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Instituto Nacional de Neurología y Neurocirugía

2010, Number 1

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Arch Neurocien 2010; 15 (1)

Heme oxygenase: general aspects and importance in the central nervous system

Orozco-Ibarra M, Pedraza-Chaverrí J

Language: Spanish
References: 90
Page: 47-55
PDF size: 195.40 Kb.


ABSTRACT

Heme oxygenase (HO) is the rate-limiting enzyme that degrades heme and produces ferrous iron, carbon monoxide and biliverdin, the latter being converted to bilirubin through biliverdin reductase. In mammals, there are at least two functionally active HO isozymes, HO-1 is a 32-kDa protein that is inducible by numerous noxious stimuli and HO-2 is a constitutively synthesized 36-kDa protein that is abundant in brain and testis. In spite of both isozymes catalyze heme degradation by a similar mechanism, they exhibit significant differences in their molecular structure, biochemical characteristics, tissue distribution and gene regulation, which suggests that HO isoforms may have distinct cellular functions. Pos mortem studies on human brains have shown that HO-1 expression is involved with the pathology of neurodegenerative diseases such as Alzheimer, Parkinson and Huntington. On the other hand, HO-2 is the predominant isozyme of the nervous tissue and cerebral vessels and is evidence about its role in cell signaling, as intracellular sensor of oxygen, nitric oxide and carbon monoxide is increasing. Also, it has been found that HO 2 confers neuroprotection against cerebral ischemia. In addition, it is now known that the products of HO reaction have an important role in the cell. For example, bilirubin and biliverdin exhibit antioxidant activity, carbon monoxide is a signaling molecule and a vasodilator and Fe2+ induces ferritin expression. Therefore, additional studies about the HO function in the nervous system are needed.


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