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The Inactivation Mechanism of Low Molecular Weight Phosphotyrosine-protein Phosphatase by H2O2 *
It is suggested that oxidative stress conditions and other processes producing hydrogen peroxide regulate the LMW-PTP in thecell, because a physiological concentration of H2O2 produces enzyme inactivation and considering that the activity is restored by reduction with low molecular weight thiols. Expand
The expression of low molecular weight protein tyrosine phosphatase is up‐regulated in 1,2‐dimethylhydrazine‐induced colon tumours in rats
A significant increase in LMW‐PTP expression in adenocarcinomas is shown, suggesting that this phenomenon is associated with the onset of malignancy, confirming an observation already reported for human colon cancer. Expand
Erythropoietin rapidly induces tyrosine phosphorylation in the human erythropoietin-dependent cell line, UT-7.
Data show that tyrosine phosphorylation and P21ras activation are early signals in the Epo-induced mitogenic pathway. Expand
Up-regulated expression of low molecular weight protein tyrosine phosphatases in different human cancers.
It is suggested that LMW-PTP enhanced expression is generally prognostic for a more aggressive cancer and can be considered an oncogene as it is overexpressed in different tumour types. Expand
The 5′‐untranslated region of the human muscle acylphosphatase mRNA has an inhibitory effect on protein expression
The hypothesis is that the product of the upstream open reading frame could play a role in this mechanism, due to the presence of the 5′‐untranslated region of acylphosphatase mRNA. Expand
Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone.
T3 induction of skeletal muscle acylphosphatase mRNA is due, at least in part, to a fast and transient increase in the rate of gene transcription, within 4 h after hormone administration, which indicates that the transcriptional regulation of the gene may be indirect. Expand
Differential role of four cysteines on the activity of a low M r phosphotyrosine protein phosphatase
The construction or five mutants of a bovine liver low M r phosphotyrosine protein phosphatase (PTPase) expressed as a fusion protein with the maltose binding protein in E. coli are described and the involvement of Cys‐12 andCys‐17 in the catalytic site is confirmed and it is suggested that Cys'62 and Cys•145 mutations may destabilise the structure of the enzyme. Expand
Assignment of the human erythrocyte acylphosphatase gene (ACYP1) to chromosome band 14q24.3
The assignment of the human CT acylphosphatase gene to chromosome arm 14q at band q24 is reported, where it is shown that both isoforms are able to hydrolyze either DNA or RNA. Expand
Guinea pig acylphosphatase: The amino acid sequence
We determined the primary structure of guinea pig skeletal muscle acylphosphatase, using the high degree of homology with several vertebrate acylphosphatases to obtain correct alignment of theExpand
Plasma protein carbonylation and physical exercise.
The aim of this research was to characterize plasma protein carbonylation in response to physical exercise in trained male endurance athletes by proteomic approach and using 2D-GE followed by western blot with specific antibodies against carbonylated proteins to obtain an overview of plasma protein oxidation after physical exercise. Expand