Published online Jan 27, 2022. doi: 10.4331/wjbc.v13.i1.15
Peer-review started: March 26, 2021
First decision: July 8, 2021
Revised: July 9, 2021
Accepted: January 13, 2022
Article in press: January 13, 2022
Published online: January 27, 2022
Processing time: 301 Days and 14.5 Hours
Core Tip: The substrates of monoamine oxidase (MAO) and semicarbazide-sensitive amine oxidase (SSAO) partly reproduce the stimulatory effect of insulin on sugar entry in rat fat cells. Especially when combined with vanadium, tyramine and benzylamine mimic more than 70% of the insulin stimulation of glucose uptake. Unfortunately, such insulin activation of glucose utilization is strongly diminished in the genetically obese Zucker rat, an animal model of the metabolic syndrome. In this insulin-resistant and obese rat, the stimulation of glucose transport by tyramine is decreased as much as that of insulin, while the effect of benzylamine is even more altered. SSAO, responsible for benzylamine oxidation, is down-regulated in adipocytes from obese Zucker rats. In contrast, MAO, which predominantly supports the oxidation of tyramine, is increased, apparently not in a sufficient manner to reach the same hexose uptake activation seen in fat cells from lean rats. However, this greater ability to oxidize tyramine was found only in white adipocytes from obese rats since no change was found in the liver or skeletal muscle when compared to lean controls. Moreover, increased MAO activity in the large adipocytes of obese rats was accompanied by an enlarged number of imidazoline binding sites, previously described to be located on MAO. Since the repeated subcutaneous administration of tyramine plus vanadate is somewhat capable of reducing plasma glucose and triglycerides in obese rats, SSAO, MAO, and its associated imidazoline I2 sites deserve further studies with respect to their mimicking insulin action on glucose and lipid metabolism in fat cells.