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Biomed Rep. 2017 Oct;7(4):301-305. doi: 10.3892/br.2017.973. Epub 2017 Aug 25.

Molecular cloning of the myo-inositol oxygenase gene from the kidney of baboons.

Author information

1
Facultad de Medicina, Universidad Autónoma de Guadalajara, Zapopan, Jalisco 45129, Mexico.
2
Servicio de Oncología, Universidad Autónoma de Nuevo León, Centro Universitario Contra el Cáncer, Hospital Universitario 'Dr José Eleuterio González', Monterrey, Nuevo León 64460, Mexico.
3
Departamento de Bioquímica y Medicina Molecular, Facultad de Medicina, Universidad Autónoma de Nuevo León, Monterrey, Nuevo León 64460, Mexico.
4
Centro Mesoamericano de Estudios en Salud Pública y Desastres (CEMESAD, Nodo Tapachula), Universidad Autónoma de Chiapas, Tuxtla Gutiérrez, Chiapas 29076, Mexico.
5
Facultad de Medicina, Universidad de Colima, Colima 28040, Mexico.
6
Instituto Nacional de Medicina Genómica (INMEGEN), Laboratorio Nutrigenética y Nutrigenómica, Tlalpan, Arenal Tepepan 14610, Mexico.
7
Departamento de Genética y Defectos Congénitos, Universidad Autónoma de Nuevo León, Centro Universitario Contra el Cáncer, Hospital Universitario 'Dr José Eleuterio González', Monterrey, Nuevo León 64460, Mexico.
8
Servicio de Anatomía Patológica y Citopatología, Universidad Autónoma de Nuevo León, Hospital Universitario 'Dr José Eleuterio González', Monterrey, Nuevo León 64460, Mexico.
9
Departamento de Ecología, Universidad Autónoma de Nuevo León, Facultad de Ciencias Biológicas, San Nicolás de los Garza, Nuevo León 66425, Mexico.
10
Centro de Biotecnología-FEMSA, Tecnológico de Monterrey Campus Monterrey, Monterrey, Nuevo León 64849, Mexico.

Abstract

The enzyme myo-Inositol oxygenase (MIOX) is also termed ALDRL6. It is a kidney-specific member of the aldo-keto reductase family. MIOX catalyzes the first reaction involved in the myo-inositol metabolism signaling pathway and is fully expressed in mammalian tissues. MIOX catalyzes the oxidative cleavage of myo-Inositol and its epimer, D-chiro-Inositol to D-glucuronate. The dioxygen-dependent cleavage of the C6 and C1 bond in myo-Inositol is achieved by utilizing the Fe2+/Fe3+ binuclear iron center of MIOX. This enzyme has also been implicated in the complications of diabetes, including diabetic nephropathy. The MIOX gene was amplified with reverse transcription-polymerase chain reaction from baboon tissue samples, and the product was cloned and sequenced. MIOX expression in the baboon kidney is described in the present study. The percentages of nucleotide and amino acid similarities between baboons and humans were 95 and 96%, respectively. The MIOX protein of the baboon may be structurally identical to that of humans. Furthermore, the evolutionary changes, which have affected these sequences, have resulted from purifying forces.

KEYWORDS:

Old World monkey; animal models; gene expression; kidney; myo-inositol oxygenase

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