Redox atlas of the mouse. Immunohistochemical detection of glutaredoxin-, peroxiredoxin-, and thioredoxin-family proteins in various tissues of the laboratory mouse.

GODOY JR, FUNKE M, ACKERMANN W, HAUNHORST P, OESTERITZ S, CAPANI F, ELSäSSER HP, LILLIG CH.

BIOCHIMICA AND BIOPHYSICA ACTA

Elsevier

Año: 2011 vol. 1810 p. 2 - 92

0006-3002

Background: Oxidoreductases of the thioredoxin family of proteins have been thoroughly studied in numerous cellular and animal models mimicking human diseases. Despite of their well documented role in various disease conditions, no systematic information on the presence of these proteins was available. Methods: Here, we have systematically analyzed the presence of some of the major constituents of the glutaredoxin (Grx)-, peroxiredoxin (Prx)-, and thioredoxin (Trx)-systems, i.e. Grx1, Grx2, Grx3 (TXNL-2/PICOT), Grx5, nucleoredoxin (Nrx), Prx1, Prx2, Prx3, Prx4, Prx5, Prx6, Trx1, thioredoxin reductase (TrxR) 1, Trx2, TrxR2, and ã-glutamyl cysteine synthetase (ã-GCS) in various tissues of the mouse using immunohistochemistry. Results: The identification of the Trx family proteins in the central nervous system, sensory organs, digestive system, lymphatic system, reproductive system, urinary system, respiratory system, endocrine system, skin, heart, and muscle revealed a number of significant differences between the different proteins with respect to their distribution in these tissues. Conclusion: Our results imply more specific functions and interactions between the proteins of this family than previously assumed. General Significance: Crucial functions of Trx family proteins have been demonstrated in various disease conditions. A detailed overview on their distribution in various tissues will be helpful to fully comprehend their potential role and the interactions of these proteins in the most thoroughly studied model for human diseases – the laboratory mouse. Oxidoreductases of the thioredoxin family of proteins have been thoroughly studied in numerous cellular and animal models mimicking human diseases. Despite of their well documented role in various disease conditions, no systematic information on the presence of these proteins was available. Methods: Here, we have systematically analyzed the presence of some of the major constituents of the glutaredoxin (Grx)-, peroxiredoxin (Prx)-, and thioredoxin (Trx)-systems, i.e. Grx1, Grx2, Grx3 (TXNL-2/PICOT), Grx5, nucleoredoxin (Nrx), Prx1, Prx2, Prx3, Prx4, Prx5, Prx6, Trx1, thioredoxin reductase (TrxR) 1, Trx2, TrxR2, and ã-glutamyl cysteine synthetase (ã-GCS) in various tissues of the mouse using immunohistochemistry. Results: The identification of the Trx family proteins in the central nervous system, sensory organs, digestive system, lymphatic system, reproductive system, urinary system, respiratory system, endocrine system, skin, heart, and muscle revealed a number of significant differences between the different proteins with respect to their distribution in these tissues. Conclusion: Our results imply more specific functions and interactions between the proteins of this family than previously assumed. General Significance: Crucial functions of Trx family proteins have been demonstrated in various disease conditions. A detailed overview on their distribution in various tissues will be helpful to fully comprehend their potential role and the interactions of these proteins in the most thoroughly studied model for human diseases – the laboratory mouse.