The ubiquitin-proteasome system.

The 2004 Nobel Prize in chemistry for the discovery of protein ubiquitination has led to the recognition of cellular proteolysis as a central area of research in biology. Eukaryotic proteins targeted for degradation by this pathway are first 'tagged' by multimers of a protein known as ubiquitin and are later proteolyzed by a giant enzyme known as the proteasome. This article recounts the key observations that led to the discovery of ubiquitin-proteasome system (UPS). In addition, different aspects of proteasome biology are highlighted. Finally, some key roles of the UPS in different areas of biology and the use of inhibitors of this pathway as possible drug targets are discussed.

Mitigation of thyroxine-induced hyperglycaemia by two plant extracts.

Extracts of Trigonella foenum-graecum (TFG) seed and Allium sativum (AS) bulb were evaluated for their efficacy to ameliorate l-thyroxine (l-T4) induced hyperglycaemia in rats. Simultaneously, the serum cholesterol concentration, a supporting parameter for thyroid function, was also estimated. Thyroxine treatment in rats (300 microg/kg b. wt./day) increased the levels of both the thyroid hormones, namely thyroxine (T4) and tri-iodothyronine (T3) with a concomitant elevation in serum glucose concentration and a reduction in serum cholesterol level. Administration of TFG (220 mg/kg/day) and AS (500 mg/kg/day) extracts in hyperthyroid animals decreased the serum glucose concentration as well as the serum thyroid hormones. For comparison, propyl thiouracil (PTU), an antithyroid compound, was used as the standard at a daily dose of 10 mg/kg. The reductions in serum glucose and thyroid hormone concentrations in the plant extract treated groups were comparable to that in PTU treated animals. Our findings indicate that TFG seed and AS bulb extracts may prove to be effective in the treatment of thyroxine-induced hyperglycaemia.