scholarly journals Peptide Transporter 1 Is Responsible for Intestinal Uptake of the Dipeptide Glycylsarcosine: Studies in Everted Jejunal Rings from Wild-type and Pept1 Null Mice

2011 ◽  
Vol 100 (2) ◽  
pp. 767-774 ◽  
Author(s):  
Katherine Ma ◽  
Yongjun Hu ◽  
David E. Smith
Keyword(s):  
Peptide Transporter ◽  
Wild Type ◽  
Intestinal Uptake ◽  
Peptide Transporter 1

scholarly journals Diabetes downregulates peptide transporter 1 in the rat jejunum: possible involvement of cholate-induced FXR activation

2020 ◽  
Vol 41 (11) ◽  
pp. 1465-1475
Author(s):  
Li-min Liang ◽  
Jun-jie Zhou ◽  
Feng Xu ◽  
Pei-hua Liu ◽  
Lan Qin ◽  
...  
Keyword(s):  
Peptide Transporter ◽  
Rat Jejunum ◽  
Peptide Transporter 1

Oseltamivir (Tamiflu) Is a Substrate of Peptide Transporter 1

2009 ◽  
Vol 37 (8) ◽  
pp. 1676-1681 ◽  
Author(s):  
Takuo Ogihara ◽  
Takashi Kano ◽  
Tamae Wagatsuma ◽  
Sho Wada ◽  
Hikaru Yabuuchi ◽  
...  
Keyword(s):  
Peptide Transporter ◽  
Peptide Transporter 1

scholarly journals Regulation profile of the intestinal peptide transporter 1 (PepT1)

2017 ◽  
Vol Volume 11 ◽  
pp. 3511-3517 ◽  
Author(s):  
Chun-Yang Wang ◽  
Shu Liu ◽  
Xiao-Nv Xie ◽  
Zhi-Rong Tan
Keyword(s):  
Peptide Transporter ◽  
Peptide Transporter 1

scholarly journals Characterization of the Opp Peptide Transporter ofCorynebacterium pseudotuberculosisand Its Role in Virulence and Pathogenicity

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Pablo M. R. O. Moraes ◽  
Nubia Seyffert ◽  
Wanderson M. Silva ◽  
Thiago L. P. Castro ◽  
Renata F. Silva ◽  
...  
Keyword(s):  
Pathogenic Bacteria ◽  
Etiologic Agent ◽  
Peptide Transporter ◽  
Intercellular Signaling ◽  
Wild Type ◽  
Cell Nutrition ◽  
Oligopeptide Permease ◽  
Extracellular Environment

Despite the economic importance of caseous lymphadenitis (CLA), a chronic disease caused byCorynebacterium pseudotuberculosis, few genes related to the virulence of its etiologic agent have been characterized. The oligopeptide permease (Opp) transporters are located in the plasma membrane and have functions generally related to the uptake of peptides from the extracellular environment. These peptide transporters, in addition to having an important role in cell nutrition, also participate in the regulation of various processes involving intercellular signaling, including the control of the expression of virulence genes in pathogenic bacteria. To study the role of Opp inC. pseudotuberculosis, an OppD deficient strain was constructed via simple crossover with a nonreplicative plasmid carrying part of theoppDgene sequence. As occurred to the wild-type, the ΔoppDstrain showed impaired growth when exposed to the toxic glutathione peptide (GSH), indicating two possible scenarios: (i) that this component can be internalized by the bacterium through an Opp-independent pathway or (ii) that there is toxicity while the peptide is extracellular. Additionally, the ΔoppDmutant presented a reduced ability to adhere to and infect macrophages compared to the wild-type, although both strains exhibit the same potential to colonize spleens and cause injury and death to infected mice.

scholarly journals A Peptide Permease Mutant of Mycobacterium bovis BCG Resistant to the Toxic Peptides Glutathione andS-Nitrosoglutathione

2000 ◽  
Vol 68 (2) ◽  
pp. 429-436 ◽  
Author(s):  
Renee M. Green ◽  
Anjali Seth ◽  
Nancy D. Connell
Keyword(s):  
Mutant Strain ◽  
Mycobacterium Bovis ◽  
Mammalian Cells ◽  
Sole Source ◽  
Cosmid Library ◽  
Peptide Transporter ◽  
Wild Type ◽  
Genome Database ◽  
Mutant Strains ◽  
Oligopeptide Permease

ABSTRACT Oligopeptides play important roles in bacterial nutrition and signaling. Using sequences from the available genome database forMycobacterium tuberculosis H37Rv, the oligopeptide permease operon (oppBCDA) of Mycobacterium bovis BCG was cloned from a cosmid library. An opp mutant strain was constructed by homologous recombination with an allele ofoppD interrupted by kanamycin and streptomycin resistance markers. The deletion was complemented with a wild-type copy of theopp operon. Two approaches were taken to characterize the peptide transporter defect in this mutant strain. First, growth of wild-type and mutant strains was monitored in media containing a wide variety of peptides as sole source of carbon and/or nitrogen. Among 25 peptides ranging from two to six amino acids in length, none was capable of supporting measurable growth as the sole carbon source in either wild-type or mutant strains. The second approach exploited the resistance of permease mutants to toxic substrates. The tripeptide glutathione (γ-glutamyl-l-cyteinylglycine [GSH]) is toxic to wild-type BCG and was used successfully to characterize peptide uptake in the opp mutant. In 2 mM GSH, growth of the wild-type strain is inhibited, whereas the opp mutant is resistant to concentrations as high as 10 mM. Similar results were found with the tripeptide S-nitrosoglutathione (GSNO), thought to be a donor of NO in mammalian cells. Using incorporation of [3H]uracil to monitor the effects of GSH and GSNO on macromolecular synthesis in growing cells, it was demonstrated that theopp mutant is resistant, whereas the wild type and the mutant complemented with a wild-type copy of the operon are sensitive to both tripeptides. In uptake measurements, incorporation of [3H]GSH is reduced in the mutant compared with wild type and the complemented mutant. Finally, growth of the three strains in the tripeptides suggests that GSH is bacteriostatic, whereas GSNO is bacteriocidal.

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