Structure of the Xenopus laevis TFF-gene xP4.1, differentially expressed to its duplicated homolog xP4.2.
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| Abstract |
TFF-peptides (formerly P-domain peptides, trefoil factors) represent major secretory products of mucous epithelia in mammals and amphibia. The nucleotide sequence of a large portion of a gene encoding the TFF-peptide xP4.1 from Xenopus laevis and its genomic organization were determined in the present study. The peptide xP4.1 containing four TFF-domains is thought to represent the functional frog homolog of human TFF2 (formerly hSP). The xP4.1 gene analyzed spans a region of about 7 kb and consists of six exons. Each TFF-domain is encoded by a single exon flanked by type 1 introns typical of shuffled modules. The 5'-upstream region contains a TATA-box, and potential binding sites for hepatocyte nuclear factor 3 and AP-1. Furthermore, the cDNA sequence of a transcript named xP4.2 with 91% similarity to xP4.1 is presented. RT-PCR analysis revealed that xP4.1 and xP4.2 genes are differentially expressed. xP4.1 transcripts are detectable only in the stomach, but not in the esophagus, whereas xP4.2 transcripts are found both in the esophagus and in the stomach with a descending gradient from fundus to antrum.
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| Authors | C Botzler, M Oertel, M Hinz, W Hoffmann |
| Journal | Biochimica et biophysica acta (Biochim Biophys Acta) Vol. 1489 Issue 2-3 Pg. 345-53 (Dec 23 1999) ISSN: 0006-3002 [Print] Netherlands |
| PMID | 10673035 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't) |
| Chemical References |
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