| Literature DB >> 29085625 |
Rafael González-Álvarez1, Diana Cristina Pérez-Ibave2, María Lourdes Garza-Rodríguez3, Ángel Lugo-Trampe4, Iván Delgado-Enciso5, María Elizabeth Tejero-Barrera6, Laura Elia Martínez-De-Villarreal7, Raquel Garza-Guajardo8, María Marisela Sánchez-Chaparro7, Gabriel Ruiz-Ayma9, Oralia Barboza-Quintana8, Hugo Alberto Barrera-Saldaña3, María Del Refugio Rocha-Pizaña10, Irám Pablo Rodríguez-Sánchez7.
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.Entities:
Keywords: Old World monkey; animal models; gene expression; kidney; myo-inositol oxygenase
Year: 2017 PMID: 29085625 PMCID: PMC5649556 DOI: 10.3892/br.2017.973
Source DB: PubMed Journal: Biomed Rep ISSN: 2049-9434