Further Characterization of a Rat Hepatoma‐Derived Aldose‐Reductase‐Like Protein

Zeindl‐Eberhart, Evelyn; Jungblut, Peter R.; Otto, Albrecht; Kerler, R.; Rabes, Hartmut M.

doi:10.1111/j.1432-1033.1997.t01-1-00792.x

Cited by 28 publications

(39 citation statements)

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“…Human ARLP expression was shown on serial 4 m sections using the polyclonal antibody described above and the Vectastain -ABC Kit (rabbit immunoglobulin G; Vector Laboratories, Burlingame, CA) and diaminobenzidine (Sigma) as described. 8 After unmasking in diluted Target Retrieval Solution (Dako Diagnostica, Hamburg, Germany) for 30 minutes in an autoclave at 1 atm, endogenous peroxidase of the sections was inhibited by 3% H 2 O 2 . Human ARLP antibody was used in a dilution of 1:80 in antibody diluent (Dako).…”

Section: Methodsmentioning

confidence: 99%

“…These protein alterations might represent tumor markers that are useful in the diagnosis of human tumors and may also help the understanding of mechanisms of tumor induction and development. Proteome analysis of liver proteins and HCC were predominantly performed using either chemically induced hepatomas in animals (predominantly the rat [5][6][7][8][9][10] ) or human HCC cell lines, such as HepG2 and Huh7 cells, 11 BEL-7404 cells, 12 or HCC-M cells. 2,13,14 Numerous so-called tumor-associated or cancer-related proteins were identified; these provide valuable information for the establishment of HCC protein databases.…”

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confidence: 99%

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Detection and identification of tumor-associated protein variants in human hepatocellular carcinomas

et al. 2004

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The proteomic approach is a valuable tool to detect and identify proteins that are associated with cancer. In previous investigations on experimentally induced rat hepatomas, we detected aldose reductase-like protein (ARLP) as a highly significant marker protein. Our present study was intended to look for the presence of similar tumor-associated marker proteins on human hepatocellular carcinomas (HCC). We found several novel tumorassociated protein variants that represent members of the aldo-keto reductase (AKR) superfamily. Human aldose reductase-like protein-1 (hARLP-1) was the most prominent tumorassociated AKR member detected in HCC by 2-dimensional electrophoresis (2-DE) and identified by mass spectrometric fingerprinting. The enzyme was found in 4 distinct forms H uman hepatocellular carcinoma (HCC) ranks fifth in worldwide cancer incidence and is an important component of public health. Many HCC risk factors are known, including hepatitis B or C (HBV or HCV) infection, ingestion of aflatoxin-contaminated food, and alcohol. 1,2 The development of HCC is associated with multiple changes at the messenger RNA (mRNA) and/or protein level, some of them serving as tumor markers, e.g., ␣-fetoprotein, 3 or, less specifically, cyclin D1 or the proliferating cell nuclear antigen. 4 Misprogramming of genetic information in cancer is reflected by quantitative and/or qualitative protein alterations. These protein alterations might represent tumor markers that are useful in the diagnosis of human tumors and may also help the understanding of mechanisms of tumor induction and development. Proteome analysis of liver proteins and HCC were predominantly performed using either chemically induced hepatomas in animals (predominantly the rat 5-10 ) or human HCC cell lines, such as HepG2 and Huh7 cells, 11 BEL-7404 cells, 12 or HCC-M cells. 2,13,14 Numerous so-called tumor-associated or cancer-related proteins were identified; these provide valuable information for the establishment of HCC protein databases. 2,[11][12][13][14] Comparative analysis of liver tissue and hepatocellular carcinomas might give additional insights into the induction or repression of tumor-associ-

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Detection and identification of tumor-associated protein variants in human hepatocellular carcinomas

et al. 2004

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“…Early proteomics studies identified tumor-associated protein variants during hepatocarcinogenesis in the rat [90]. Other cancer tissues were analyzed using proteome methods, such as of lung [91,92], liver [93], colon [77,94], bladder [95][96][97][98], heart [99] or prostate [100].…”

Section: Examples Of Successful Application Of Proteomicsmentioning

confidence: 99%

Two‐dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry

2006

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The proteome analysis by 2-DE is one of the most potent methods of analyzing the complete proteome of cells, cell lines, organs and tissues in proteomics studies. It allows a fast overview of changes in cell processes by analysis of the entire protein extracts in any biological and medical research projects. New instrumentation and advanced technologies provide proteomics studies in a wide variety of biological and biomedical questions. Proteomics work is being applied to study antibiotics-resistant strains and human tissues of various brain, lung, and heart diseases. It cumulated in the identification of antigens for the design of new vaccines. These advances in proteomics have been possible through the development of advanced high-resolution 2-DE systems allowing resolution of up to 10 000 protein spots of entire cell lysates in combination with protein identification by new highly sensitive mass spectrometric techniques. The present technological achievements are suited for a high throughput screening of different cell situations. Proteomics may be used to investigate the health effects of radiation and electromagnetic field to clarify possible dangerous alterations in human beings.

