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We began analyzing https://link.springer.com/article/10.1007/s11064-005-6771-1, but it redirected us to https://link.springer.com/article/10.1007/s11064-005-6771-1. The analysis below is for the second page.

Title[redir]:
A Study of Glutathione S-transferase pi Expression in Central Nervous System of Subjects with Amyotrophic Lateral Sclerosis Using RNA Extraction from Formalin-Fixed, Paraffin-Embedded Material | Neurochemical Research
Description:
The expression of glutathione S-transferase pi (GST pi), an enzyme responsible for inactivation of a large variety of toxic compounds was studied in spinal cord, motor and sensory brain cortex obtained from patients who died in the course of amyotrophic lateral sclerosis (ALS). The studies were performed on formalin-fixed, paraffin-embedded (FFPE) and freshly frozen tissues. The method of RNA isolation from FFPE was modified. A significant decrease of GST pi-mRNA expression was found in cervical spinal cord and motor brain cortex of ALS subjects comparing to analogue control tissues (P < 0.01), as well as in motor cortex of ALS subjects comparing to their sensory cortex (P < 0.05). In spinal cords the decrease in GST pi-mRNA expression was accompanied by a decrease of GST pi protein level. Results indicated lowered GST pi expression on both mRNA and protein levels in the regions of nervous system affected by ALS. The non-properly inactivated by GST toxic electrophiles and organic peroxides may thus contribute to motor neurons damage.

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Keywords {🔍}

google, scholar, article, pubmed, glutathione, expression, amyotrophic, lateral, sclerosis, brain, human, stransferase, formalinfixed, paraffinembedded, motor, gene, biochem, analysis, subjects, rna, gst, res, privacy, cookies, content, research, barańczykkuźma, spinal, cortex, access, publish, search, system, beata, kaźmierczak, kuźma, cord, stransferases, mannervik, warsaw, function, data, information, log, journal, nervous, material, usarek, gajewska, anna,

Topics {✒️}

brain glutathione-s-transferase neurochem paraffin-embedded material published amyotrophic lateral sclerosis paraffin-embedded material glutathione s-transferase pi cervical spinal cord paraffin-embedded tumor tissue glutathione-s-transferases pi month download article/chapter microdissected archival formalin-fixed spinal cord motor brain cortex human glutathione s-transferases gst pi-mrna expression glutathione s-transferase formalin-fixed samples methylmercury-exposed experimental neurotoxicity ifn-gamma mrna levels glutathione s-transferases anna barańczyk-kuźma glutathione transferase catalyse astrocytoma brain biochim mdr1 gene expression peripheral motor nerve paraffin-embedded privacy choices/manage cookies full article pdf motor cortex motor neurons damage antioxidant drugs block mdr1 mrna expression human brain central nervous system freshly frozen tissues analogue control tissues spinal cords nervous system affected oxidative stress biochem check access instant access formalin-fixed ppar-gamma signaling european economic area sensory cortex gst toxic electrophiles immunologically distinct types molecular biology application 26500-mr subunits biochem conditions privacy policy related subjects

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      description:The expression of glutathione S-transferase pi (GST pi), an enzyme responsible for inactivation of a large variety of toxic compounds was studied in spinal cord, motor and sensory brain cortex obtained from patients who died in the course of amyotrophic lateral sclerosis (ALS). The studies were performed on formalin-fixed, paraffin-embedded (FFPE) and freshly frozen tissues. The method of RNA isolation from FFPE was modified. A significant decrease of GST pi-mRNA expression was found in cervical spinal cord and motor brain cortex of ALS subjects comparing to analogue control tissues (P < 0.01), as well as in motor cortex of ALS subjects comparing to their sensory cortex (P < 0.05). In spinal cords the decrease in GST pi-mRNA expression was accompanied by a decrease of GST pi protein level. Results indicated lowered GST pi expression on both mRNA and protein levels in the regions of nervous system affected by ALS. The non-properly inactivated by GST toxic electrophiles and organic peroxides may thus contribute to motor neurons damage.
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