Tissue, species, and environmental differences in absolute quantities of murine mRNAs coding for alpha, mu, omega, pi, and theta glutathione S-transferases.
This article reports the first absolute quantitative analysis of expression patterns of murine transcripts (Gsta1/2, Gsta3, Gsta4, Gstm1, Gstm2, Gstm3, Gsto1, Gstp1/2, Gstt1, Gstt2) coding for most glutathione S-transferases (GSTs) of alpha, mu, omega, pi, and theta classes. We examine how the steady-state numbers of transcripts are modulated in association with: three animal organs (liver, kidney, and lung) where extensive detoxification occurs; two species (Mus musculus and Mus spretus) representing common laboratory and aboriginal mice; and two genetic and animal living conditions (wild-derived inbred animals and free-living mice). Moreover, quantitations performed examine how the pulmonary steady-state Gst mRNA amounts are affected in M. musculus by paraquat (a superoxide generator), and in M. spretus by dwelling at a polluted area. The results point to complex tissue-, species-, and life condition-dependent expression of the investigated transcripts. Among others, they show: i) the ubiquity of most transcripts, except Gstm3 mRNA that was virtually absent or at very low amounts (< or = 0.001 molecules/pg) in kidney and lung of M. spretus; ii) unique expression profiles for each transcript and mouse organ examined; iii) outstanding species-specific differences in basal amounts of most Gst mRNAs, this effect being most apparent in the case of Gsta1/2, Gsta3, Gstm2, Gsto1, Gstt1, and Gstt2; iv) paraquat-induced upregulation of most Gst mRNAs, with the notable exception of those coding for theta class GSTs; v) a tendency for mice dwelling at a wildlife reserve of having lower and more homogeneous Gsta3 mRNA levels than those collected in an anthropogenic environment.
Ruiz-Laguna
Julia
J
Departamento de Bioquímica y Biologá Molecular, Campus de Rabanales, edificio Severo Ochoa, planta 2a, Carretera Madrid-Cádiz Km 396-a, Universidad de Córdoba, 14071-Córdoba, Spain.
Abril
Nieves
N
Prieto-Alamo
María-José
MJ
López-Barea
Juan
J
Pueyo
Carmen
C
D000818:Animals; D015415:Biomarkers; D002352:Carrier Proteins / Q000096:biosynthesis*; D002467:Cell Nucleus / Q000378:metabolism; D017931:DNA Primers / Q000737:chemistry; D004777:Environment; D005786:Gene Expression Regulation; D051549:Glutathione S-Transferase pi / Q000096:biosynthesis*; D005982:Glutathione Transferase / Q000096:biosynthesis* / Q000378:metabolism; D007527:Isoenzymes / Q000096:biosynthesis*; D007668:Kidney / Q000378:metabolism; D008099:Liver / Q000378:metabolism; D008168:Lung / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D015233:Models, Statistical; D018384:Oxidative Stress; D010269:Paraquat / Q000494:pharmacology; D012313:RNA / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism*; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013045:Species Specificity; D013481:Superoxides / Q000378:metabolism; D014018:Tissue Distribution; D015854:Up-Regulation
D015415:Biomarkers; D002352:Carrier Proteins; D017931:DNA Primers; C117709:Gsto1 protein, mouse; D007527:Isoenzymes; D012333:RNA, Messenger; D013481:Superoxides; D012313:RNA; C413545:glutathione S-transferase T1; D051549:Glutathione S-Transferase pi; D005982:Glutathione Transferase; C119995:glutathione S-transferase alpha; D010269:Paraquat