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Potent induction of phase 2 enzymes in human prostate cells by sulforaphane

Autor: J D, Brooks, V G, Paton, G, Vidanes

Publikováno v: Cancer epidemiology, biomarkersprevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology. 10(9)

Two population-based, case-control studies have documented reduced risk of prostate cancer in men who consume cruciferous vegetables. Cruciferae contain high levels of the isothiocyanate sulforaphane. Sulforaphane is known to bolster the defenses of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::342fdf63f7b642a7453e44bf9413af59
https://pubmed.ncbi.nlm.nih.gov/11535546

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Splice donor site mutations in the 3-hydroxy-3-methylglutaryl coenzyme A reductase gene cause a deficiency of the endoplasmic reticulum 3-hydroxy-3-methylglutaryl coenzyme A reductase protein in UT2 cells

Autor: W H, Engfelt, K R, Masuda, V G, Paton, S K, Krisans

Publikováno v: Journal of lipid research. 39(11)

UT2 cells are a mutant clone of Chinese hamster ovary (CHO) cells that are deficient in the 97 kDa endoplasmic reticulum (ER) 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase protein. The analysis of UT2 cell cDNA and genomic DNA has led to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5f831da7115bdebbac65954dce44867c
https://pubmed.ncbi.nlm.nih.gov/9799804

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Characterization of UT2 cells. The induction of peroxisomal 3-hydroxy-3-methylglutaryl-coenzyme a reductase

Autor: W H, Engfelt, J E, Shackelford, N, Aboushadi, N, Jessani, K, Masuda, V G, Paton, G A, Keller, S K, Krisans

Publikováno v: The Journal of biological chemistry. 272(39)

In the liver 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase is present not only in the endoplasmic reticulum but also in the peroxisomes. However, to date no information is available regarding the function of the peroxisomal HMG-CoA reduct

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2f687da664ac343fdfaa62da0b0bc38e
https://pubmed.ncbi.nlm.nih.gov/9305924

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Cloning and subcellular localization of hamster and rat isopentenyl diphosphate dimethylallyl diphosphate isomerase. A PTS1 motif targets the enzyme to peroxisomes

Autor: V G, Paton, J E, Shackelford, S K, Krisans

Publikováno v: The Journal of biological chemistry. 272(30)

To date, isopentenyl diphosphate:dimethylallyl diphosphate isomerase (IPP isomerase; EC 5.3.3.2) is presumed to have a cytosolic localization. However, we have recently shown that in permeabilized cells lacking cytosolic components, mevalonate can be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::41157ac864efd1b2cf0ffe0cf368ff78
https://pubmed.ncbi.nlm.nih.gov/9228075

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