In contrast, it was reported that leptin directly activates neutro-phils and delays spontaneous apoptosis of these cells by inhibiting proapoptotic events proximal to mitochondria, the effect being mediated via PI3K and p38 MAPK signaling pathways [ 68].
Recently, it has been reported that the functional leptin receptor OB-Rb is expressed in endothelial cells and it is functionally competent [ 20].
In addition, it has recently been reported that an increase in leptin levels in diet-induced obese rodents drives an increase in blood pressure, an effect that was not seen in animals deficient of leptin or leptin receptors [ 40].
Recently, it has been reported that the levels of expression of leptin and leptin receptor correlate with distant metastasis [ 47].
It has been reported that the promoter region of leptin gene contains transcription response elements including a TATA box, a CCAAT/enhancer binding protein (C/EBP) element, a leptin promoter specific factor (LP1) and a Sp1 site [31].
It has been reported that Dgat2 is regulated by Leptin and is involved in insulin resistance [ 43].
For example, it has been reported that smaller, hydrophilic peptides (e.g., leptin, 16 kDa) can be widely distributed throughout the CNS upon ICV delivery whereas larger polypeptides (e.g., FGF-2, 22 kDa; GDNF, 24 kDa) which also have an affinity for components (e.g., heparan sulfate) of the extracellular matrix have a more limited distribution [26], [27].
It has recently been reported that changes in adiponectin/leptin (A/L) ratio were independent predictors of carotid intima-media thickness (IMT) alterations [ 11].
In 2008, Unger and colleagues reported that leptin overexpression is capable of rescuing the sever hyperglycemia and lethality brought on by insulin deficiency in rodents [ 2].
Similarly, it was reported that serum leptin and resistin levels were positively associated with BMI and adiponectin is negatively correlated with BMI [ 52].
