| Literature DB >> 9952219 |
Abstract
This paper describes the identification and characterization of a novel cDNA encoding a putative protein of 254 amino acids that is highly homologous to triosephosphate isomerase. The cDNA was isolated by subtractive hybridization and was differentially expressed in the remnant rat ileum after massive small bowel resection. The novel triosephosphate isomerase was named rsTPI (resection-induced TPI) and the putative protein encoded RSTPI. The nucleotide and amino acid sequences of rsTPI and RSTPI were about 60% and 62% homologous to Giardia lamblia TPI and TPI, respectively. Active catalytic sites (Lys 13, His 95, and Glu 167) and the peptide motifs, AYEPVWSIGT and GGASLKPEF found in other triosephosphate isomerases were conserved in RSTPI. rsTPI expression was detected in normal ileum and pancreas by reverse transcription-polymerase chain reaction. Expression of rsTPI in remnant rat ileum was detectable by northern blot analysis one week after massive small bowel resection. Expression increased significantly by 2.8-fold between one and two weeks after surgery. High levels were maintained for at least one month after surgery. The up-regulation of triosephosphate isomerase expression in the remnant small intestine after massive resection indicates that it may play an important role in the adaptive process.Entities:
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Year: 1999 PMID: 9952219 DOI: 10.1023/a:1026685613212
Source DB: PubMed Journal: Dig Dis Sci ISSN: 0163-2116 Impact factor: 3.199