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Review
. 2021 Nov:47:102170.
doi: 10.1016/j.redox.2021.102170. Epub 2021 Oct 20.

The non-canonical effects of heme oxygenase-1, a classical fighter against oxidative stress

Jiajia Wu  1 , Siyu Li  1 , Cheng Li  1 , Liying Cui  1 , Jiajia Ma  1 , Yang Hui  2
Affiliations
Review

The non-canonical effects of heme oxygenase-1, a classical fighter against oxidative stress

Jiajia Wu et al. Redox Biol. 2021 Nov.

Abstract

The role of heme oxygenase-1 in resisting oxidative stress and cell protection has always been a hot research topic. With the continuous deepening of research, in addition to directly regulating redox by catalyzing the degradation of heme, HO-1 protein also participates in the gene expression level in a great diversity of methods, thereby initiating cell defense. Particularly the non-canonical nuclear-localized HO-1 and HO-1 protein interactions play the role of a warrior against oxidative stress. Besides, HO-1 may be a promising marker for disease prediction and detection in many clinical trials. Especially for malignant diseases, there may be new advances in the treatment of HO-1 by regulating abnormal ROS and metabolic signaling. The purpose of this review is to systematically sort out and describe several aspects of research to facilitate further detailed mechanism research and clinical application promotion in the future.

Keywords: Disease diagnosis and treatment; Gene expression control; Heme oxygenase-1; Protein-protein interaction; Redox system regulation.

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Conflict of interest statement

None.

Figures

Image 1
Graphical abstract
Fig. 1
Fig. 1
The nuclear location of HO-1 Under scores of stress stimuli, heme oxygenase-1 initiates certain protein cleavage mechanisms in cells, hydrolyzes, and removes the carboxy-terminal amino acid sequence to form a truncated protein form. The truncated HO-1 dissociates in the cytoplasm and then is transported into the cell under some vital mechanisms. What follows next, nuclear HO-1 responds to the initial emergency stimulus by regulating the expression level of the target gene. That contains a variety of potential new regulatory mechanisms.
Fig. 2
Fig. 2
The protein-protein interaction of Heme oxygenase-1 Heme oxygenase-1 protein combines with a variety of proteins, not only determines the cellular location of HO-1 but also participates in a variety of intracellular signal transduction pathways. HO-1，heme oxygenase-1; CPR, cytochrome P450 reductase; PARP, poly (ADP-ribose) polymerase; PARG, poly (ADP-ribose) glycohydrolase; Ub, ubiquitin; CO, carbon monoxide; CAV, caveolin.
See this image and copyright information in PMC

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