Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.5.1.18 (glutathione S-transferase)
 22,582 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Saccharomyces cerevisiae mutants that were unable to utilize extracellular ethanolamine for phosphatidylethanolamine synthesis were isolated. Two of them carried recessive chromosomal mutations in a same gene and were defective in CTP:phosphoethanolamine cytidylyltransferase (ECT) activity in vitro (Ect-). In an Ect- mutant that also carried the cho1 mutation, phosphatidylethanolamine accounted for less than 2% of total phospholipids, suggesting the importance of ECT in phosphatidylethanolamine synthesis. By screening a genomic library on a low copy number vector, three complementary clones of different size were isolated. A 2.8-kb common DNA region carried an open reading frame (ORF) of 969 bp in length, of which a truncated from failed to complement the Ect- mutation. This ORF was identical to the previously isolated MUQ1 gene of unknown function. Its deduced amino acid sequence had significant similarity to CTP: phosphocholine cytidylyl-transferases of yeast and rat. The entire ORF, when combined with the glutathione S-transferase gene and expressed in Escherichia coli, exhibited ECT activity. These results indicate that the cloned gene encodes a catalytic subunit of ECT of S. cerevisiae.
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PMID:Isolation and characterization of ECT1 gene encoding CTP: phosphoethanolamine cytidylyltransferase of Saccharomyces cerevisiae. 898 74

Aberrant signalling activities of beta-catenin, originally identified as a component of cell-adhesion complexes, are now considered to be an important factor in colorectal carcinogenesis. However, recently it was shown that also gamma- as well as p120 catenins have a dual role either in cell adhesion or in affecting some gene activation. Therefore, the levels and interactions of these three catenins in human colorectal carcinoma cell lines were analysed. A great heterogeneity in the expression of all catenins tested was found in colorectal carcinoma cell lines HT29 and LS174T. Detailed analysis of beta-catenin interactions was done. GST-APC fragment-fused proteins were used to absorb beta-catenin and its complexes from cell lysates. Similarly, the E-cadherin binding capacity of the residual pool of beta-catenin was analysed using the GST-ECT construct. It was found that the level of beta-catenin does not necessarily depend either on the APC or beta-catenin gene mutations and that co-precipitation of beta-, gamma-, and p120 catenins is not limited to cells that express E-cadherin.
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PMID:Expression and interaction of different catenins in colorectal carcinoma cells. 1171 88