Proteomic analysis and molecular characterization of tissue ferritin light chain in hepatocellular carcinoma

Park, Kang Sik; Kim, Hoguen; Kim, Nam Gyun; Cho, Sang Yun; Choi, Kun Ho; Seong, Je Kyung; Paik, Young Ki

doi:10.1053/jhep.2002.33204

Cited by 108 publications

(63 citation statements)

References 35 publications

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“…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-ated protein variants within an intact organism. Clinical material was used for proteome analysis comparing normal liver tissue and HCC, [15][16][17] or normal liver, cirrhotic liver, and HCC 18 or sera from HCC patients for the identification of tumor autoantibodies. 19 Different protein variants were proposed as tumor-marker candidates.…”

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confidence: 99%

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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confidence: 99%

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

et al. 2004

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“…Under normal conditions, it can represent 25% of the total iron found in the body (19). Anemia is the most common hematologic abnormality associated with kidney cancer (1).…”

Section: Discussionmentioning

confidence: 99%

Differencial proteome of clear-cell renal cell carcinoma (ccRCC) tissues

et al. 2013

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Purpose: We attempted to detect, for the first time in a Brazilian cohort, differences in protein expression between clear-cell renal cell carcinoma (ccRCC) and their normal adjacent tissues, aiming to identify biomarkers and/or therapeutic target candidates for this disease. Material and Methods: Twenty-four ccRCC and adjacent normal tissues were collected after surgery and their protein extracts were quantified, pooled and separated by two--dimensional polyacrylamide gel electrophoresis (2DE), followed by statistical analysis of the stained gels. Spots of interest were excised from the gels, digested with trypsin and identified by MALDI-TOF-TOF mass spectrometry. Results: Twenty-six differential spots were detected between the two classes of tissues, among which twenty were identified by mass spectrometry and sixteen were found to be non-redundant. Eleven proteins were either underexpressed or undetected in the ccRCC extracts, such as prohibitin and peroxiredoxin-3, whereas five were found to be overexpressed or exclusively detected in the ccRCC extract, including αβ crystalin and heat shock protein 27. Conclusions: Several proteins were detected at differential levels when compared to normal adjacent tissues, and, moreover, many have been previously described by their relationship with RCC. Therefore, this work corroborates previous reports on the search for biomarkers for ccRCC, as well as it points out new candidates that may be validated in future studies.

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“…In a study to investigate the molecular basis for iron depletion in human HCC, 19 paired HCC tumor and adjacent non-tumor tissue samples were compared using 2D-PAGE-MS. The expression of an iron-storage protein, tissue ferritin light chain, was identified as severely reduced, whereas the corresponding transcript was not changed (Park et al, 2002b). Our group has applied proteomic tools to the comparative analysis of protein profiles between HCC and adjacent non-tumor liver tissues as a means of discovering novel molecular markers (Chignard et al, 2006).…”

Section: Tumor Tissuesmentioning

confidence: 99%