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2014 ; 20
(11
): 1709-22
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Heme oxygenase-1: a metabolic nike
#MMPMID24180257
Wegiel B
; Nemeth Z
; Correa-Costa M
; Bulmer AC
; Otterbein LE
Antioxid Redox Signal
2014[Apr]; 20
(11
): 1709-22
PMID24180257
show ga
SIGNIFICANCE: Heme degradation, which was described more than 30 years ago, is
still very actively explored with many novel discoveries on its role in various
disease models every year. RECENT ADVANCES: The heme oxygenases (HO) are
metabolic enzymes that utilize NADPH and oxygen to break apart the heme moiety
liberating biliverdin (BV), carbon monoxide (CO), and iron. Heme that is derived
from hemoproteins can be toxic to the cells and if not removed immediately, it
causes cell apoptosis and local inflammation. Elimination of heme from the milieu
enables generation of three products that influences numerous metabolic changes
in the cell. CRITICAL ISSUES: CO has profound effects on mitochondria and
cellular respiration and other hemoproteins to which it can bind and affect their
function, while BV and bilirubin (BR), the substrate and product of BV,
reductase, respectively, are potent antioxidants. Sequestration of iron into
ferritin and its recycling in the tissues is a part of the homeodynamic processes
that control oxidation-reduction in cellular metabolism. Further, heme is an
important component of a number of metabolic enzymes, and, therefore, HO-1 plays
an important role in the modulation of cellular bioenergetics. FUTURE DIRECTIONS:
In this review, we describe the cross-talk between heme oxygenase-1 (HO-1) and
its products with other metabolic pathways. HO-1, which we have labeled Nike, the
goddess who personified victory, dictates triumph over pathophysiologic
conditions, including diabetes, ischemia, and cancer.
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