Effects of Neem Flowers, Thai and Chinese Bitter Gourd Fruits and Sweet Basil Leaves on Hepatic Monooxygenases and Glutathione S-transferase Activities, and In Vitro Metabolic Activation of Chemical Carcinogens in Rats

1998 ◽  
Vol 36 (6) ◽  
pp. 475-484 ◽  
Author(s):  
W.R Kusamran ◽  
A Ratanavila ◽  
A Tepsuwan
1970 ◽  
Vol 7 (1) ◽  
pp. 57-61 ◽  
Author(s):  
MR Amin ◽  
M Mostofa ◽  
ME Hoque ◽  
MA Sayed

The prevalence of natural gastrointestinal nematodes was observed in cattle during the period from June, 2004 to May, 2005 in Sadar upazila of Mymensingh district. The prevalence of gastrointestinal nematodes was 84.1% (rainy seasons-97%, summer-85.5% and winter seasons-69.8%). The prevalence of strongyles (Haemonchus sp., Trichostrongylus sp., Oesophagostomum sp. and Mecistocirrus sp.), Bunostomum sp., Strongyloides sp., Trichuris sp. and Capillaria sp. were 63.9%, 26.3%, 21.5%, 17.3% and 24.5%, respectively. Water extracts of 20 indigenous plants(neem, tobacco plant, barbados lilac, betel leaf, pineapple, jute, turmeric, garlic, devil's tree, papaya, lime tree, dodder, white teak, conessi tree, bitter gourd, sweet basil, white verticillia, pomegranate, sage, chaste tree) showed potential in vitro activities against adult parasites. Out of these, 20 plant extracts, 10 plants (neem, tobacco, barbados lilac, betel leaf, pineapple, jute, turmeric, garlic, dodder and bitter gourd) showed 100% efficacy against adult worms, 4 plants (devil's tree, papaya, white verticillia and chaste tree) showed 90-98% and others (lime tree, white teak, conessi tree, sweet basil, pomegranate and sage) showed below 90%. Keywords: Anthelmintic; Gastrointestinal nematodes; In vitro; Prevalence; Medicinal plants DOI: 10.3329/jbau.v7i1.4799 J. Bangladesh Agril. Univ. 7(1): 57-61, 2009


2015 ◽  
Vol 2 (1-4) ◽  
pp. 24-27 ◽  

Hypericin is a pigment present in the widely distributed medicinal plant Hypericum perforatum L. (Hypericaceae). In our research, hypericin was found to be an inhibitor of NADPH/Fe2+ induced microsomal lipid peroxidation and NADPH-dependent lucigenin chemiluminescence emission in vitro. Hypericin also inhibited the microsomal CYP1Adependent 7-ethoxyresorufin O-deethylase (EROD) which participates in the metabolic activation of xenobiotics including chemical carcinogens.


2001 ◽  
Vol 355 (3) ◽  
pp. 663-670 ◽  
Author(s):  
Claudia TROST ◽  
Christiane BERGS ◽  
Nina HIMMERKUS ◽  
Veit FLOCKERZI

The mammalian gene products, transient receptor potential (trp)1 to trp7, are related to the Drosophila TRP and TRP-like ion channels, and are candidate proteins underlying agonist-activated Ca2+-permeable ion channels. Recently, the TRP4 protein has been shown to be part of native store-operated Ca2+-permeable channels. These channels, most likely, are composed of other proteins in addition to TRP4. In the present paper we report the direct interaction of TRP4 and calmodulin (CaM) by: (1) retention of in vitro translated TRP4 and of TRP4 protein solubilized from bovine adrenal cortex by CaM–Sepharose in the presence of Ca2+, and (2) TRP4–glutathione S-transferase pull-down experiments. Two domains of TRP4, amino acid residues 688–759 and 786–848, were identified as being able to interact with CaM. The binding of CaM to both domains occurred only in the presence of Ca2+ concentrations above 10µM, with half maximal binding occurring at 16.6µM (domain 1) and 27.9µM Ca2+ (domain 2). Synthetic peptides, encompassing the two putative CaM binding sites within these domains and covering amino acid residues 694–728 and 829–853, interacted directly with dansyl–CaM with apparent Kd values of 94–189nM. These results indicate that TRP4/Ca2+-CaM are parts of a signalling complex involved in agonist-induced Ca2+ entry.


1977 ◽  
Vol 36 (1) ◽  
pp. 65-71 ◽  
Author(s):  
D Papadopoulo ◽  
S Levy ◽  
L Chamaillard ◽  
O Beesau ◽  
M Hubert-Harbart ◽  
...  
Keyword(s):  

2009 ◽  
Vol 23 (2) ◽  
pp. 169-175 ◽  
Author(s):  
Kenichi Miyako ◽  
Laura J. Cobb ◽  
Malik Francis ◽  
Alden Huang ◽  
Bonnie Peng ◽  
...  

Abstract IGF-binding proteins (IGFBPs) have multiple cellular effects, which occur by both IGF-dependent and -independent mechanisms. IGFBP-2 is involved in the regulation of both normal and carcinogenic cell growth. To further understand the actions of IGFBP-2, we carried out a yeast two-hybrid screen to search for intracellular partner proteins using a human prostate cDNA library. We isolated Pim-1-associated protein-1 (PAP-1)-associated protein-1 (PAPA-1) as an IGFBP-2-binding protein, whose expression and subcellular localization is regulated by both IGFBP-2 and androgens. Coimmunoprecipitation and glutathione S-transferase pull-down assay confirmed the interaction in vitro, and confocal microscopy showed the colocalization of IGFBP-2 and PAPA-1 in the nucleus. Suppression of PAPA-1 by small interfering RNA treatment enhanced the growth-promoting effect of IGFBP-2. Conversely, IGFBP-2-promoted bromodeoxyuridine incorporation into LNCaP cells was abrogated by the simultaneous overexpression of myc-hPAPA-1. Mouse embryonic fibroblasts from IGFBP-2 knockout mouse showed diminished growth activity compared with wild type, and expression of FLAG-mPAPA-1 decreased cell proliferation in IGFBP-2 knockout, but not control mouse embryonic fibroblasts. These studies suggest that the growth-promoting role of IGFBP-2 in prostate cancer is inhibited by its intracellular interaction with PAPA-1.


2009 ◽  
Vol 105 (4) ◽  
pp. 1179-1182 ◽  
Author(s):  
Lakshmy Srinivasan ◽  
Nisha Mathew ◽  
Kalyanasundaram Muthuswamy

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