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5 results on '"David Oaxaca-Castillo"'

1. Docosahexaenoic acid inhibits cancer cell growth via p27Kip1, CDK2, ERK1/ERK2, and retinoblastoma phosphorylation

Author

Naim A. Khan, Kazuhiro Nishimura, Virginie Aires, Tomoko Yamashita, David Oaxaca-Castillo, Keiko Kashiwagi, and Kazuei Igarashi

Subjects
fatty acids, cell cycle, cyclin-dependent kinase, Biochemistry, QD415-436
Abstract

Docosahexaenoic acid (DHA), a PUFA of the n-3 family, inhibited the growth of FM3A mouse mammary cancer cells by arresting their progression from the late-G1 to the S phase of the cell cycle. DHA upregulated p27Kip1 levels by inhibiting phosphorylation of mitogen-activated protein (MAP) kinases, i.e., ERK1/ERK2. Indeed, inhibition of ERK1/ERK2 phosphorylation by DHA, U0126 [chemical MAPK extracellularly signal-regulated kinase kinase (MEK) inhibitor], and MEKSA (cells expressing dominant negative constructs of MEK) resulted in the accumulation of p27Kip1. MAP kinase (MAPK) inhibition by DHA did not increase p27Kip1 mRNA levels. Rather, this fatty acid stabilized p27Kip1 contents and inhibited MAPK-dependent proteasomal degradation of this protein. DHA also diminished cyclin E phosphorylation, cyclin-dependent kinase-2 (CDK2) activity, and phosphorylation of retinoblastoma protein in these cells. Our study shows that DHA arrests cell growth by modulating the phosphorylation of cell cycle-related proteins.

Published
2006
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4. Biochemical characterization of two functional human liver acyl-CoA oxidase isoforms 1a and 1b encoded by a single gene

Author

Sangtao Yu, David Oaxaca-Castillo, Pierre Andreoletti, Paul P. Van Veldhoven, Aurore Vluggens, Mustapha Cherkaoui-Malki, and Janardan K. Reddy

Subjects
chemistry.chemical_classification, Gene isoform, Oxidase test, Biophysics, Cell Biology, Biology, Peroxisome, Biochemistry, Isozyme, Molecular biology, Article, Enzyme Activation, Isoenzymes, Molecular Weight, Enzyme, chemistry, Liver, Enzyme Stability, Acyl-CoA oxidase, ACOX1, Humans, Heterologous expression, Acyl-CoA Oxidase, Molecular Biology
Abstract

Human acyl-CoA oxidase 1 (ACOX1) is a rate-limiting enzyme in peroxisomal fatty acids β-oxidation and its deficiency is associated with a lethal, autosomal recessive disease, called pseudoneonatal-adrenoleukodystrophy. Two mRNA variants, transcribed from a single gene encode ACOX1a or ACOX1b isoforms, respectively. Recently, a mutation in a splice site has been reported [H. Rosewich, H.R. Waterham, R.J. Wanders, S. Ferdinandusse, M. Henneke, D. Hunneman, J. Gartner, Pitfall in metabolic screening in a patient with fatal peroxisomal β-oxidation defect, Neuropediatrics 37 (2006) 95–98.], which results in the defective peroxisomal fatty acids β-oxidation. Here, we show that these mRNA splice variants are expressed differentially in human liver. We investigated the biochemical role of the two human ACOX1 isoforms by heterologous expression of the catalytically active ACOX1a and ACOX1b enzymes in Escherichia coli. ACOX1a seems to be more labile and exhibits only 50% specific activity toward palmitoyl-CoA as compared to ACOX1b.

Published
2007

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