ArticleJournal of bioenergetics and biomembranes2004
Characterization of rat testes mitochondrial retinoylating system and its partial purification.
Article in Journal of bioenergetics and biomembranes, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Capsaicin Analogues Derived fromNutrients · 2019Article
- Theophylline action on primary human bronchial epithelial cells under proinflammatory stimuli and steroidal drugs: a therapeutic rationale approach.Drug design, development and therapy · 2017Article
- Article
- Retinoylation reactions are inversely related to the cardiolipin level in testes mitochondria from hypothyroid rats.Journal of bioenergetics and biomembranes · 2010Article
- Adrenal glands and testes as steroidogenic tissue are affected by retinoylation reaction.Journal of bioenergetics and biomembranes · 2009Article
- Retinoic acid-induced testosterone production and retinoylation reaction are concomitant and exhibit a positive correlation in Leydig (TM-3) cells.Journal of bioenergetics and biomembranes · 2008Article
- Dietary fatty acid composition differently influences retinoylation reaction in rat testes mitochondria.Journal of bioenergetics and biomembranes · 2007Article
- Binding of all-trans-retinoic acid to MLTC-1 proteins.Molecular and cellular biochemistry · 2005Article
- Retinoylation reaction of proteins in Leydig (TM-3) cells.Journal of bioenergetics and biomembranes · 2005Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Retinoylation (retinoic acid acylation), a posttranslational modification of proteins occurring in a variety of eukariotic cell lines both in vivo and in vitro, was studied in rat testes mitochondria. all-trans-Retinoic acid, a highly active form of vitamin A in inducing cellular differentiation, is incorporated covalently into proteins of rat testes mitochondria. The maximum retinoylation activity of rat testes mitochondrial proteins was 21.6 pmoles mg protein(-1) 90 min(-1) at 37 degrees C. The activation energy was 44 kJ mol(-1) from 5 to 37 degrees C. The retinoylation activity had a pH optimum of 7.5. The retinoylation process was specific for the presence of ATP, ADP, and GTP (even if only 30% of the control). The half saturation constant (Km) was 0.69 microM for all-trans-retinoic acid, while the inhibition constant (Ki) was 1.5 microM for 13-cis-retinoic acid. Retinoylation was not inhibited by high concentrations of myristic acid (MA) and palmitic acid (PA), indicating that retinoylation and acylation reactions involved different rat testes mitochondrial proteins. The ATP or CoASH saturation curves of retinoylation reaction showed sigmoidal behavior with apparent half saturation constants (K0.5) of 6.5 mM ATP and 40.6 microM CoASH. On SDS-gel electrophoresis, the hydroxylapaptite/celite eluate showed various protein bands between 25 and 80 kDa. This retinoylated protein was purified 17-fold with respect to the mitochondrial extract.
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