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Last update 08 May 2025

HMOX2

Last update 08 May 2025

Basic Info

Synonyms

heme oxygenase (decycling) 2, Heme oxygenase 2, Heme oxygenase 2 soluble form

+ [4]

Introduction

Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron.

Drugs associated with HMOX2

Stannsoporfin

Target

HMOX1 x HMOX2

Mechanism

HMOX1 inhibitors [+1]

Active Org.-

Originator Org.

Shire Development LLC

Active Indication-

Inactive Indication

Hyperbilirubinemia [+4]

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with HMOX2

NCT02000830

/ CompletedNot Applicable

A Four-Year Blinded Outcomes Follow-up Study of Patients Who Received Stannsoporfin or Placebo in Clinical Trial 64,185-204

The objectives of this follow up study are to evaluate the long-term effects of stannsoporfin (Stanate) on the health, growth, and development of patients who received a single dose of stannsoporfin with PT used to treat hyperbilirubinemia compared with patients in the control (placebo plus PT) group in clinical trial 64,185-204.

Start Date17 Oct 2013

Sponsor / Collaborator

InfaCare Pharmaceutical Corp.

NCT01887327

/ CompletedPhase 2

A Phase 2b Multicenter, Single Dose, Randomized, Double Blind, Placebo-Controlled, Parallel-Group Study Evaluating the Safety and Efficacy of Two Doses of Stannsoporfin in Combination With Phototherapy in Neonates

It is normal for red blood cells to die, even in newborn babies. The waste from that is called bilirubin. The liver clears bilirubin out of the body.
Some babies are born with illness that makes red blood cells die too fast, so the liver is not strong enough to keep up with it.
The yellowish color in eyes or skin means there is too much bilirubin in the body. It can be dangerous if a baby's bilirubin gets too high.
Special lights are put on jaundiced babies (called phototherapy) to help the liver get rid of bilirubin.
This study tests an experimental drug to see if it can help the liver even more, by safely cutting down the amount of bilirubin the body is making in the first place.

Start Date16 Oct 2013

Sponsor / Collaborator

InfaCare Pharmaceutical Corp.

EUCTR2009-018267-27-ES

/ Not yet recruitingNot Applicable

A 5-Year, Extension, Follow-up, Blinded-Outcomes Trial of Subjects Having Received Stannsoporfin or Placebo in Clinical Trial 64,185-202Un estudio ciego de seguimiento y ampliación de 5 años de duración de pacientes que recibieron estansoporfina o placebo en el ensayo clínico 64.185-202

Start Date08 Jun 2010

Sponsor / Collaborator

InfaCare Pharmaceutical Corp.

100 Clinical Results associated with HMOX2

100 Translational Medicine associated with HMOX2

0 Patents (Medical) associated with HMOX2

1,094

Literatures (Medical) associated with HMOX2

13 Mar 2025·Journal of Medicinal Chemistry

Chemoproteomic Profiling of a Carbon-Stabilized Gold(III) Macrocycle Reveals Cellular Engagement with HMOX2

Article

Author: McCorkle, J. Robert ; Kolesar, Jill M. ; Kim, Jong H. ; Kwakye, Gunnar F. ; Parkin, Sean ; Awuah, Samuel G. ; Ratliff, Libby ; Olelewe, Chibuzor ; Gukathasan, Sailajah ; Ackerman, Alyson M.

In this work, we discovered a novel organometallic gold(III) macrocycle, Au-Mac1, that demonstrates anticancer potency in a panel of triple-negative breast cancer cells (TNBC), and based on this complex, a biotinylated-Au-Mac1 probe was designed for target identification via chemoproteomics, which uncovered the engagement of HMOX2 of the heme-energy metabolism pathway. Using orthogonal chemical biology and molecular biology approaches, including immunoblotting, flow cytometry, and cellular thermal shift assays, it was confirmed that Au-Mac1 engages HMOX2 in cells. Downstream effects of Au-Mac1 on the depletion of mitochondrial membrane proteins and bioenergetics point to the potential role of HMOX2 in cancer. Importantly, Au-Mac1 inhibits in vivo tumor growth of metastatic breast tumor-bearing mice. We believe that this approach is clinically relevant in network-oriented drug discovery. To the best of our knowledge, Au-Mac1 is the first gold complex that targets HMOX2 to elicit an anticancer effect.

