Proteomic alterations of the variants of human aldehyde dehydrogenase isozymes correlate with hepatocellular carcinoma

Kang Sik Park; Sang Yun Cho; Hoguen Kim; Young Ki Paik

doi:10.1002/ijc.1585

Proteomic alterations of the variants of human aldehyde dehydrogenase isozymes correlate with hepatocellular carcinoma

Kang Sik Park, Sang Yun Cho, Hoguen Kim, Young Ki Paik

Research output: Contribution to journal › Article › peer-review

82 Citations (Scopus)

Abstract

To develop novel markers for hepatocellular carcinomas (HCC), 10 cases were analyzed by 2-dimensional electrophoresis (2DE) and matrix-assisted laser desorption ionization mass spectrometry. Results were compared to those of paired adjacent nontumorous liver tissues. Comparative analysis of the respective spot patterns in 2DE revealed that 3 variants of class 3 aldehyde dehydrogenase (ALDH-3) newly appeared while 2 variants of ALDH-2 diminished to undetectable levels in HCC. However, 4 ALDH-1 variants with different pls remained unaffected. This pattern of concomitant appearance and disappearance of ALDH-3 and ALDH-2 variants was consistently observed in all HCC tissues. Our results suggest that alterations of ALDH isozyme variants may be closely correlated to HCC and that proteomic analysis of these proteins might be a novel approach to identify the molecular events in detail during hepatocarcinogenesis.

Original language	English
Pages (from-to)	261-265
Number of pages	5
Journal	International Journal of Cancer
Volume	97
Issue number	2
DOIs	https://doi.org/10.1002/ijc.1585
Publication status	Published - 2002 Jan 10

All Science Journal Classification (ASJC) codes

Oncology
Cancer Research

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1002/ijc.1585

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title = "Proteomic alterations of the variants of human aldehyde dehydrogenase isozymes correlate with hepatocellular carcinoma",

abstract = "To develop novel markers for hepatocellular carcinomas (HCC), 10 cases were analyzed by 2-dimensional electrophoresis (2DE) and matrix-assisted laser desorption ionization mass spectrometry. Results were compared to those of paired adjacent nontumorous liver tissues. Comparative analysis of the respective spot patterns in 2DE revealed that 3 variants of class 3 aldehyde dehydrogenase (ALDH-3) newly appeared while 2 variants of ALDH-2 diminished to undetectable levels in HCC. However, 4 ALDH-1 variants with different pls remained unaffected. This pattern of concomitant appearance and disappearance of ALDH-3 and ALDH-2 variants was consistently observed in all HCC tissues. Our results suggest that alterations of ALDH isozyme variants may be closely correlated to HCC and that proteomic analysis of these proteins might be a novel approach to identify the molecular events in detail during hepatocarcinogenesis.",

author = "Park, {Kang Sik} and Cho, {Sang Yun} and Hoguen Kim and Paik, {Young Ki}",

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AU - Park, Kang Sik

AU - Cho, Sang Yun

AU - Kim, Hoguen

AU - Paik, Young Ki

PY - 2002/1/10

Y1 - 2002/1/10

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AB - To develop novel markers for hepatocellular carcinomas (HCC), 10 cases were analyzed by 2-dimensional electrophoresis (2DE) and matrix-assisted laser desorption ionization mass spectrometry. Results were compared to those of paired adjacent nontumorous liver tissues. Comparative analysis of the respective spot patterns in 2DE revealed that 3 variants of class 3 aldehyde dehydrogenase (ALDH-3) newly appeared while 2 variants of ALDH-2 diminished to undetectable levels in HCC. However, 4 ALDH-1 variants with different pls remained unaffected. This pattern of concomitant appearance and disappearance of ALDH-3 and ALDH-2 variants was consistently observed in all HCC tissues. Our results suggest that alterations of ALDH isozyme variants may be closely correlated to HCC and that proteomic analysis of these proteins might be a novel approach to identify the molecular events in detail during hepatocarcinogenesis.

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Proteomic alterations of the variants of human aldehyde dehydrogenase isozymes correlate with hepatocellular carcinoma

Abstract

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