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Molecular and Cellular Biology, November 2004, p. 9942-9947, Vol. 24, No. 22
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.22.9942-9947.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Carbonic Anhydrase III Is Not Required in the Mouse for Normal Growth, Development, and Life Span

Geumsoo Kim,¹ Tae-Hoon Lee,^2, Petra Wetzel,³ Cornelia Geers,³ Mary Ann Robinson,⁴ Timothy G. Myers,⁴ Jennie W. Owens,⁵ Nancy B. Wehr,¹ Michael W. Eckhaus,⁵ Gerolf Gros,³ Anthony Wynshaw-Boris,^6, and Rodney L. Levine^1*

Laboratories of Biochemistry,¹ Cell Signaling, National Heart, Lung, and Blood Institute,² Research Technologies Branch, National Institute of Allergy and Infectious Diseases,⁴ Division of Veterinary Resources, Office of Research Services,⁵ Laboratory of Genetic Disease Research, National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland,⁶ Zentrum Physiologie, Medizinische Hochschule Hannover, Hannover, Germany³

Received 4 June 2004/ Returned for modification 15 August 2004/ Accepted 19 August 2004

Carbonic anhydrase III is a cytosolic protein which is particularly abundant in skeletal muscle, adipocytes, and liver. The specific activity of this isozyme is quite low, suggesting that its physiological function is not that of hydrating carbon dioxide. To understand the cellular roles of carbonic anhydrase III, we inactivated the Car3 gene. Mice lacking carbonic anhydrase III were viable and fertile and had normal life spans. Carbonic anhydrase III has also been implicated in the response to oxidative stress. We found that mice lacking the protein had the same response to a hyperoxic challenge as did their wild-type siblings. No anatomic alterations were noted in the mice lacking carbonic anhydrase III. They had normal amounts and distribution of fat, despite the fact that carbonic anhydrase III constitutes about 30% of the soluble protein in adipocytes. We conclude that carbonic anhydrase III is dispensable for mice living under standard laboratory husbandry conditions.

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* Corresponding author. Mailing address: NIH, Building 50, Room 2351, Bethesda, MD 20892-0812. Phone: (301) 496-2310. Fax: (301) 496-0599. E-mail: rlevine{at}nih.gov.

Present address: Department of Oral Biochemistry, College of Dentistry, Chonnam National University, Kwangju, South Korea.

Present address: Departments of Pediatrics and Medicine, University of California, San Diego School of Medicine, La Jolla, Calif.

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Molecular and Cellular Biology, November 2004, p. 9942-9947, Vol. 24, No. 22
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.22.9942-9947.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

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