Identification and characterisation of a sequence related to human sorbitol dehydrogenase.

The polyol pathway comprises the enzymes aldose reductase and sorbitol dehydrogenase which convert glucose to fructose via sorbitol. Accumulation of sorbitol within the cell has been suggested to contribute to the progression of secondary complications of diabetes. High levels of sorbitol accumulate within the cell due to inadequate regulation of blood glucose levels. It has also been suggested that polymorphism in either the aldose reductase or sorbitol dehydrogenase genes might contribute to sorbitol accumulation. The human sorbitol dehydrogenase gene (SORD) has been described previously and a range of putative polymorphic variants were identified. Further analysis of human SORD yeast artificial chromosome clones has now shown that there is a second SORD-like sequence in man, which is extremely similar in sequence to SORD itself and which also maps to chromosome 15. Detailed sequence analysis suggests that this SORD-related gene cannot be expressed as a full-length sorbitol dehydrogenase isoenzyme. However, knowledge of the presence of this highly similar sequence in the human genome is essential to ensure that sequence variations identified during genetic analysis of SORD are not attributed to polymorphisms within that gene itself.

[1]  J. McKinley-McKee,et al.  Effect of pH on sheep liver sorbitol dehydrogenase steady-state kinetics. , 1995, European journal of biochemistry.

[2]  I. Rodriguez,et al.  Structural organization of the human sorbitol dehydrogenase gene (SORD). , 1995, Genomics.

[3]  L. Diemel,et al.  Aldose reductase inhibitors and their potential for the treatment of diabetic complications. , 1994, Trends in pharmacological sciences.

[4]  S. Chung,et al.  The human sorbitol dehydrogenase gene: cDNA cloning, sequence determination, and mapping by fluorescence in situ hybridization. , 1994, Genomics.

[5]  J. Jurka,et al.  A young Alu subfamily amplified independently in human and African great apes lineages. , 1994, Nucleic acids research.

[6]  A. Sarthy,et al.  Cloning and sequence determination of the gene encoding sorbitol dehydrogenase from Saccharomyces cerevisiae. , 1994, Gene.

[7]  J. Nyengaard,et al.  Hyperglycemic Pseudohypoxia and Diabetic Complications , 1993, Diabetes.

[8]  O. Yamashita,et al.  A cold-inducible Bombyx gene encoding a protein similar to mammalian sorbitol dehydrogenase. Yolk nuclei-dependent gene expression in diapause eggs. , 1993, European journal of biochemistry.

[9]  D. V. Vander Jagt,et al.  Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications. , 1992, The Journal of biological chemistry.

[10]  H. Jörnvall,et al.  Sorbitol dehydrogenase: cDNA coding for the rat enzyme. Variations within the alcohol dehydrogenase family independent of quaternary structure and metal content. , 1991, European journal of biochemistry.

[11]  A. Markham,et al.  Structure of the human aldose reductase gene. , 1991, The Journal of biological chemistry.

[12]  J. Riley,et al.  A 3.5 genome equivalent multi access YAC library: construction, characterisation, screening and storage. , 1990, Nucleic acids research.

[13]  H. Jörnvall,et al.  Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme. , 1989, European journal of biochemistry.

[14]  B. Aronson,et al.  The primary structure of Escherichia coli L-threonine dehydrogenase. , 1989, The Journal of biological chemistry.

[15]  W. Maret,et al.  Purification and characterization of human liver sorbitol dehydrogenase. , 1988, Biochemistry.

[16]  M. Burg.  Role of aldose reductase and sorbitol in maintaining the medullary intracellular milieu. , 1988, Kidney international.

[17]  J L Sussman,et al.  Refined crystal structure of dogfish M4 apo-lactate dehydrogenase. , 1989, Journal of molecular biology.

[18]  D. Greene,et al.  Sorbitol, phosphoinositides, and sodium-potassium-ATPase in the pathogenesis of diabetic complications. , 1987, The New England journal of medicine.

[19]  H. Eklund,et al.  Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases. , 1985, Biochemistry.

[20]  H. Jörnvall,et al.  Sorbitol dehydrogenase. The primary structure of the sheep-liver enzyme. , 1984, European journal of biochemistry.

[21]  A. Cerami,et al.  The biochemistry of the complications of diabetes mellitus. , 1981, Annual review of biochemistry.

[22]  G. Pettersson,et al.  Kinetic transients in the reduction of aldehydes catalysed by liver alcohol dehydrogenase. , 1976, European journal of biochemistry.