Literature DB >> 10037490

Rat brain thioltransferase: regional distribution, immunological characterization, and localization by fluorescent in situ hybridization.

S Balijepalli1, P S Tirumalai, K V Swamy, M R Boyd, J J Mieyal, V Ravindranath.   

Abstract

Thioltransferase (TTase) is a member of the family of thiol-disulfide oxidoreductases that are involved in the maintenance of sulfhydryl homeostasis in cells by catalyzing thiol-disulfide interchange reactions. One of the major consequences of oxidative stress in brain is the formation of protein-glutathione mixed disulfides (through oxidation of protein thiols), which can be reversed by TTase during the recovery of brain from oxidative stress. We therefore examined the presence of TTase in brain regions from rat. In the rat, TTase activity in the whole brain was comparable with the corresponding activity in liver, but significantly higher in hippocampus. The enzyme activity was significantly lower in striatum and cerebellum compared with activity in whole brain. Rat brain TTase shared immunological similarity with the human red blood cell enzyme, but not with the pig liver enzyme. The constitutive expression of the mRNA to TTase was demonstrable by northern blotting. Localization of the TTase mRNA in rat brain by fluorescent in situ hybridization showed the presence of high amounts of mRNA in the olfactory bulb, cortex, and hippocampus and its predominant localization in the neurons. TTase mRNA was also present in Purkinje cells in the cerebellum, in giant reticular neurons in the midbrain, and in the striatal and thalamic neurons. This study demonstrates the constitutive presence of a functional TTase system in brain and delineates the regional and cellular localization of the enzyme in rat brain.

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Year:  1999        PMID: 10037490     DOI: 10.1046/j.1471-4159.1999.0721170.x

Source DB:  PubMed          Journal:  J Neurochem        ISSN: 0022-3042            Impact factor:   5.372


  6 in total

Review 1.  Thiol-redox signaling, dopaminergic cell death, and Parkinson's disease.

Authors:  Aracely Garcia-Garcia; Laura Zavala-Flores; Humberto Rodriguez-Rocha; Rodrigo Franco
Journal:  Antioxid Redox Signal       Date:  2012-05-03       Impact factor: 8.401

2.  Glutaredoxin 1 protects dopaminergic cells by increased protein glutathionylation in experimental Parkinson's disease.

Authors:  Humberto Rodriguez-Rocha; Aracely Garcia Garcia; Laura Zavala-Flores; Sumin Li; Nandakumar Madayiputhiya; Rodrigo Franco
Journal:  Antioxid Redox Signal       Date:  2012-09-14       Impact factor: 8.401

3.  A disruption in iron-sulfur center biogenesis via inhibition of mitochondrial dithiol glutaredoxin 2 may contribute to mitochondrial and cellular iron dysregulation in mammalian glutathione-depleted dopaminergic cells: implications for Parkinson's disease.

Authors:  Donna W Lee; Deepinder Kaur; Shankar J Chinta; Subramanian Rajagopalan; Julie K Andersen
Journal:  Antioxid Redox Signal       Date:  2009-09       Impact factor: 8.401

4.  Reduced glutathione is highly expressed in white matter and neurons in the unperturbed mouse brain--implications for oxidative stress associated with neurodegeneration.

Authors:  V M Miller; D A Lawrence; T K Mondal; R F Seegal
Journal:  Brain Res       Date:  2009-04-22       Impact factor: 3.252

5.  Thioltransferase (glutaredoxin) mediates recovery of motor neurons from excitotoxic mitochondrial injury.

Authors:  Rajappa S Kenchappa; Latha Diwakar; Michael R Boyd; Vijayalakshmi Ravindranath
Journal:  J Neurosci       Date:  2002-10-01       Impact factor: 6.167

6.  Role of the P-Type ATPases, ATP7A and ATP7B in brain copper homeostasis.

Authors:  Jonathon Telianidis; Ya Hui Hung; Stephanie Materia; Sharon La Fontaine
Journal:  Front Aging Neurosci       Date:  2013-08-23       Impact factor: 5.750

  6 in total

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