Sea urchin embryonic development provides a model for evaluating therapies against β-amyloid toxicity

2008 ◽  
Vol 75 (1) ◽  
pp. 94-100 ◽  
Author(s):  
Gennady A. Buznikov ◽  
Lyudmila A. Nikitina ◽  
Vladimir V. Bezuglov ◽  
Ivan Milošević ◽  
Lidija Lazarević ◽  
...  
Keyword(s):  
Embryonic Development ◽  
Sea Urchin ◽  
Amyloid Toxicity ◽  
Β Amyloid

scholarly journals Induction of phosphorylation of dolichol during embryonic development of the sea urchin.

1981 ◽  
Vol 256 (20) ◽  
pp. 10538-10542
Author(s):  
D.P. Rossignol ◽  
W.J. Lennarz ◽  
C.J. Waechter
Keyword(s):  
Embryonic Development ◽  
Sea Urchin

Kainate exacerbates β-amyloid toxicity in rat hippocampus

2003 ◽  
Vol 340 (3) ◽  
pp. 242-244 ◽  
Author(s):  
Kiyoshi Morimoto ◽  
Tomiichiro Oda
Keyword(s):  
Rat Hippocampus ◽  
Amyloid Toxicity ◽  
Β Amyloid

scholarly journals Liuwei Dihuang (LWDH), a Traditional Chinese Medicinal Formula, Protects against β-Amyloid Toxicity in Transgenic Caenorhabditis elegans

PLoS ONE ◽  
2012 ◽  
Vol 7 (8) ◽  
pp. e43990 ◽  
Author(s):  
Jatinder S. Sangha ◽  
Xiaoli Sun ◽  
Owen S. D. Wally ◽  
Kaibin Zhang ◽  
Xiuhong Ji ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Amyloid Toxicity ◽  
Β Amyloid

scholarly journals In vivo exposure to northern diatoms arrests sea urchin embryonic development

Toxicon ◽  
2016 ◽  
Vol 109 ◽  
pp. 63-69 ◽  
Author(s):  
Elena Gudimova ◽  
Hans C. Eilertsen ◽  
Trond Ø. Jørgensen ◽  
Espen Hansen
Keyword(s):  
Embryonic Development ◽  
Sea Urchin

Polypeptide composition and organization of the sea urchin extraembryonic hyaline layer

1990 ◽  
Vol 68 (9) ◽  
pp. 1083-1089 ◽  
Author(s):  
John J. Robinson
Keyword(s):  
Embryonic Development ◽  
Sea Urchin ◽  
Organization Development ◽  
Structural Organization ◽  
Protein Composition ◽  
Ruthenium Red ◽  
Proteinase K ◽  
Polypeptide Composition ◽  
Layer Composition ◽  
Precipitable Protein

The protein composition and organization of the sea urchin extraembryonic hyaline layer was examined. Hyalin and a polypeptide of 45 kilodaltons (kDa) were present in hyaline layers isolated from 1-h-old embryos through to the pluteus larva stage. In contrast, several polypeptide species ranging in size from 175 to 32 kDa either decreased in amount or disappeared from the layer as embryonic development proceeded. Concomitant with the changes in composition, hyaline layers became progressively more refractory to dissolution by washing in Ca2+, Mg2+-free seawater. Incubation of intact layers, isolated from 1-h-old embryos, with proteinase K resulted in the selective digestion of hyalin and was accompanied by release of the 45-kDa polypeptide from the layers. Washing intact layers in 20 mM Tris (pH 8.0) also resulted in the selective removal of hyalin and the 45-kDa polypeptide. The Ca2+-precipitable protein hyalin, alone among the hyaline layer polypeptides, bound the Ca2+-antagonist ruthenium red. These results suggest a structural organization within the hyaline layer that is both heterogenous and dynamic throughout embryonic development.Key words: hyaline layer, composition, organization, development.

scholarly journals Neutralization of TRAIL death pathway protects human neuronal cell line from β-amyloid toxicity

2003 ◽  
Vol 10 (1) ◽  
pp. 134-141 ◽  
Author(s):  
G Cantarella ◽  
D Uberti ◽  
T Carsana ◽  
G Lombardo ◽  
R Bernardini ◽  
...  
Keyword(s):  
Cell Line ◽  
Neuronal Cell ◽  
Neuronal Cell Line ◽  
Amyloid Toxicity ◽  
Human Neuronal Cell ◽  
Β Amyloid
Sign in / Sign up

Export Citation Format

Share Document