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the regulation of PPOX (show OX Proteins) gene expression can also occur through a post-transcriptional modulation of the amount of gene product and this modulation can be mediated by 5' untranslated exon 1.
GAPDH (show GAPDH Proteins) and protoporphyrinogen oxidase were shown to have higher expression in faster growing cell lines and primary tumors. Pharmacologic inhibition of GAPDH (show GAPDH Proteins) or PPOX (show OX Proteins) reduced the growth of colon cancer cells in vitro
Variegate porphyria is the result of decreased protoporphyrinogen oxidase activity. Diet supplementation with vitamins E and C restores PPOX (show OX Proteins) gene expression in lymphocytes of variegate porphyria patients.
in the hepatic cancer tissue of two acute porphyria patients, somatic second-hit mutations result in nearly complete inactivation of PPOX (show OX Proteins) and HMBS (show HMBS Proteins)
The c.851G>T and the c.1013C>G of PPOX (show OX Proteins) gene were found in two and four unrelated families respectively. 1 experienced only photosensitivity, 1 only neurological symptoms and the 2 both clinical manifestations.
The mutation 1082-1083insC(1 base pair insertion at position 1082) in exon 10 of the PPOX (show OX Proteins) gene was prevalent in the Swiss population.
findings emphasize the usefulness of MLPA analysis as a complement to PPOX (show OX Proteins) gene sequencing analysis for comprehensive genetic diagnostics in patients with variegate prophyria
Information required for targeting to the mitochondria is contained within the first 250 amino acid residues of human PPOX (show OX Proteins).
Modulation of penetrance by the wild-type allele in dominantly inherited erythrohepatic and acute hepatic porphyrias was studied using PPOX (show OX Proteins).
Protoporphyrinogen oxidase targeting mechanism to the mitochondrion.
The tetrapyrrole biosynthetic enzyme PPO1 is required for plastid RNA editing.
determined significant differences in the proteomes of freshly ingested down boli corresponding to the presence or absence of active PPO. These results show that in the presence of PPO the forage protein is less amenable to proteolysis and provide the novel information that the protected proteins are putatively chloroplastically located.
This gene encodes the penultimate enzyme of heme biosynthesis, which catalyzes the 6-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX. Mutations in this gene cause variegate porphyria, an autosomal dominant disorder of heme metabolism resulting from a deficiency in protoporphyrinogen oxidase, an enzyme located on the inner mitochondrial membrane. Alternatively spliced transcript variants encoding the same protein have been identified.
, protoporphyrinogen oxidase
, Catechol oxidase
, polyphenol oxidase, chloroplastic