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Mohiadeen Batcha M.,Sajith Ahamed A.,Ur Rahman M. Ashiq,Janarthanan S.,Krishnan M. 한국응용곤충학회 2023 Journal of Asia-Pacific Entomology Vol.26 No.2
The present study aims to focus on the site of fat bodies involved in the differential expression of vitellogenin protein in Bombyx mori L which is not yet fully understood. Culturing fat bodies and analyzing in in vitro and in vivo approaches made it useful to study this pattern. In Bombyx mori, L. The vitellogenin protein is 200–205 kDa and resolves at two molecular weight regions that are at 180 kDa and 42 kDa. We subject dorsal perivisceral (DPV) and ventral perivisceral fat body (VPV), haemolymph for this radio labeling cell culture and incorporation experiment. Based on our in vitro and in vivo experiments of S 35 methionine fluorography, Scanning densito metric, Western blot analysis and RT-PCR expression studies had strongly proven that the ventral perivisceral fat body is the significant and exclusive site of differential vitellogenin expression in silkworm, Bombyx mori but not in dorsal peripheral fat body tissues, haemolymph by radiolabeling studies. The present paper describes an experimental set-up based on the incubation of ventral perivisceral and dorsal perivisceral fat bodies and the measurement of vitellogenin with S 35 protein labeling incorporation method. These findings from our lab were the first report proved by in vitro and in vivo labeling experiments.
Lee, Sanghyun,Zheng, Xueyun,Krishnamoorthy, Janarthanan,Savelieff, Masha G.,Park, Hyun Min,Brender, Jeffrey R.,Kim, Jin Hoon,Derrick, Jeffrey S.,Kochi, Akiko,Lee, Hyuck Jin,Kim, Cheal,Ramamoorthy, Ayy American Chemical Society 2014 JOURNAL OF THE AMERICAN CHEMICAL SOCIETY - Vol.136 No.1
<P>Alzheimer’s disease (AD) is characterized by multiple, intertwined pathological features, including amyloid-β (Aβ) aggregation, metal ion dyshomeostasis, and oxidative stress. We report a novel compound (<B><B>ML</B></B>) prototype of a rationally designed molecule obtained by integrating structural elements for Aβ aggregation control, metal chelation, reactive oxygen species (ROS) regulation, and antioxidant activity within a single molecule. Chemical, biochemical, ion mobility mass spectrometric, and NMR studies indicate that the compound <B><B>ML</B></B> targets metal-free and metal-bound Aβ (metal–Aβ) species, suppresses Aβ aggregation in vitro, and diminishes toxicity induced by Aβ and metal-treated Aβ in living cells. Comparison of <B><B>ML</B></B> to its structural moieties (i.e., 4-(dimethylamino)phenol (<B>DAP</B>) and (8-aminoquinolin-2-yl)methanol (<B>1</B>)) for reactivity with Aβ and metal–Aβ suggests the synergy of incorporating structural components for both metal chelation and Aβ interaction. Moreover, <B><B>ML</B></B> is water-soluble and potentially brain permeable, as well as regulates the formation and presence of free radicals. Overall, we demonstrate that a rational structure-based design strategy can generate a small molecule that can target and modulate multiple factors, providing a new tool to uncover and address AD complexity.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/2014/jacsat.2014.136.issue-1/ja409801p/production/images/medium/ja-2013-09801p_0008.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/ja409801p'>ACS Electronic Supporting Info</A></P>