Reduction of senescence‐associated beta‐galactosidase activity by vitamin E in human fibroblasts depends on subjects’ age and cell passage number

BioFactors ◽  
2020 ◽  
Vol 46 (4) ◽  
pp. 665-674
Author(s):  
Roberta Ricciarelli ◽  
Angelo Azzi ◽  
Jean‐Marc Zingg
Keyword(s):  
Vitamin E ◽  
Human Fibroblasts ◽  
Galactosidase Activity ◽  
Cell Passage ◽  
Passage Number ◽  
Beta Galactosidase

Decline of Fibroblast Chemotaxis with Age of Donor and Cell Passage Number

1988 ◽  
Vol 8 (1) ◽  
pp. 23-37 ◽  
Author(s):  
Adriana Albini ◽  
Bertram Pontz ◽  
Matthias Pulz ◽  
Gabriella Allavena ◽  
Hartwig Mensing ◽  
...  
Keyword(s):  
Cell Passage ◽  
Passage Number

Overlapping reading frames at the LYS5 locus in the yeast Yarrowia lipolytica

1990 ◽  
Vol 10 (9) ◽  
pp. 4795-4806
Author(s):  
J W Xuan ◽  
P Fournier ◽  
N Declerck ◽  
M Chasles ◽  
C Gaillardin
Keyword(s):  
Yarrowia Lipolytica ◽  
Stop Codon ◽  
Open Reading Frames ◽  
Yeast Cells ◽  
Lacz Gene ◽  
Galactosidase Activity ◽  
Phenotypic Effect ◽  
Frame Fusion ◽  
Beta Galactosidase ◽  
Reading Frames

Mutants affected at the LYS5 locus of Yarrowia lipolytica lack detectable dehydrogenase (SDH) activity. The LYS5 gene has previously been cloned, and we present here the sequence of the 2.5-kilobase-pair (kb) DNA fragment complementing the lys5 mutation. Two large antiparallel open reading frames (ORF1 and ORF2) were observed, flanked by potential transcription signals. Both ORFs appear to be transcribed, but several lines of evidence suggest that only ORF2 is translated and encodes SDH. (i) The global amino acid compositions of Saccharomyces cerevisiae SDH and of the putative ORF2 product are similar and that of ORF1 is dissimilar. (ii) An in-frame translational fusion of ORF2 with the Escherichia coli lacZ gene was introduced into yeast cells and resulted in a beta-galactosidase activity regulated similarly to SDH; no beta-galactosidase activity was obtained with an in-frame fusion of ORF1 with lacZ. (iii) The introduction of a stop codon at the beginning of ORF2 prevented SDH expression in yeast cells, whereas no phenotypic effect was observed when ORF1 translation was blocked.

scholarly journals Turnover of β-galactosidase in fibroblasts from patients with genetically different types of β-galactosidase deficiency

1981 ◽  
Vol 200 (1) ◽  
pp. 143-151 ◽  
Author(s):  
O P Van Diggelen ◽  
A W Schram ◽  
M L Sinnott ◽  
P J Smith ◽  
D Robinson ◽  
...  
Keyword(s):  
Hydrolytic Activity ◽  
Cellular Protein ◽  
Turnover Time ◽  
Galactosidase Activity ◽  
Normal Amount ◽  
Gm1 Gangliosidosis ◽  
Different Types ◽  
Suicide Substrate ◽  
Mutant Cells ◽  
Beta Galactosidase

The turnover of lysosomal beta-galactosidase was studied in fibroblast cultures from patients with Gm1-gangliosidosis and combined beta-galactosidase and neuraminidase deficiency, which had 5-10% residual beta-galactosidase activity. beta-Galactosidase was specifically inactivated with the suicide substrate beta-D-galactopyranosylmethyl-p-nitro-phenyltriazene (beta-Gal-MNT) and from the subsequent restoration of enzyme activity in cell cultures turnover times were calculated. By using [3H]beta-Gal-MNT, the hydrolytic activity per molecule of beta-galactosidase was determined. 3H-labelled beta-D-galactopyranosylmethylamine, the precursor of [3H]beta-gal-MNT, was obtained by Raney-nickel-catalysed exchange with 3H2O. The rate of synthesis of beta-galactosidase in normal and all mutant cells tested was found to be 0.4-0.5 pmol/day per mg of cellular protein. The GM1-gangliosidosis cells tested contain the normal amount of 0.5 pmol of beta-galactosidase/mg of protein with a normal turnover time of about 10 days, but only 10% of beta-galactosidase activity per enzyme molecule. Cells with combined beta-galactosidase and neuraminidase deficiency contain only 0.3 pmol of beta-galactosidase/mg of protein with a decreased turnover time of 1 day and normal hydrolytic properties (200 nmol of 4-methylumbelliferyl galactoside/h pmol of beta-galactosidase).

scholarly journals Vitamin E activates CRABP-II gene expression in cultured human fibroblasts, role of protein kinase C

FEBS Letters ◽  
2004 ◽  
Vol 569 (1-3) ◽  
pp. 240-244 ◽  
Author(s):  
Amparo Gimeno ◽  
Rosa Zaragozá ◽  
Juan R Viña ◽  
Vicente J Miralles
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Vitamin E ◽  
Protein Kinase ◽  
Human Fibroblasts ◽  
Kinase C ◽  
Cultured Human Fibroblasts ◽  
Crabp Ii
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