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“…AKR inducing agents have included ethacrynic acid (9), ethoxyquin (19), 3Ј-methyl-4-dimethyl-aminoazobenzene (20), and N-methyl-N-nitrosourea (21), while spontaneous induction has been observed during the development of hereditary hepatitis leading to hepatocarcinogenesis (6). Hormonal regulation of AKR members has been observed during the estrous cycle (7), in the cell cycle of Leishmania major (22) and due to the effects of basic fibroblast growth factor on astrocytes (8).…”

Section: Resultsmentioning

confidence: 99%

Cloning, Sequencing, and Enzymatic Activity of an Inducible Aldo-Keto Reductase from Chinese Hamster Ovary Cells

Hyndman¹,

Takenoshita²,

Vera³

et al. 1997

Journal of Biological Chemistry

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Treatment of Chinese hamster ovary (CHO) cells by the aldehyde containing calpain inhibitor I resulted in the induction of a 35-kDa protein that was partially sequenced and shown to be a member of the aldo-keto reductase superfamily (Inoue, S., Sharma, R. C., Schimke, R. T., and Simoni, R. D. (1993) J. Biol. Chem. 268, 5894 -5898). Using rapid amplification of cDNA ends polymerase chain reaction, we have sequenced the cDNA for this protein (CHO reductase). This enzyme is a new member of the aldo-keto reductase superfamily and shows greatest amino acid sequence identity to mouse fibroblast growth factor-regulated protein and mouse vas deferens protein (92 and 80% sequence identity, respectively). The enzyme exhibits about 70% sequence identity with the aldose reductases (ALR2; EC 1.1.1.21) and about 47% with the aldehyde reductases (ALR1; EC 1.1.1.2). Northern analysis showed that it is induced in preference to either ALR1 or ALR2 and RNase protection assays showed gene expression in bladder, testis, jejunum, and ovary in descending order of expression. The cDNA for this inducible reductase was cloned into the pET16b vector and expressed in BL21(DE3) cells. Expressed CHO reductase showed kinetic properties distinct from either ALR1 or ALR2 including the ability to metabolize ketones. This protein joins a growing number of inducible aldo-keto reductases that may play a role in cellular regulation and protection.To characterize the calpain inhibitor I-sensitive protease(s) involved in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, Simoni's group (1) attempted to isolate Chinese hamster ovary (CHO) 1 cells resistant to this peptide aldehyde (N-acetyl-leucyl-leucyl-norleucinal (ALLN)). Instead of inducing a protease, a 35-kDa protein was overexpressed which gave tryptic peptide fragments with a high degree of sequence identity to members of the aldo-keto reductase superfamily. 2 This superfamily is a rapidly growing group of monomeric oxidoreductases containing at least 40 members at present (2). This group includes the aldehyde and aldose reductases, a number of hydroxysteroid dehydrogenases, Shaker channels, and plant chalcone reductases. They are characterized by a TIM-barrel structure (3) and the preferential use of NADPH over NADH. Substrates include aliphatic and aromatic aldehydes, monosaccharides, steroids, prostaglandins, polycyclic aromatic hydrocarbons, and isoflavinoid phytoalexins.Several members of this family have been shown to be induced in response to hormonal or chemical factors. These include fibroblast growth factor-regulated protein (FR-1) (4), mouse vas deferens protein (MVDP) (5), aldose reductase (ALR2) (6 -8), and dihydrodiol dehydrogenase (9). To determine the relationship of this new reductase to the other members of the family we have used RACE PCR to isolate and sequence its mRNA from CHO cells. It shows highest sequence identity to FR-1 and MVDP at 92 and 80%, respectively. FR-1 and MVDP have not been extensively characterized kinetically but CHO reductase showed a greater ...

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Further Characterization of a Rat Hepatoma‐Derived Aldose‐Reductase‐Like Protein

Cited by 28 publications

References 61 publications

Detection and identification of tumor-associated protein variants in human hepatocellular carcinomas

Detection and identification of tumor-associated protein variants in human hepatocellular carcinomas

Two‐dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry

Cloning, Sequencing, and Enzymatic Activity of an Inducible Aldo-Keto Reductase from Chinese Hamster Ovary Cells

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