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1. Sequence and structure of the human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2)

Author

Díaz-Guillén Ma, Santiago Rodríguez de Córdoba, Alex J. Lange, and Damian Heine-Suñer

Subjects
Gene isoform, Phosphofructokinase-2, Molecular Sequence Data, Restriction Mapping, Fructose 1,6-bisphosphatase, Biochemistry, Gene Expression Regulation, Enzymologic, Exon, Multienzyme Complexes, Transcription (biology), Complementary DNA, Humans, Phosphofructokinase 2, Amino Acid Sequence, Cloning, Molecular, Binding site, Gene, Conserved Sequence, Binding Sites, Base Sequence, Sequence Homology, Amino Acid, biology, Myocardium, Phosphotransferases, Exons, Sequence Analysis, DNA, Introns, Phosphoric Monoester Hydrolases, biology.protein, Sequence Alignment
Abstract

6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2) is a bifunctional enzyme that catalyzes the synthesis and degradation of Fru-2,6-P2, a key regulator of glycolysis. In mammals, several genes have been found to code for different PFK-2/FBPase-2 isoforms that differ in tissue distribution and enzymatic activities. In the present study, we report the characterization of the PFK-2/FBPase-2 heart isoform gene in humans (PFKFB2), including a full analysis of repetitive sequences and potential transcription binding sites. The genomic sequence of the PFKFB2 gene spans 22 485 bp and contains 15 exons. Heart cDNA analysis shows that PFKFB2 codes for a protein of 505 amino acids with a deduced molecular mass of 58 849 Da. Comparison of the human PFKFB2 gene to the homologous genes in rat and ox outlines a significant conservation of the intron-exon structure, sequence of 5 ′ and 3′ flanking regions, and simple sequence repetitive element positions. Most important, the human heart PFK-2/ FBPase-2 protein was found to retain all the important regulatory sites, as well as the catalytic and substrate binding sites identified in the rat and bovine heart isoforms, suggesting that the human enzyme is regulated in a manner similar to that observed in these organisms.

Published
1998
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2. Sequence and structure of the human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2).

Author

Heine-Suñer D, Díaz-Guillén MA, Lange AJ, and Rodríguez de Córdoba S

Subjects
Amino Acid Sequence, Base Sequence, Binding Sites physiology, Cloning, Molecular, Conserved Sequence genetics, Exons genetics, Gene Expression Regulation, Enzymologic genetics, Humans, Introns genetics, Molecular Sequence Data, Phosphofructokinase-2, Restriction Mapping, Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Multienzyme Complexes chemistry, Myocardium enzymology, Phosphoric Monoester Hydrolases chemistry, Phosphotransferases chemistry
Abstract

6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2) is a bifunctional enzyme that catalyzes the synthesis and degradation of Fru-2,6-P2, a key regulator of glycolysis. In mammals, several genes have been found to code for different PFK-2/FBPase-2 isoforms that differ in tissue distribution and enzymatic activities. In the present study, we report the characterization of the PFK-2/FBPase-2 heart isoform gene in humans (PFKFB2), including a full analysis of repetitive sequences and potential transcription binding sites. The genomic sequence of the PFKFB2 gene spans 22,485 bp and contains 15 exons. Heart cDNA analysis shows that PFKFB2 codes for a protein of 505 amino acids with a deduced molecular mass of 58,849 Da. Comparison of the human PFKFB2 gene to the homologous genes in rat and ox outlines a significant conservation of the intron-exon structure, sequence of 5' and 3' flanking regions, and simple sequence repetitive element positions. Most important, the human heart PFK-2/ FBPase-2 protein was found to retain all the important regulatory sites, as well as the catalytic and substrate binding sites identified in the rat and bovine heart isoforms, suggesting that the human enzyme is regulated in a manner similar to that observed in these organisms.

Published
1998
Full Text
View/download PDF

3. A region of allelic imbalance in 1q31-32 in primary breast cancer coincides with a recombination hot spot.

Author

Benítez J, Osorio A, Barroso A, Arranz E, Díaz-Guillén MA, Robledo M, Rodríguez de Córdoba S, and Heine-Suñer D

Subjects
Breast Neoplasms pathology, Carcinoma, Ductal, Breast genetics, Disease Progression, Female, Genes, Tumor Suppressor, Genetic Markers, Humans, Loss of Heterozygosity, Male, Microsatellite Repeats, Sex Characteristics, Alleles, Breast Neoplasms genetics, Chromosomes, Human, Pair 1 genetics, Recombination, Genetic
Abstract

Previous studies have shown that the 1q31-32 region frequently presents allelic imbalance (AI) in various neoplastic diseases, such as breast cancer, medulloblastoma, male germ cell tumors, and renal collecting duct carcinoma, suggesting the presence of a tumor suppressor gene in this location. We used 19 informative microsatellite markers to analyze 33 primary breast tumors for AI in the 1q31-32 region. Our results demonstrate a 10-cM critical region of AI that is present in more than 60% of the tumors. This region is located proximal to the REN locus and is flanked by the CACNL1A3 and D1S2655 markers. Most important, the critical region of AI coincides with a female hot spot of recombination, suggesting a possible correlation between the two regions.

Published
1997

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