Abstract
The PPAR nuclear receptor family has acquired great relevance in the last decade, which is formed by three different isoforms (PPARα, PPARβ/δ, and PPAR ϒ). Those nuclear receptors are members of the steroid receptor superfamily which take part in essential metabolic and life-sustaining actions. Specifically, PPARG has been implicated in the regulation of processes concerning metabolism, inflammation, atherosclerosis, cell differentiation, and proliferation. Thus, a considerable amount of literature has emerged in the last ten years linking PPARG signalling with metabolic conditions such as obesity and diabetes, cardiovascular disease, and, more recently, cancer. This review paper, at crossroads of basic sciences, preclinical, and clinical data, intends to analyse the last research concerning PPARG signalling in obesity and cancer. Afterwards, possible links between four interrelated actors will be established: PPARG, the vitamin D/VDR system, obesity, and cancer, opening up the door to further investigation and new hypothesis in this fascinating area of research.
Highlights
There are three subtypes of PPARG, known as PPARG1, PPARG2, and PPARG3
The considerable host of actions performed by PPARG can be compared to those of vitamin D and vitamin D receptor (VDR) [15], which has been implicated in neurologic disorders [16,17,18], autoimmune pathologies [19,20,21], cardiovascular disease [22], diabetes mellitus [23, 24], psoriasis [15] or infectious disease [25, 26], and, above all of what is mentioned, cancer [27, 28]
The PPARG transcription factor has been classically associated with metabolic homeostasis and lipid storage functions
Summary
There are three subtypes of PPARG, known as PPARG1, PPARG2, and PPARG3. It has been established that PPARG2 leads in potency as a transcription factor [1]. In order to modulate gene expression, the PPAR NRs family, and the PPARG, after binding with either natural or synthetic ligands, heterodimerizes with the Retinoid X Receptor (RXR) as vitamin D receptor (VDR) does. The complex PPARG-RXR translocates to the nucleus in order to get attached to PPREs (PPAR Response Elements), genome nucleotides sequences wherefrom the PPARs will coordinate the expression or repression of some genes involved in metabolism, immunity, differentiation, or cellular proliferation, to cite some [3,4,5,6]. Several molecules known as corepressors and coactivators, which show histone modifying activities by themselves [7], bind the PPARG-RXR complex, showing some control over the genetic expression-repression interplay. Afar of its PPAR Research adipose functions PPARG is vital for development of some important organs such as heart and the placenta [11]
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