Results 31 to 40 of about 4,768 (212)

Diagnosis and treatment of icteric hepatitis caused by erythropoietic protoporphyria: A case report

Liver Research, 2022
Erythropoietic protoporphyria (EPP) is a rare inherited disease caused by partial deficiency activity of the enzyme ferrochelatase (FECH), resulting in excessive accumulation of protoporphyrin IX in erythrocyte and tissues. Here, we report a patient with
Hanqing Huang, Leiqin Cai, Xinhua Li, Shuru Chen   +3 more
doaj   +1 more source

Ferrochelatase of spinach chloroplasts [PDF]

Biochemical Journal, 1968
Spinach chloroplasts catalyse the incorporation of Fe2+ into protoporphyrin, mesoporphyrin and deuteroporphyrin to form the corresponding haems. This ferrochelatase activity was detected by pyridine haemochrome formation with acetone-dried powders of chloroplasts, or from the formation of [59Fe]haems by intact chloroplasts. Decreasing the mitochondrial
openaire   +2 more sources

Substrate interactions with human ferrochelatase [PDF]

Proceedings of the National Academy of Sciences, 2007
Ferrochelatase, the terminal enzyme in heme biosynthesis, catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX. Human ferrochelatase is a homodimeric, inner mitochondrial membrane-associated enzyme that possesses an essential [2Fe-2S] cluster.
Amy, Medlock, Larkin, Swartz, Tamara A, Dailey, Harry A, Dailey, William N, Lanzilotta   +4 more
openaire   +2 more sources

Hyperlipidemia and atherosclerosis associated with liver disease in ferrochelatase-deficient mice1

Journal of Lipid Research, 2001
Erythropoietic protoporphyria (EPP) is an inherited disorder of heme synthesis caused by deficiency of the mitochondrial enzyme ferrochelatase. EPP in humans is associated with liver disease, hypertriglyceridemia, and a low level of high density ...
Vincent W. Bloks, Torsten Plösch, Harry van Goor, Han Roelofsen, Juul Baller, Rick Havinga, Henkjan J. Verkade, Aad van Tol, Peter L.M. Jansen, Folkert Kuipers   +9 more
doaj   +1 more source

Inhibition of ferrochelatase impairs vascular eNOS/NO and sGC/cGMP signaling. [PDF]

PLoS ONE, 2018
Ferrochelatase (FECH) is an enzyme necessary for heme synthesis, which is essential for maintaining normal functions of endothelial nitric oxide synthase (eNOS) and soluble guanylyl cyclase (sGC). We tested the hypothesis that inhibition of vascular FECH
Bin Zhang, Norah Alruwaili, Sharath Kandhi, Wensheng Deng, An Huang, Michael S Wolin, Dong Sun   +6 more
doaj   +1 more source

Alectinib treatment improves photodynamic therapy in cancer cell lines of different origin

BMC Cancer, 2021
Background Photodynamic therapy with a photosensitizer such as protoporphyrin-IX, a light sensitive metabolite of heme synthesis, is a highly selective treatment for various carcinomas.
Bernhard Gillissen, Antje Richter, Frank Essmann, Wolfgang Kemmner   +3 more
doaj   +1 more source

Erythropoietin signaling regulates heme biosynthesis

eLife, 2017
Heme is required for survival of all cells, and in most eukaryotes, is produced through a series of eight enzymatic reactions. Although heme production is critical for many cellular processes, how it is coupled to cellular differentiation is unknown ...
Jacky Chung, Johannes G Wittig, Alireza Ghamari, Manami Maeda, Tamara A Dailey, Hector Bergonia, Martin D Kafina, Emma E Coughlin, Catherine E Minogue, Alexander S Hebert, Liangtao Li, Jerry Kaplan, Harvey F Lodish, Daniel E Bauer, Stuart H Orkin, Alan B Cantor, Takahiro Maeda, John D Phillips, Joshua J Coon, David J Pagliarini, Harry A Dailey, Barry H Paw   +21 more
doaj   +1 more source

Crosstalk between metal ions in Bacillus subtilis ferrochelatase

, 2006
Ferrochelatase (EC 4.99.1.1), the terminal enzyme in the heme biosynthetic pathway, catalyzes the insertion of Fe2+ into protoporphyrin IX, generating heme.
Hansson, Mattias, Lindstam, Mats, Hansson, Mats   +2 more
core   +2 more sources

Cloning of murine ferrochelatase. [PDF]

Proceedings of the National Academy of Sciences, 1991
Ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1) catalyzes the last step in the heme biosynthetic pathway, the chelation of ferrous iron and protoporphyrin to form heme. The activity of ferrochelatase is deficient in the inherited disease protoporphyria.
D A, Brenner, F, Frasier
openaire   +2 more sources

Direct Spectroscopic Ferrochelatase Assay. [PDF]

Methods Mol Biol
Ferrochelatases (E.C. 4.99.1.1) catalyze the insertion of ferrous iron into either protoporphyrin IX to make protoheme IX or coproporphyrin III to make coproheme III. Ferrochelatase activity in extracts or purified protein can be measured via several assays.
Dailey HA, Medlock AE.
europepmc   +3 more sources