Disease relevance of Paracentrotus

• Toxicity of tributyltin and triphenyltin to early life-stages of Paracentrotus lividus (Echinodermata: Echinoidea) [1].

High impact information on Paracentrotus

• DNA was extracted from Paracentrotus lividus embryos at the third S phase afer fertilization and analyzed with the electron microscope [2].
• Here, we report the cloning of an orthopedia (Otp)-related gene from Paracentrotus lividus, PlOtp [3].
• After proteolytic digestion of sperm tubulin from sea urchin Paracentrotus lividus, C-terminal peptides were isolated by chromatographic separations [4].
• Pl-nectin is an ECM protein located on the apical surface of ectoderm cells of Paracentrotus lividus sea urchin embryo [5].
• We have investigated the possibility of obtaining the same morphological effect as with lithium by utilizing Fabs against the maternal Bep4 protein that is localized in the animal part of Paracentrotus lividus egg and embryos [6].

Chemical compound and disease context of Paracentrotus

• The present study was undertaken to evaluate the toxicity of aluminum sulfate, ferric chloride and their 1:1 mixture (Mix) on early development, fertilization and offspring quality in three sea urchins species (Sphaerechinus granularis, Paracentrotus lividus, Psammechinus microtuberculatus) and in mussels (Mytilus galloprovincialis) [7].

Biological context of Paracentrotus

• Analysis of the genome structure of the Paracentrotus lividus (sea urchin) DNA methyltransferase (DNA MTase) gene showed the presence of an open reading frame, named METEX, in intron 7 of the gene [8].
• The turnover and localization of the enzyme DNA (cytosine-5) methyltransferase (Dnmt1) were studied during Paracentrotus lividus sea urchin embryo development using antibody preparations against the NH(2) and COOH-terminal regions of the molecule [9].
• A 2935-bp cDNA clone encoding glutamine synthetase (GS) was isolated from a cDNA library prepared from four-blastomere Paracentrotus lividus sea urchin embryos [10].
• Eggs of Paracentrotus exposed to 1 mM 2,4-dinitrophenol (DNP) in sea water at 10-min intervals from 10 to 40 min after insemination and returned to normal sea water 60 min later, divide into two cells [11].
• We have isolated and characterized a cDNA clone corresponding to a new member of bep (butanol, extracted, proteins) Paracentrotus lividus multigene family coding for cell surface proteins [12].

Anatomical context of Paracentrotus

• Paracentrotus lividus unfertilized eggs were centrifuged in a sucrose gradient, so to split each into two parts: a nucleated light fragment and an anucleated heavy fragment [13].
• The existence of a response to acetylcholine (ACh) and cholinomimetic drugs in sea urchin eggs and zygotes was investigated in two sea urchin species: Paracentrotus lividus and Lytechinus pictus [14].
• We have identified and partially characterised two antigens, extracted with 3% butanol, from Paracentrotus lividus embryos dissociated at the blastula stage, and encoded by the cDNA clones previously described as bep1 and bep4 (bep-butanol extracted proteins) [15].
• Unfertilized Paracentrotus lividus egg cytoskeleton is prepared by mild, nonionic detergent extraction at 4 degrees C in buffer systems containing either 2-methyl-2,4-pentanediol (hexylene glycol) or glycerol [16].
• The aim of this work was to chemically characterize the different PTM occurring in the C-terminal tail of axonemal tubulin purified from sea urchin, Paracentrotus lividus, spermatozoa [17].

Associations of Paracentrotus with chemical compounds

• Treatment of Paracentrotus lividus embryos with lithium, which is known to block the polyphosphoinositide (PPI) cycle, induces their development into vegetalized larvae [18].
• An increase in the amount of cytoplasmic filamentous structures (cytoplasmic matrix and aster) which were recovered after hexylene glycol/Triton X-100 treatment of sea urchin eggs (Paracentrotus lividus) activated by 0.2-2.5 mM procaine was observed [19].
• Intracellular pH (pHi) of sea urchin eggs (Paracentrotus lividus) was determined using DMO (dimethyloxazolidinedione) and a rapid filtration technique (P. Payan, J.P. Girard, R. Christen and C. Sardet (1981). Exp. Cell Res. 134, 339-344) [20].
• The cytochrome b of the sea urchin Paracentrotus lividus is naturally resistant to myxothiazol and mucidin [21].
• Two cDNA clones related to Paracentrotus lividus butanol-extracted proteins, presumably belonging to cell surface proteins, were isolated by a lambda gt11 expression library of ovary poly A+ RNA [22].

Gene context of Paracentrotus

• Seawi is a major component of microtubule-ribonucleoprotein (MT-RNP) complexes isolated from two different species of sea urchin, Strongylocentrotus purpuratus and Paracentrotus lividus [23].
• Three skeletal tissues of the adult echinoid Paracentrotus lividus (the pedicellaria primordium, the test, and the tooth) were immunolabeled with three sera raised against the total mineralization organic matrix and two specific matrix proteins (SM30 and SM50) from the embryo of the echinoid Strongylocentrotus purpuratus [24].
• Marisa cornuarietis (Mollusc), Hyalella azteca (Crustacean), and Paracentrotus lividus (Echinoderm) demonstrated the ability to metabolize androgens through different pathways catalyzed by 5alpha-reductases (5alpha-R), hydroxysteroid dehydrogenases (HSD), hydroxylases, sulfotransferases (SULT), and fatty-acid acyl-CoA acyltransferases (ATAT) [25].
• The protein displays a very high similarity with the Paracentrotus lividus homologue as it contains also the two leucine zipper-like domains which are thought to be involved in intramolecular interactions needed to expose the two DNA binding domains in the correct position for contacting DNA [26].
• It is demonstrated by DNA electrophoresis analysis, morphological observations and TdT in situ reaction, that Paracentrotus embryos if treated with TPA plus heat undergo an apoptotic reaction [27].

Analytical, diagnostic and therapeutic context of Paracentrotus

• We have used Northern blot and whole-mount in situ hybridizations to analyze the temporal and spatial expression pattern of the Pl alpha 2 alpha-tubulin gene in Paracentrotus lividus sea urchin embryos [28].
• Simultaneous determination of thiamin and riboflavin in the sea urchin, Paracentrotus lividus, by high-performance liquid chromatography [29].

References