A cluster of eight hydroxysteroid dehydrogenase genes belonging to the aldo-keto reductase supergene family on mouse chromosome 13

Vergnes, Laurent; Phan, Jack; Stolz, Andrew; Reue, Karen

doi:10.1194/jlr.m200399-jlr200

Cited by 52 publications

(62 citation statements)

References 45 publications

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“…However, antibodies raised against recombinant protein failed to detect a product in native human tissue (Azuma et al, 2004). Thus, it appears that due to a mutation altering the exon-intron junction during the evolution, the human protein acquired 19 additional amino acids which diminished its catalytic activity, and other changes occurred making expression specific to testis [AKR1E1 is ubiquitously expressed in mouse tissues (Vergnes et al, 2003)]. It has been speculated that human AKR1E regulates spermatogenesis, as it is expressed in germ cells (Azuma et al, 2004).…”

Section: B) Homology Between Human and Rodent Akr Genesmentioning

confidence: 99%

“…In mice, a cluster of 8 Akr1c genes and Akr1e1 gene is located on chromosome 13A1 (Vergnes et al, 2003). AKR1C proteins all consist of 323 amino acids (same as human) and share more than 75% similarity in their amino acid sequence, making it difficult to assign specific parallels between them and human HSDs.…”

Section: B) Homology Between Human and Rodent Akr Genesmentioning

confidence: 99%

“…Only the mouse protein and gene have been characterized, while the rat sequence has only been identified through large-scale genome sequencing (NM_001008342 on chromosome 17q12.3). Both murine and rat Akr1es cluster with Akr1c family on chromosomes 13 and 17, respectively, however they possess 10 rather than 9 exons and encode for 301 amino acid proteins (AKRs 1Cs consist of 323 amino acids) (Vergnes et al, 2003). AKR1E1 displays distinct catalytic properties , which places it in a separate subfamily altogether.…”

Section: B) Homology Between Human and Rodent Akr Genesmentioning

confidence: 99%

“…AKR1C1 (20α-HSD) catalyzes the reduction of progesterone to inactive metabolite 20α-hydroxyprogesterone (in ovaries and uterus) (Fig. 11) (Vergnes et al, 2003). Ensuing reduction in the progesterone level initiates parturition and termination of pregnancy.…”

Section: D) Steroidsmentioning

confidence: 99%

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The Aldo-Keto Reductase Superfamily and its Role in Drug Metabolism and Detoxification

Barski

Tipparaju

Bhatnagar

2008

Drug Metabolism Reviews

442

340

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The Aldo-Keto Reductase (AKR) superfamily comprises of several enzymes that catalyze redox transformations involved in biosynthesis, intermediary metabolism and detoxification. Substrates of the family include glucose, steroids, glycosylation end products, lipid peroxidation products, and environmental pollutants. These proteins adopt a (β/α) 8 barrel structural motif interrupted by a number of extraneous loops and helixes that vary between proteins and bring structural identity to individual families. The human AKR family differs from the rodent families. Due to their broad substrate specificity, AKRs play an important role in the Phase II detoxification of a large number of pharmaceuticals, drugs, and xenobiotics.

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Section: B) Homology Between Human and Rodent Akr Genesmentioning

confidence: 99%

Section: B) Homology Between Human and Rodent Akr Genesmentioning

confidence: 99%

Section: B) Homology Between Human and Rodent Akr Genesmentioning

confidence: 99%

Section: D) Steroidsmentioning

confidence: 99%

See 2 more Smart Citations

The Aldo-Keto Reductase Superfamily and its Role in Drug Metabolism and Detoxification

Barski

Tipparaju

Bhatnagar

2008

Drug Metabolism Reviews

442

340

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“…cDNA was prepared and analyzed as described (29). Primers were as follows: Lmnb1-3Ј forward, TCAGGGAGAGGAGGTTGCTC-3Ј; Lmnb1-3Ј reverse, TCT-GCACTGTATACAGGACTC-3Ј; Lmnb1-5Ј forward, 5Ј-GGGCGTCAGATTGAGTATGAG-3Ј; Lmnb1-5Ј reverse, 5Ј-TTAGAGAGCTGTGAGGAGAGG-3Ј; Lmna forward, 5Ј-GACTTGGTGTGGAAGGCGCAGA-3Ј; Lmna reverse, 5Ј-GCTTCGAGTGACTGTGACACTGGA-3Ј; Lmnc forward, same as Lmna forward; Lmnc reverse, 5Ј-GCAGGGCTAC-CCTTGTGGGCT-3Ј; Hprt forward, CACAGCACTAGAA-CACCTGC-3Ј; and Hprt reverse, 5Ј-GCTGGTGAAAAGGAC-CTCT-3Ј.…”

