mBio, 2018 Staphylococcus aureus is responsible for a significant amount of devastating disease. Its ability to colonize the host and cause infection is supported by a variety of proteins that are dependent on the cofactor heme.
Jacob E. Choby +5 more
doaj +1 more source
New Marker of Colon Cancer Risk Associated with Heme Intake: 1,4-Dihydroxynonane Mercapturic Acid [PDF]
, 2006 Background: Red meat consumption is associated with an increased risk of colon cancer. Animal studies show that heme, found in red meat, promotes preneoplastic lesions in the colon, probably due to the oxidative properties of this compound.
G. Gottardi +21 more
core +1 more source
Heme catabolism by heme oxygenase-1 confers host resistance to Mycobacterium infection [PDF]
, 2013 Heme oxygenases (HO) catalyze the rate-limiting step of heme degradation. The cytoprotective action of the inducible HO-1 isoform, encoded by the Hmox1 gene, is required for host protection against systemic infections. Here we report that upregulation of
Larsen, Rasmus +10 more
core +1 more source
Heme Oxygenase-2 Is a Hemoprotein and Binds Heme through Heme Regulatory Motifs That Are Not Involved in Heme Catalysis [PDF]
Journal of Biological Chemistry, 1997 The heme oxygenase (HO) system degrades heme to biliverdin and CO and releases chelated iron. In the primary sequence of the constitutive form, HO-2, there are three potential heme binding sites: two heme regulatory motifs (HRMs) with the absolutely conserved Cys-Pro pair, and a conserved 24-residue heme catalytic pocket with a histidine residue ...
W K, McCoubrey, T J, Huang, M D, Maines
openaire +2 more sources
HMOX1 gene promoter alleles and high HO-1 levels are associated with severe malaria in Gambian children. [PDF]
, 2012 Heme oxygenase 1 (HO-1) is an essential enzyme induced by heme and multiple stimuli associated with critical illness. In humans, polymorphisms in the HMOX1 gene promoter may influence the magnitude of HO-1 expression.
Madi Njie (177625) +101 more
core +1 more source
The heme-responsive PrrH sRNA regulates Pseudomonas aeruginosa pyochelin gene expression
mSphere, 2023 Pseudomonas aeruginosa is an opportunistic pathogen that requires iron for growth and virulence, yet this nutrient is sequestered by the innate immune system during infection. When iron is limiting, P. aeruginosa expresses the PrrF1 and PrrF2 small RNAs (
Tra-My Hoang +8 more
doaj +1 more source
Frontiers in Microbiology, 2020 Ferric uptake regulator (Fur) is a transcriptional regulator playing a central role in iron homeostasis of many bacteria, and Fur inactivation commonly results in pleiotropic phenotypes.
Lulu Liu +5 more
doaj +1 more source
Proposed mechanisms for free-heme-dependent potentiation of lung infection after trauma hemorrhage. [PDF]
, 2018 We hypothesize that when resuscitation with stored red blood cells (RBCs) leads to increased circulating heme that is in excess of hemopexin, 2 parallel pathways are activated involving (i) release of HMGB1 and subsequent decreased immune-cell-dependent ...
Jean-Francois Pittet (254567) +14 more
core +1 more source
Dual role of heme iron in cancer; promotor of carcinogenesis and an inducer of tumour suppression [PDF]
, 2021 PURPOSE: Heme is a crucial compound for cell survival but is also equipped with the potential to be toxic and carcinogenic to cells. However, with the recent advancement of knowledge regarding ferroptosis, the iron mediated cell death, heme can be ...
Lee, Katherine TW +4 more
core +1 more source
Heme oxygenation and the widening paradigm of heme degradation [PDF]
Archives of Biochemistry and Biophysics, 2014 Heme degradation through the action of heme oxygenase (HO) is unusual in that it utilizes heme as both a substrate and cofactor for its own degradation. HO catalyzes the oxygen-dependent degradation of heme to biliverdin with the release of CO and "free" iron.
Angela, Wilks, Geoffrey, Heinzl
openaire +2 more sources