Preparation and Characterization of Posttranslationally Modified Tubulins From Artemia franciscana

2007 ◽  
pp. 45-63
Author(s):  
Paul A. O’Connell ◽  
Thomas H. MacRae
Keyword(s):  
Artemia Franciscana

scholarly journals Caspase activity during cell stasis: avoidance of apoptosis in an invertebrate extremophile, Artemia franciscana

2007 ◽  
Vol 292 (5) ◽  
pp. R2039-R2047 ◽  
Author(s):  
Michael A. Menze ◽  
Steven C. Hand
Keyword(s):  
Caspase 3 ◽  
Biochemical Characterization ◽  
Artemia Franciscana ◽  
Differential Sensitivity ◽  
Caspase Activity ◽  
Caspase 9 ◽  
Human Hepatoma Cells ◽  
Energy Limitation ◽  
Exogenous Calcium

Evaluation of apoptotic processes downstream of the mitochondrion reveals caspase-9- and low levels of caspase-3-like activities in partly purified extracts of Artemia franciscana embryos. However, in contrast to experiments with extracts of human hepatoma cells, cytochrome c fails to activate caspase-3 or -9 in extracts from A. franciscana. Furthermore, caspase-9 activity is sensitive to exogenous calcium. The addition of 5 mM calcium leads to a 4.86 ± 0.19 fold (SD) ( n = 3) increase in activity, which is fully prevented with 150 mM KCl. As with mammalian systems, high ATP (>1.25 mM) suppresses caspase activity in A. franciscana extracts. A strong inhibition of caspase-9 activity was also found by GTP. Comparison of GTP-induced inhibition of caspase-9 at 0 and 2.5 mM MgCl2 indicates that free (nonchelated) GTP is likely to be the inhibitory form. The strongest inhibition among all nucleotides tested was with ADP. Inhibition by ADP in the presence of Mg2+ is 60-fold greater in diapause embryos than in postdiapause embryos. Because ADP does not change appreciably in concentration between the two physiological states, it is likely that this differential sensitivity to Mg2+-ADP is important in avoiding caspase activation during diapause. Finally, mixtures of nucleotides that mimic physiological concentrations in postdiapause and diapause states underscore the depressive action of these regulators on caspase-9 during diapause. Our biochemical characterization of caspase-like activity in A. franciscana extracts reveals that multiple mechanisms are in place to reduce the probability of apoptosis under conditions of energy limitation in this embryo.

scholarly journals Knockdown of the small heat-shock protein p26 by RNA interference modifies the diapause proteome of Artemia franciscana

2019 ◽  
Vol 97 (4) ◽  
pp. 471-479
Author(s):  
Hajer Salem Malitan ◽  
Alejandro M. Cohen ◽  
Thomas H. MacRae
Keyword(s):  
Rna Interference ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Stress Tolerance ◽  
Small Heat Shock Protein ◽  
Isotopic Labeling ◽  
Artemia Franciscana ◽  
Signal Transducers ◽  
Translation Factors

Embryos of the crustacean Artemia franciscana may arrest as gastrulae, forming cysts that enter diapause, which is a state of reduced metabolism and enhanced stress tolerance. Diapausing cysts survive physiological stresses for years due, in part, to molecular chaperones. p26, a small heat-shock protein, is an abundant diapause-specific molecular chaperone in cysts, and it affects embryo development and stress tolerance. p26 is therefore thought to influence many proteins in cysts, and this study was undertaken to determine how the loss of p26 by RNA interference (RNAi) affects the diapause proteome of A. franciscana. The proteome was analyzed by shot-gun proteomics coupled to differential isotopic labeling and tandem mass spectrometry. Proteins in the diapause proteome included metabolic enzymes, antioxidants, binding proteins, structural proteins, transporters, translation factors, receptors, and signal transducers. Proteins within the diapause proteome either disappeared or were reduced in amount when p26 was knocked down, or conversely, proteins appeared or increased in amount. Those proteins that disappeared may be p26 substrates, whereas the synthesis of those proteins that appeared or increased may be regulated by p26. This study provides the first global characterization of the diapause proteome of A. franciscana and demonstrates that the sHsp p26 influences proteome composition.