Section: Rt-pcrmentioning

confidence: 99%

Lamin B1 is required for mouse development and nuclear integrity

Vergnes

Péterfy

Bergö

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

354

355

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Lamins are key structural components of the nuclear lamina, an intermediate filament meshwork that lies beneath the inner nuclear membrane. Lamins play a role in nuclear architecture, DNA replication, and gene expression. Mutations affecting A-type lamins have been associated with a variety of human diseases, including muscular dystrophy, cardiomyopathy, lipodystrophy, and progeria, but mutations in B-type lamins have never been identified in humans or in experimental animals. To investigate the in vivo function of lamin B1, the major B-type lamin, we generated mice with an insertional mutation in Lmnb1. The mutation resulted in the synthesis of a mutant lamin B1 protein lacking several key functional domains, including a portion of the rod domain, the nuclear localization signal, and the CAAX motif (the carboxylterminal signal for farnesylation). Homozygous Lmnb1 mutant mice survived embryonic development but died at birth with defects in lung and bone. Fibroblasts from mutant embryos grew under standard cell-culture conditions but displayed grossly misshapen nuclei, impaired differentiation, increased polyploidy, and premature senescence. Thus, the lamin B1 mutant mice provide evidence for a broad and nonredundant function of lamin B1 in mammalian development. These mutant mice and cell lines derived from them will be useful models for studying the role of the nuclear lamina in various cellular processes.nuclear envelope ͉ lamins ͉ knockout mice ͉ gene trapping T he nuclear lamina, a protein meshwork that lines the inner nuclear membrane, is critical in fundamental cellular processes, including nuclear organization, chromatin segregation, DNA replication, and gene transcription (1-5). The principal protein components of the lamina are lamins, which are members of the intermediate filament protein family. Like other intermediate filament proteins, lamins possess an aminoterminal head domain and a highly conserved central ␣-rod domain for polymerization and oligomerization (6). Lamins are, however, distinguished from other intermediate filament proteins by a nuclear localization motif. In addition, prelamin A and lamins B1 and B2 contain a carboxyl-terminal CAAX motif that triggers a series of posttranslational modifications (farnesylation, endoproteolytic trimming of the last three amino acid residues, and methylation of the newly exposed farnesylcysteine) (6). Aside from their structural role in the formation of the nuclear lamina, lamins A and C are found in the nucleoplasm adjacent to sites of DNA synthesis and RNA processing, suggesting that these proteins could influence both DNA replication and gene expression (2,7,8).In vertebrates, lamins are classified as A or B type, based on sequence homology, expression pattern, biochemical properties, and localization during mitosis. The A-type lamins, lamins A and C, are synthesized from alternatively spliced transcripts of LMNA and are expressed in most differentiated cells (9). Somatic cells also express two B-type lamins, lamin B1 and lamin B2, which are encode...

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Sn_20.5□_3.5As₂₂I₈: A Largely Disordered Cationic Clathrate with a New Type of Superstructure and Abnormally Low Thermal Conductivity

Zaikina

Kovnir²,

Sobolev

et al. 2007

Chemistry A European J

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Sn(20.5)As(22)I(8), a new cationic clathrate, has been prepared by using an ampoule technique. According to the X-ray powder diffraction data, it crystallizes in the face-centered cubic space group F23 or Fm(-)3 with a unit-cell parameter of a=22.1837(4) A. Single-crystal X-ray data allowed solution of the crystal structure in the subcell with a unit-cell parameter of a(0)=11.092(1) A and the space group Pm(-)3n (R=5.7 %). Sn(20.5)As(22)I(8) (or Sn(20.5) square(3.5)As(22)I(8), accounting for the vacancies in the framework) possesses the clathrate-I type crystal structure, with iodine atoms occupying the cages of the cationic framework composed of tin and arsenic atoms. The crystal structure is strongly disordered. The main features are a random distribution of vacancies, and shifts of the tin and arsenic atoms away from their ideal positions. The coordination of the tin atoms has been confirmed by using (119)Sn Mössbauer spectroscopy. Electron diffraction and high-resolution electron microscopy (HREM) analyses have confirmed the presence of the superstructure ordering, which results in a doubling of the unit-cell parameter and a change of the space group from Pm(-)3n to either F23 or Fm(-)3. Analysis of the crystal structure has led to the construction of four ordering models for the superstructure, which have been corroborated by HREM, and has also led to the identification of disordered regions originating from overlap of the different types of ordered domains. Sn(20.5)As(22)I(8) is a diamagnetic semiconductor with an estimated band gap of 0.45 eV; it displays abnormally low thermal conductivity, with the room temperature value being just 0.5 W m(-1) K(-1).

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A cluster of eight hydroxysteroid dehydrogenase genes belonging to the aldo-keto reductase supergene family on mouse chromosome 13

Cited by 52 publications

References 45 publications

The Aldo-Keto Reductase Superfamily and its Role in Drug Metabolism and Detoxification

The Aldo-Keto Reductase Superfamily and its Role in Drug Metabolism and Detoxification

Lamin B1 is required for mouse development and nuclear integrity

Sn_20.5□_3.5As₂₂I₈: A Largely Disordered Cationic Clathrate with a New Type of Superstructure and Abnormally Low Thermal Conductivity

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A cluster of eight hydroxysteroid dehydrogenase genes belonging to the aldo-keto reductase supergene family on mouse chromosome 13

Cited by 52 publications

References 45 publications

The Aldo-Keto Reductase Superfamily and its Role in Drug Metabolism and Detoxification

The Aldo-Keto Reductase Superfamily and its Role in Drug Metabolism and Detoxification

Lamin B1 is required for mouse development and nuclear integrity

Sn20.5□3.5As22I8: A Largely Disordered Cationic Clathrate with a New Type of Superstructure and Abnormally Low Thermal Conductivity

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Sn_20.5□_3.5As₂₂I₈: A Largely Disordered Cationic Clathrate with a New Type of Superstructure and Abnormally Low Thermal Conductivity