Differential expression of the TFF-peptides xP1 and xP4 in the gastrointestinal tract of Xenopus laevis

1997 ◽  
Vol 291 (1) ◽  
pp. 13-18 ◽  
Author(s):  
Wolfgang Jagla ◽  
Antje Wiede ◽  
Sabine K�lle ◽  
W. Hoffmann
Keyword(s):  
Gastrointestinal Tract ◽  
Xenopus Laevis ◽  
Differential Expression ◽  
Tff Peptides

Differential expression of two TEF-1 (TEAD) genes during Xenopus laevis development and in response to inducing factors

2007 ◽  
Vol 51 (8) ◽  
pp. 745-752 ◽  
Author(s):  
Francois Naye ◽  
Karine Treguer ◽  
Fabienne Soulet ◽  
Corinne Faucheux ◽  
Sandrine Fedou ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Differential Expression ◽  
Inducing Factors

scholarly journals Transcriptionally inactive oocyte-type 5S RNA genes of Xenopus laevis are complexed with TFIIIA in vitro.

1987 ◽  
Vol 7 (10) ◽  
pp. 3503-3510 ◽  
Author(s):  
L J Peck ◽  
L Millstein ◽  
P Eversole-Cire ◽  
J M Gottesfeld ◽  
A Varshavsky
Keyword(s):  
Xenopus Laevis ◽  
Differential Expression ◽  
Gene Transcription ◽  
Nuclear Extract ◽  
In Vitro Transcription ◽  
5S Rna ◽  
Differential Binding ◽  
5S Rna Genes ◽  
Rna Genes

An extract from whole oocytes of Xenopus laevis was shown to transcribe somatic-type 5S RNA genes approximately 100-fold more efficiently than oocyte-type 5S RNA genes. This preference was at least 10-fold greater than the preference seen upon microinjection of 5S RNA genes into oocyte nuclei or upon in vitro transcription in an oocyte nuclear extract. The approximately 100-fold transcriptional bias in favor of the somatic-type 5S RNA genes observed in vitro in the whole oocyte extract was similar to the transcriptional bias observed in developing Xenopus embryos. We also showed that in the whole oocyte extract, a promoter-binding protein required for 5S RNA gene transcription, TFIIIA, was bound both to the actively transcribed somatic-type 5S RNA gene and to the largely inactive oocyte-type 5S RNA genes. These findings suggest that the mechanism for the differential expression of 5S RNA genes during Xenopus development does not involve differential binding of TFIIIA to 5S RNA genes.

Localization of xenopsin and xenopsin precursor fragment immunoreactivities in the skin and gastrointestinal tract of Xenopus laevis

1992 ◽  
Vol 270 (2) ◽  
pp. 257-263 ◽  
Author(s):  
Kirsten C. Sadler ◽  
Charles L. Bevins ◽  
Jane C. Kaltenbach
Keyword(s):  
Gastrointestinal Tract ◽  
Xenopus Laevis

scholarly journals Differential expression of arid5b isoforms in Xenopus laevis pronephros

2014 ◽  
Vol 58 (5) ◽  
pp. 363-368
Author(s):  
Ronan Le Bouffant ◽  
Anne-Claire Cunin ◽  
Isabelle Buisson ◽  
Jérôme Cartry ◽  
Jean-François Riou ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Differential Expression

Effect of sequence differences between somatic and oocyte 5S RNA genes on transcriptional efficiency in an oocyte S150 extract

1988 ◽  
Vol 8 (11) ◽  
pp. 5056-5058
Author(s):  
W F Reynolds
Keyword(s):  
Xenopus Laevis ◽  
Differential Expression ◽  
Internal Control ◽  
Transcriptional Activity ◽  
Stable Complex ◽  
5S Rna ◽  
Internal Control Region ◽  
5S Rna Genes ◽  
Rna Genes ◽  
5S Gene

The differential expression of the Xenopus laevis somatic and oocyte 5S RNA genes is partially, but not solely, due to several base differences near the 5' boundary of the internal control region. A hybrid oocyte 5S gene with somatic-type base changes at +47, +53, +55, and +56 had intermediate transcriptional activity in oocyte S150 extracts. These base substitutions also resulted in increased affinity for a factor(s), other than TFIIIA, which forms a stable complex with the 5S gene.

scholarly journals The TFF Peptides xP1 and xP4 Appear in Distinctive Forms in the Xenopus laevis Gastric Mucosa: Indications for Different Protective Functions

2019 ◽  
Vol 20 (23) ◽  
pp. 6052 ◽  
Author(s):  
Stürmer ◽  
Reising ◽  
Hoffmann
Keyword(s):  
Gastric Mucosa ◽  
Xenopus Laevis ◽  
Molecular Mass ◽  
Molecular Forms ◽  
Binding Studies ◽  
Mucus Barrier ◽  
A Minor ◽  
Tff Peptides ◽  
Mass Form

The gastric secretory trefoil factor family (TFF) peptides xP1 and xP4 are the Xenopus laevis orthologs of mammalian TFF1 and TFF2, respectively. The aim of this study was to analyze the molecular forms of xP1 and xP4 in the X. laevis gastric mucosa by FPLC. xP1 mainly occurred in a monomeric low-molecular-mass form and only a minor subset is associated with the mucus fraction. The occurrence of monomeric xP1 is unexpected because of its odd number of cysteine residues. Probably a conserved acidic residue flanking Cys55 allows monomeric secretion. Furthermore, Cys55 is probably post-translationally modified. For the first time, we hypothesize that the free thiol of monomeric xP1-and probably also its mammalian ortholog TFF1-could have a protective scavenger function, e.g., for reactive oxygen/nitrogen species. In contrast, xP4 mainly occurs in a high-molecular-mass form and is non-covalently bound to a mucin similarly as TFF2. In vitro binding studies with radioactively labeled porcine TFF2 even showed binding to X. laevis gastric mucin. Thus, xP4 is expected to bind as a lectin to an evolutionary conserved sugar epitope of the X. laevis ortholog of mucin MUC6 creating a tight mucus barrier. Taken together, xP1 and xP4 appear to have different gastric protective functions.

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