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A 45 kDa protein related to PPARγ2, induced by peroxisome proliferators, is located in the mitochondrial matrix
Author(s) -
Casas François,
Domenjoud Lionel,
Rochard Pierrick,
Hatier Renée,
Rodier Anne,
Daury Laetitia,
Bianchi Arnaud,
Kremarik-Bouillaud Pascaline,
Becuwe Philippe,
Keller Jean-Marie,
Schohn Hervé,
Wrutniak-Cabello Chantal,
Cabello Gérard,
Dauça Michel
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01814-7
Subject(s) - peroxisome , peroxisome proliferator activated receptor , biology , peroxisome proliferator activated receptor alpha , clofibrate , blot , immunoprecipitation , mitochondrion , receptor , microbiology and biotechnology , mitochondrial matrix , organelle , biochemistry , nuclear receptor , transcription factor , cytosol , gene , enzyme
Besides their involvement in the control of nuclear gene expression by activating several peroxisome proliferator‐activated receptors (PPARs), peroxisome proliferators influence mitochondrial activity. By analogy with the previous characterization of a mitochondrial T3 receptor (p43), we searched for the presence of a peroxisome proliferator target in the organelle. Using several antisera raised against different domains of PPARs, we demonstrated by Western blotting, immunoprecipitation and electron microscopy experiments, that a 45 kDa protein related to PPARγ2 (mt‐PPAR) is located in the matrix of rat liver mitochondria. In addition, we found that the amounts of mt‐PPAR are increased by clofibrate treatment. Moreover, in EMSA experiments mt‐PPAR bound to a DR2 sequence located in the mitochondrial D‐loop, by forming a complex with p43. Last, studies of tissue‐specific expression indicated that mt‐PPAR is detected in mitochondria of all tissues tested except the brain in amounts positively related to p43 abundance.