01 Dec 2024·Molecular and Cellular Neuroscience

Inhibition of phosphodiesterase 10A mitigates neuronal injury by modulating apoptotic pathways in cold-induced traumatic brain injury

Article

Author: Dogan, Enes ; Kilic, Ertugrul ; Beker, Mustafa C ; Balaban, Buse ; Altintas, Mehmet O ; Beker, Mustafa C. ; Ozpinar, Aysenur ; Sengun, Nursena ; Bayraktaroglu, Cigdem ; Altunay, Serdar ; Altintas, Mehmet O.

Brain injury develops from a complex series of pathophysiological phases, resulting in acute necrotic or delayed apoptotic cell death after traumatic brain injury (TBI). Inhibition of apoptotic cell death is critical for the treatment of acute neurodegenerative disorders, such as TBI. Here, we investigated the role of phosphodiesterase 10A (PDE10A) in the development of neuronal injury, particularly in apoptotic cell death. Using the PDE10A inhibitor TAK-063, we found that PDE10A inhibition is associated with decreased brain injury, brain swelling, and blood brain barrier disruption 48 h after cold-induced TBI. Furthermore, a particularly notable result was observed with 3 mg/kg TAK-063, which reduced disseminated neuronal injury. Protein abundance analysis revealed that PDE10A inhibition activates survival kinases AKT and ERK-1/-2, which were associated with the decreased activation of MMP-9 and PTEN. Additionally, iNOS and nNOS levels significantly reduced in the TAK-063 group, playing roles in inflammation and apoptosis. A planar surface immunoassay was performed for in-depth analyses of the apoptotic signaling pathways. We observed that inhibition of PDE10A resulted in the decreased expression of TNFRSF1A, TNFRSF10B, and TNFRSF6 receptors, particularly inducing apoptotic cell death. Moreover, these findings correlated with reduced levels of pro-apoptotic proteins, including PTEN, p27, Cytochrome-c, cleaved Caspase-3, Bad, and p53. Interestingly, TAK-063 treatment reduced levels of anti-apoptotic proteins or enzymes, including XIAP, Claspin, and HIF1α, without affecting Bcl-x, MCL-1, SMAC, HO-1, HO-2, HSP27, HSP60, and HSP70. The findings suggest that PDE10A regulates cellular signaling predominantly pro-apoptotic pathways, and inhibition of this protein is a promising approach for the treatment of acute brain injury.

01 Dec 2024·Food Science & Nutrition

Protective Effects of Polysaccharides From Sargassum hemiphyllum (Turner) C. Agardh Against Alcohol‐Induced LO2 Cell Damage

Article

Author: Liu, Xiaofei ; Chen, Jianping ; Zhong, Saiyi ; Liang, Yuxuan ; Wang, Zhuo ; Li, Rui

ABSTRACTThe study aimed to explore the protective impact of polysaccharide derived from Sargassum hemiphyllum (Turner) C. Agardh (SHP) against ethanol‐induced injury in LO2 hepatocytes, along with its potential mechanism of action. A model of alcoholic injury in LO2 cells was established to assess the shielding effect of SHP against liver injury induced by alcohol. Treatment with 800 mmol/L ethanol for 6 h was selected for the construction of the hepatocyte injury model. Compared with those in the alcohol model group, the survival rate of LO2 cells in the SHP treatment group was significantly greater. When the concentration of SHP reached 60 μg/mL, the cell viability increased to 89.17% ± 3.58%. Moreover, SHP treatment significantly reduced the level of intracellular reactive oxygen species (ROS), increased the levels of intracellular glutathione (GSH), lactate dehydrogenase (LDH), and catalase (CAT), reduced the level of malondialdehyde (MDA), and prevented the leakage of intrahepatic enzymes (aspartate aminotransferase (AST) and alanine transaminase (ALT)) to protect LO2 cells from alcohol‐induced injury. Moreover, at a concentration of 60 μg/mL, SHP inhibited the ethanol‐induced reduction in the protein expressions of Nrf2, HO‐2, and GCLC, indicating its potential to modulate the antioxidant system to restore the homeostatic state, consequently shielding the liver from peroxidative damage induced by alcohol. These results propose that SHP exhibits a protective role against oxidative damage in LO2 cells and holds promise as a novel natural hepatoprotective agent for averting liver injury.

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HMOX2

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