Biochemical Studies on Sphingolipid of Artemia franciscana (I) Isolation and Characterization of Sphingomyelin

Lipids ◽  
2010 ◽  
Vol 45 (7) ◽  
pp. 635-643 ◽  
Author(s):  
Hisao Kojima ◽  
Takashi Inoue ◽  
Mutsumi Sugita ◽  
Saki Itonori ◽  
Masahiro Ito
Keyword(s):  
Artemia Franciscana ◽  
Isolation And Characterization ◽  
Biochemical Studies

Further evidence and characterization of Artemia franciscana (Kellogg, 1906) populations in Argentina

2004 ◽  
Vol 31 (11) ◽  
pp. 1735-1749 ◽  
Author(s):  
Francisco Amat ◽  
Rosa Graciela Cohen ◽  
Francisco Hontoria ◽  
Juan Carlos Navarro
Keyword(s):  
Artemia Franciscana

scholarly journals Purification and characterization of a proteolytic active fragment of DNA topoisomerase I from the brine shrimp Artemia franciscana (Crustacea Anostraca)

1992 ◽  
Vol 282 (1) ◽  
pp. 249-254 ◽  
Author(s):  
G Badaracco ◽  
N Landsberger ◽  
R Benfante
Keyword(s):  
Molecular Mass ◽  
Topoisomerase I ◽  
Specific Inhibitor ◽  
Artemia Franciscana ◽  
Type I ◽  
Bivalent Cation ◽  
Dna Topoisomerase ◽  
Proteolytic Fragment ◽  
Dna Complex

The ATP-independent type I topoisomerase from the crustacean Artemia franciscana was purified to near-homogeneity. Its activity was measured by an assay that uses the formation of an enzyme-cleaved DNA complex in the presence of the specific inhibitor camptothecin. The purification procedure is reported. Purified topoisomerase is a single-subunit enzyme with a molecular mass of 63 kDa. Immunoblot performed on the different steps of purification shows that the purified 63 kDa peptide is a proteolytic fragment of a protein with a molecular mass of 110 kDa. Similarly to the other purified eukaryotic topoisomerases, the crustacean enzyme does not require a bivalent cation for activity, but is stimulated in the presence of 10 mM-MgCl2; moreover, it can relax both negative and positive superhelical turns. The enzyme activity is strongly inhibited by the antitumour drug camptothecin. The enzyme inhibition is related to the stabilization of the cleavable complex between topoisomerase I and DNA.

scholarly journals Molecular characterization of artemin and ferritin from Artemia franciscana

2002 ◽  
Vol 270 (1) ◽  
pp. 137-145 ◽  
Author(s):  
Tao Chen ◽  
Reinout Amons ◽  
James S. Clegg ◽  
Alden H. Warner ◽  
Thomas H. MacRae
Keyword(s):  
Molecular Characterization ◽  
Artemia Franciscana

Characterization of the microtubule proteome during post-diapause development of Artemia franciscana

2006 ◽  
Vol 1764 (5) ◽  
pp. 920-928 ◽  
Author(s):  
Paul A. O'Connell ◽  
Devanand M. Pinto ◽  
Ken A. Chisholm ◽  
Thomas H. MacRae
Keyword(s):  
Artemia Franciscana ◽  
Diapause Development

scholarly journals Effect of bacterial probiotics bio encapsulated into Artemia franciscana on weight and length of the shortfin silverside (Chirostoma humboldtianum), and PCR DGGE characterization of its intestinal bacterial community

2017 ◽  
Vol 45 (5) ◽  
pp. 1031-1043 ◽  
Author(s):  
Gabriela Vazquez Silva ◽  
Hugo Ramirez Saad ◽  
Jose Aguirre Garrido ◽  
Lino Mayorga Reyes ◽  
Alejandro Azaola Espinosa ◽  
...  
Keyword(s):  
Bacterial Community ◽  
Artemia Franciscana ◽  
Intestinal Bacterial Community
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