isoform Bpnt1 is expressed at relatively similar levels in a majority of tissues including the brain, heart, lungs, spleen, pancreas, stomach, liver, small intestine, colon, kidneys, and testes. Bpnt1 is most enriched in the enterocytes of the small intestine and the proximal tubule and thick ascending limb epithelia of the kidneys
mice deficient for bisphosphate 3'-nucleotidase Bpnt1 do not exhibit skeletal defects but instead develop severe liver pathologies, including hypoproteinemia, hepatocellular damage, and in severe cases, frank whole body edema and death. These phenotypes are accompanied by tissue-specific elevations of the substrate 3'-phosphoadenosine 5'-phosphate, up to 50fold in liver, repressed translation, and aberrant nucleolar architecture. The phenotypes of the Bpnt1 knockout are rescued by generating a double mutant mouse deficient for both 3'-phosphoadenosine 5'-phosphate synthesis and hydrolysis, consistent with a mechanism in which 3'-phosphoadenosine 5'-phosphate accumulation is toxic to tissue function independent of sulfation
while cytoplasmic bisphosphate nucleotidase Bpnt1 is widely expressed in a majority of tissues, in Bpnt1 knockout mice only the liver, duodenum, and kidneys show high levels of its substrate 3'-phosphoadenosine 5'-phosphate and nucleolar reorganization
mice deficient for bisphosphate 3'-nucleotidase Bpnt1 do not exhibit skeletal defects but instead develop severe liver pathologies, including hypoproteinemia, hepatocellular damage, and in severe cases, frank whole body edema and death. These phenotypes are accompanied by tissue-specific elevations of the substrate 3?-phosphoadenosine 5'-phosphate, up to 50fold in liver, repressed translation, and aberrant nucleolar architecture. The phenotypes of the Bpnt1 knockout are rescued by generating a double mutant mouse deficient for both 3'-phosphoadenosine 5'-phosphate synthesis and hydrolysis, consistent with a mechanism in which 3'-phosphoadenosine 5'-phosphate accumulation is toxic to tissue function independent of sulfation