard. "Only One of Four Oligopeptide Transport Systems Mediates Nitrogen Nutrition in Staphylococcus aureus." Journal of Bacteriology 189, no. 14 (2007): 5119–29. http://dx.doi.org/10.1128/jb.00274-07.

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ABSTRACT Oligopeptides internalized by oligopeptide permease (Opp) transporters play key roles in bacterial nutrition, signaling, and virulence. To date, two opp operons, opp-1 and opp-2, have been identified in Staphylococcus aureus. Systematic in silico analysis of 11 different S. aureus genomes revealed the existence of two new opp operons, opp-3 and opp-4, plus an opp-5A gene encoding a putative peptide-binding protein. With the exception of opp-4, the opp operons were present in all S. aureus strains. Within a single strain, the different opp operons displayed little sequence similarity a

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4

Wiles, Amy M., Houjian Cai, Fred Naider, and Jeffrey M. Becker. "Nutrient regulation of oligopeptide transport in Saccharomyces cerevisiae." Microbiology 152, no. 10 (2006): 3133–45. http://dx.doi.org/10.1099/mic.0.29055-0.

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Small peptides (2–5 amino acid residues) are transported into Saccharomyces cerevisiae via two transport systems: PTR (Peptide TRansport) for di-/tripeptides and OPT (OligoPeptide Transport) for oligopeptides of 4–5 amino acids in length. Although regulation of the PTR system has been studied in some detail, neither the regulation of the OPT family nor the environmental conditions under which family members are normally expressed have been well studied in S. cerevisiae. Using a lacZ reporter gene construct fused to 1 kb DNA from upstream of the genes OPT1 and OPT2, which encode the two S. cere

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5

Minami, H., H. Daniel, E. L. Morse, and S. A. Adibi. "Oligopeptides: mechanism of renal clearance depends on molecular structure." American Journal of Physiology-Renal Physiology 263, no. 1 (1992): F109—F115. http://dx.doi.org/10.1152/ajprenal.1992.263.1.f109.

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We have investigated the relative contribution of hydrolysis, intact transport and urinary excretion to the renal clearance of Gly-Sar, Gly-Sar-Sar, and Gly-Gly-Sar in fed and starved rats. The results obtained from isolated kidney perfusion studies are summarized as follows: 1) clearance was fastest for Gly-Gly-Sar and slowest for Gly-Sar-Sar, 2) urinary excretion of Gly-Sar-Sar exceeded that of Gly-Gly-Sar or Gly-Sar, 3) there was accumulation of products of hydrolysis of Gly-Gly-Sar in the perfusate but not of Gly-Sar or Gly-Sar-Sar, 4) isolated brush-border and basolateral membranes of ren

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6

Koide, Akiko, Marta Perego, and James A. Hoch. "ScoC Regulates Peptide Transport and Sporulation Initiation in Bacillus subtilis." Journal of Bacteriology 181, no. 13 (1999): 4114–17. http://dx.doi.org/10.1128/jb.181.13.4114-4117.1999.

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ABSTRACT Oligopeptides are transported into Bacillus subtilis by two ABC transport systems, App and Opp. Transcription of the operon encoding the Opp system was found to occur during exponential growth, whereas the app operon was induced at the onset of stationary phase. Transcription of both operons was completely curtailed by overproduction of the ScoC regulator from a multicopy plasmid and was enhanced in strains with the scoC locus deleted. ScoC, a member of the MarR family of transcription regulators, is known from previous studies to be a negative regulator of sporulation and of protease

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7

Daniel, Hannelore, and Isabel Rubio-Aliaga. "An update on renal peptide transporters." American Journal of Physiology-Renal Physiology 284, no. 5 (2003): F885—F892. http://dx.doi.org/10.1152/ajprenal.00123.2002.

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The brush-border membrane of renal epithelial cells contains PEPT1 and PEPT2 proteins that are rheogenic carriers for short-chain peptides. The carrier proteins display a distinct surface expression pattern along the proximal tubule, suggesting that initially di- and tripeptides, either filtered or released by surface-bound hydrolases from larger oligopeptides, are taken up by the low-affinity but high-capacity PEPT1 transporter and then by PEPT2, which possesses a higher affinity but lower transport capacity. Both carriers transport essentially all possible di- and tripeptides and numerous st

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8

Weinberg, Michael V., and Robert J. Maier. "Peptide Transport in Helicobacter pylori: Roles of Dpp and Opp Systems and Evidence for Additional Peptide Transporters." Journal of Bacteriology 189, no. 9 (2007): 3392–402. http://dx.doi.org/10.1128/jb.01636-06.

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ABSTRACT Despite research into the nutritional requirements of Helicobacter pylori, little is known regarding its use of complex substrates, such as peptides. Analysis of genome sequences revealed putative ABC-type transporter genes for dipeptide (dppABCDF) and oligopeptide (oppABCD) transport. Genes from each system were PCR amplified, cloned, and disrupted by cassette insertion either individually (dppA, dppB, dppC, oppA, oppB, and oppC) or to create double mutants (dppA oppA, dppB oppB, dppB dppC, and oppB oppC). Peptide-utilizing abilities of the strains were assessed by monitoring growth

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9

Dunkel, Nico, Tobias Hertlein, Renate Franz, et al. "Roles of Different Peptide Transporters in Nutrient Acquisition in Candida albicans." Eukaryotic Cell 12, no. 4 (2013): 520–28. http://dx.doi.org/10.1128/ec.00008-13.

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ABSTRACT Fungi possess two distinct proton-coupled peptide transport systems, the dipeptide/tripeptide transporters (PTR) and the oligopeptide transporters (OPT), which enable them to utilize peptides as nutrients. In the pathogenic yeast Candida albicans , peptide transporters are encoded by gene families consisting of two PTR genes and eight OPT genes. To gain insight into the functions and importance of specific peptide transporters, we generated mutants lacking the two dipeptide/tripeptide transporters Ptr2 and Ptr22, as well as the five major oligopeptide transporters Opt1 to Opt5. These

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10

Picon, A., M. A. García-Casado, and M. Nuñez. "Proteolytic activities, peptide utilization and oligopeptide transport systems of wild Lactococcus lactis strains." International Dairy Journal 20, no. 3 (2010): 156–62. http://dx.doi.org/10.1016/j.idairyj.2009.10.002.

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