Xi-Lin Zhoa

Nankai University

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Adrian Hilton

University of Surrey

Defeng Chen

Beijing Institute of Technology

Thomas H. Woo

Johns Hopkins University

Xiongwei Chen

Wuhan University of Science and Technology

Ya‐Wen Chen

National Health Research Institutes

Qiang Liu

Chinese Academy of Medical Sciences & Peking Union Medical College

O. Michael Colvin

Duke University

Arthur I. Radin

New York Medical College

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Johns Hopkins University

University of Surrey

Royal Brisbane and Women's Hospital

UK Dementia Research Institute

Imperial College London

Signal Processing (United States)

Natural Hazards Research Australia

Commonwealth Scientific and Industrial Research Organisation

UNSW Sydney

Victoria Heart Institute Foundation

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Structure and expression of the cytosolic aldehyde dehydrogenase gene in cyclophosphamide-resistant murine leukemia L1210 cells

Biochemical Pharmacology (1991)

Arthur I. Radin Xi-Lin Zhoa Thomas H. Woo O. Michael Colvin Adrian Hilton

These investigations were performed to clarify the molecular basis for the enhanced expression of cytosolic aldehyde dehydrogenase (ALDH-1) enzymatic activity in the cyclophosphamide-resistant L1210/CPA murine leukemia cell line, as compared to the parental L1210/O strain. Western immunoblot analysis was performed using a 15-fold greater quantity of cytosolic protein from the L1210/O as compared to the L1210/CPA cell line. Nevertheless, ALDH-1 immunoreactive protein could be detected only in the L1210/CPA cells. Northern analyses, performed using total cellular and polyadenylated RNA, again demonstrated ALDH-1-specific transcripts only in the L1210/CPA cell line. This transcript was identical in size to the ALDH-1 message expressed by normal murine hepatocytes. On Southern analysis, no evidence of gene amplification, gene rearrangement, or significant mutations of length was detected. These studies suggest that the ALDH-1 protein produced by the L1210/CPA cell line is structurally normal. Moreover, overexpression of the gene does not appear to have arisen as a result of an incremental process, such as gene amplification. Rather, a qualitative abnormality in the regulation of this gene appears to exist in the L1210/CPA cells, which distinguishes them from L1210/O cells and from normal murine lymphocytes.

L1210 cells

10.1016/0006-2952(91)90592-s

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The inhibition of restrication endonuclease Pcull cleavage activity by methylaytion outside its recognitionm sequecne

Nucleic Acids Research (1991)

Defeng Chen Qiang Liu Xiongwei Chen Xi-Lin Zhoa Ya‐Wen Chen

The recombinant plasmid pGEM4Z-ras DNA which was methylated on dam and dcm sites outside the PvuII recognition sequence was digested with restriction endonuclease PvuII, and one of the three PvuII sites was about 16-fold less efficient to cleave than either of the other two. On the contrary, the three PvuII sites were cleaved at about the same rate on the unmethylated DNA molecule. The results show that the cleavage inhibition of the methylated DNA on the certain PvuII site was caused by methylation outside the PvuII recognition sequence. Maybe a adjacent methylated dam site *A was responsible for the less efficient cleavage. This observation suggests that methylation outside the recognition sequence may be considered a new factor in the kinetic experiment of restriction endonuclease.

Cleavage (geology)

Recognition sequence

Cleave

10.1093/nar/19.20.5703

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Citations (9)