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Induction of ovarian cancer cell apoptosis by 1,25-dihydroxyvitamin D3 through the down-regulation of telomerase. Jiang F, Bao J, Li P, Nicosia SV, Bai W. J Biol Chem. 2004 Dec 17;279(51):53213-21. Epub 2004 Oct 12. PMID: 15485861 doi: 10.1074/jbc.M410395200 Overall, the study suggests that the down-regulation of telomerase activity by 1,25(OH)2VD3 and the resulting cell death are important components of the response of OCa cells to 1,25(OH)2VD3-induced growth suppression. Progressive shortening of telomere associated with cell divisions limits the life span of normal cells and eventually leads to senescence. To become immortal, human cancers including OCa are invariably associated with activation of mechanism that maintains telomere length. Approximately 85-90% of cancers show reactivation of telomerase. The present study shows that telomerase in OCa cells is down-regulated by 1,25(OH)2VD3. Down-regulation of telomerase is due to decreased stability of hTERT mRNA rather than VDRE-mediated transcriptional repression through the putative VDRE present in the regulatory region of the hTERT gene. It is known that the inhibition of telomerase may lead to a phenotypic lag during which cells would continue to divide until the point at which the telomeres became critically short. This phenomenon may explain why the apoptotic induction by 1,25(OH)2VD3 needs the treatment for more than 6 days. As mentioned in the results, no detectable shortening of telomeric repeats was observed in parental OVCAR3 cells after 9 days of treatment with 1,25(OH)2VD3 (Fig. 4D). This is likely due to the fact that the short telomere (about 3 kb) in OVCAR3 cells is very close to the minimal length required for survival and that cells with detectably shorter telomere may have been selected against apoptosis. It has been shown that transformed human cells enter crisis once the terminal restriction fragment of the telomere reaches a length of about 4 kb. This is insufficient to protect chro

The summer season each year brings wafting memories of a juicy and luscious fruit called litchi. The origins of Litchi lie in southern China where as a crop it has been cultivated uninterruptedly for close to 2500 years. Its geographical propagation has been rather slow, which is due to the short life-span of its seed and the peculiar soil and climatic requirements associated with the plant.A classical instance of this is India which is the second largest producer just behind China, but litchi farming is chronologically speaking, very recent having been introduced only sometime in the middle of the 1700's. Together China and India between themselves produce more than 90% of the world's Litchi, leaving the rest of the world far behind. In the backdrop of all this it is interesting to know the various cultivars and varieties which dot the world of Litchi farming. Most or all of them have their genesis probably in China but have been suitably bred and modified to thrive in countries of their adoption.

The terms 'cultivar' and 'variety' have often been used interchangeably but this convention often seems to ignore the obvious differences which exist between the two. A 'cultivar' is bred with the help of vegetative propagation, which could include cutting, grafting,budding and tissue culture and is a product of human effort and ingenuity. A 'variety' on the other hand is a natural phenomenon and is bred through seedlings. A 'variety' will always produce clones of the parent plant, but in a cultivar,there may be slight variation in a progeny compared to the parent particularly in the case of hybrids. The Litchi cultivars in India number about 40 out of which around 12 or 13 are commercially cultivated.The same cultivar or variety may be known by different names in various parts of the country. In China there are about 200 known cultivars although only 20 or so are in commercial farming, which means the genetic repository is much more widespread compar

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"5' AMP-activated protein kinase or AMPK or 5' adenosine monophosphate-activated protein kinase is an enzyme that plays a role in cellular energy homeostasis. It consists of three proteins (subunits) that together make a functional enzyme, conserved from yeast to humans. It is expressed in a number of tissues, including the liver, brain, and skeletal muscle. The net effect of AMPK activation is stimulation of hepatic fatty acid oxidation and ketogenesis, inhibition of cholesterol synthesis, lipogenesis, and triglyceride synthesis, inhibition of adipocyte lipolysis and lipogenesis, stimulation of skeletal muscle fatty acid oxidation and muscle glucose uptake, and modulation of insulin secretion by pancreatic beta-cells.[1] It should not be confused with cyclic AMP-activated protein kinase (protein kinase A), which, although being of similar nature, may have opposite effects.[2]"