PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21084130-0 2011 Regulation of the expression of the hepatocellular sulfate-oxalate exchanger SAT-1 (SLC26A1) by glyoxylate: a metabolic link between liver and kidney? glyoxylic acid 96-106 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 77-82 21093948-0 2011 Glyoxylate is a substrate of the sulfate-oxalate exchanger, sat-1, and increases its expression in HepG2 cells. glyoxylic acid 0-10 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 60-65 21093948-4 2011 METHODS: Sat-1 expressing oocytes were used for cis-inhibition, trans-stimulation, and efflux experiments with labelled sulfate and oxalate to demonstrate the interactions of oxalate, glyoxylate, and glycolate with sat-1. glyoxylic acid 184-194 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 9-14 21093948-12 2011 Glyoxylate was the only oxalate precursor stimulating sat-1 mRNA-expression. glyoxylic acid 0-10 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 54-59 21093948-13 2011 After incubation of HepG2 cells in glyoxylate, both sat-1 protein-expression and sulfate uptake into the cells increased. glyoxylic acid 35-45 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 52-57 21093948-15 2011 CONCLUSIONS: The oxalate precursor glyoxylate was identified as a substrate of sat-1. glyoxylic acid 35-45 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 79-84 21093948-16 2011 Upregulated expression of sat-1 mRNA and of a functional sat-1 protein indicates that glyoxylate may be responsible for the elevated oxalate release from hepatocytes observed in hyperoxaluria. glyoxylic acid 86-96 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 26-31 21093948-16 2011 Upregulated expression of sat-1 mRNA and of a functional sat-1 protein indicates that glyoxylate may be responsible for the elevated oxalate release from hepatocytes observed in hyperoxaluria. glyoxylic acid 86-96 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 57-62