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Gene Review:

Hmox3 - heme oxygenase (decycling) 3

Rattus norvegicus

This record was replaced with 100359946.

Hayashi, S. et al., Scapagnini, G. et al., McCoubrey, W.K. et al., Fu, W.J. et al., Wilcox, R.A. et al.

Scapagnini, D'Agata, Calabrese, Pascale, Colombrita, Alkon, Cavallaro,

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Disease relevance of LOC365909

Escherichia coli expressed and purified HO-3 protein does not cross react with polyclonal antibodies to either rat HO-1 or HO-2, is a poor heme catalyst, and displays hemoprotein spectral characteristics [1].

High impact information on LOC365909

Results of the microarray analysis indicated that arginine supplementation increased adipose tissue expression of key genes responsible for fatty acid and glucose oxidation: NO synthase-1 (145%), heme oxygenase-3 (789%), AMP-activated protein kinase (123%), and peroxisome proliferator-activated receptor gamma coactivator-1alpha (500%) [2].
Characterization of rat heme oxygenase-3 gene. Implication of processed pseudogenes derived from heme oxygenase-2 gene [3].
Our results suggested that there are no functional HO-3 genes in rat and that the HO-3a and HO-3b genes are processed pseudogenes derived from HO-2 transcripts [3].
HO-3 mRNA was expressed mainly in hippocampus, cerebellum and cortex [4].
While HO-1 and HO-2 were detected in both cellular types, HO-3 transcript was uniquely found in astrocytes [4].

Anatomical context of LOC365909

The HO-3 transcript is found in the spleen, liver, thymus, prostate, heart, kidney, brain and testis and is the product of a single-copy gene [1].

Associations of LOC365909 with chemical compounds

The results show that HO-2 and HO-3 of Ins(1,4,5)P3 have a relatively insignificant role in receptor binding and calcium release [5].

Analytical, diagnostic and therapeutic context of LOC365909

In this study, we examined the structure of the rat HO-3 gene with genomic PCR [3].
No HO-3-related mRNAs were amplified by RT-PCR, and no HO-3-related proteins were detected in tissues by Western blot analysis [3].
To further investigate the regional brain expression of this elusive and poorly studied isoform, we have performed in situ hybridization using an HO-3 specific riboprobe [4].

References

Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3. McCoubrey, W.K., Huang, T.J., Maines, M.D. Eur. J. Biochem. (1997) [Pubmed]
Dietary L-arginine supplementation reduces fat mass in Zucker diabetic fatty rats. Fu, W.J., Haynes, T.E., Kohli, R., Hu, J., Shi, W., Spencer, T.E., Carroll, R.J., Meininger, C.J., Wu, G. J. Nutr. (2005) [Pubmed]
Characterization of rat heme oxygenase-3 gene. Implication of processed pseudogenes derived from heme oxygenase-2 gene. Hayashi, S., Omata, Y., Sakamoto, H., Higashimoto, Y., Hara, T., Sagara, Y., Noguchi, M. Gene (2004) [Pubmed]
Gene expression profiles of heme oxygenase isoforms in the rat brain. Scapagnini, G., D'Agata, V., Calabrese, V., Pascale, A., Colombrita, C., Alkon, D., Cavallaro, S. Brain Res. (2002) [Pubmed]
The role of the 2- and 3-hydroxyl groups of 1D-myo-inositol 1,4,5-trisphosphate in the mobilisation of calcium from permeabilised human 1321N1 astrocytoma cells. Wilcox, R.A., Nahorski, S.R., Sawyer, D.A., Liu, C., Potter, B.V. Carbohydr. Res. (1992) [Pubmed]

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