Articles written in Journal of Biosciences
Volume 20 Issue 4 September 1995 pp 461-471
The non-transmembrane protein tyrosine phosphatase, PTP-S, is located predominantly in the cell nucleus in association with chromatin. Here we have analysed the expression of PTP-S upon mitogenic stimulation and during cell division cycle. During liver regeneration after partial hepatectomy, PTP-S mRNA levels increased 16-fold after 6 h (G1 phase) and declined thereafter. Upon stimulation of serum starved cells in culture with serum, PTP-S mRNA levels increased reaching a maximum during late G1 phase and declined thereafter. No significant change in PTP-S RNA levels was observed in growing cells during cell cycle. PTP-S protein levels were also found to increase upon mitogenic stimulation. Upon serum starvation for 72 h, PTP-S protein disappears from the nucleus and is seen in the cytoplasm; after 96 h of serum starvation the PTP-S protein disappears from the nucleus as well as cytoplasm. Refeeding of starved cells for 6 h results in reappearance of this protein in the nucleus. Our results suggest a role of this phosphatase during cell proliferation.
Volume 25 Issue 1 March 2000 pp 33-40 Articles
PTP-S2 is a tyrosine specific protein phosphatase that binds to DNA and is localized to the nucleus in association with chromatin. It plays a role in the regulation of cell proliferation. Here we show that the subcellular distribution of this protein changes during cell division. While PTP-S2 was localized exclusively to the nucleus in interphase cells, during metaphase and anaphase it was distributed throughout the cytoplasm and excluded from condensed chromosomes. At telophase PTP-S2 began to associate with chromosomes and at cytokinesis it was associated with chromatin in the newly formed nucleus. It was hyperphosphorylated and showed retarded mobility in cells arrested in metaphase.
Volume 29 Issue 2 June 2004 pp 129-131 Clipboard
Volume 35 Issue 4 December 2010 pp 501-505
Volume 41 Issue 4 December 2016 pp 563-567 COMMENTARY
The Nobel Prize in Physiology or Medicine, 2016, was awarded to Prof Yoshinori Ohsumi from TokyoInstitute of Technology, Yokohoma, Japan, for his work that helped in understanding the molecularmechanisms of autophagy, a process used by most eukaryotic cells to degrade a portion of cytoplasmincluding damaged organelles, large protein complexes and aggregated proteins in lysosomes. This processof autophagy (self-eating) maintains cellular homeostasis and helps the cell and the organism to surviveduring periods of stress, such as starvation, by recycling the cellular components to generate amino acidsand nutrients needed for producing energy. Autophagy and ubiquitin-proteasome system are the two majorprotein degradation systems in the cell.The lysosome was identified by Christian de Duve in the 1950s as a membrane bound organelle in thecell that contains degradative enzymes such as proteases, lipases, acid phosphatases, etc. (de Duve, 2005).The term autophagy was coined by Christian de Duve in 1963. Autophagy generally occurs at low level, butit increases under conditions such as stress and differentiation/remodelling of tissues. Autophagy wasprimarily studied by electron microscopy for decades because no molecular markers were available for itsmolecular analysis.
Volume 44 | Issue 5
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