Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin

Increasing the plasma phenylalanine concentration to levels as high as 0.560-0.870 mM (over ten times normal levels) had no detectable effect on the rate of brain protein synthesis in adult rats. The average rates for 7-week-old rats were: valine, 0.58 +/- 0.05%/h, phenylalanine, 0.59 +/- 0.06%/h, and tyrosine, 0.60 +/- 0.09%/h, or 0.59 +/- 0.06%/h overall. Synthesis rates calculated on the basis of the specific activity of the tRNA-bound amino acid were slightly lower (4% lower for phenylalanine) than those based on the brain free amino acid pool. Similarly, the specific activities of valine and phenylalanine in microdialysis fluid from striatum were practically the same as those in the brain free amino acid pool. Thus the specific activities of the valine and phenylalanine brain free pools are good measures of the precursor specific activity for protein synthesis. In any event, synthesis rates, whether based on the specific activities of the amino acids in the brain free pool or those bound to tRNA, were unaffected by elevated levels of plasma phenylalanine. Brain protein synthesis rates measured after the administration of quite large doses of phenylalanine (> 1.5 mumol/g) or valine (15 mumol/g) were in agreement (0.62 +/- 0.01 and 0.65 +/- 0.01%/h respectively) with the rates determined with infusions of trace amounts of amino acids. Thus the technique of stabilizing precursor-specific activity, and pushing values in the brain close to those of the plasma, by the administration of large quantities of precursor, appears to be valid.

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Changes in the brain protein levels following administration of kainic acid

Electrophoresis ◽

10.1002/1522-2683(200106)22:10<2086::aid-elps2086>3.0.co;2-4 ◽

2001 ◽

Vol 22 (10) ◽

pp. 2086-2091 ◽

Cited By ~ 26

Author(s):

Kurt Krapfenbauer ◽

Michael Berger ◽

Gert Lubec ◽

Michael Fountoulakis

Keyword(s):

Kainic Acid ◽

Brain Protein ◽

Protein Levels ◽

The Brain

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Galectin-1 Modulates Human Glioblastoma Cell Migration into the Brain Through Modifications to the Actin Cytoskeleton and Levels of Expression of Small GTPases

Journal of Neuropathology & Experimental Neurology ◽

10.1093/jnen/61.7.585 ◽

2002 ◽

Vol 61 (7) ◽

pp. 585-596 ◽

Cited By ~ 127

Author(s):

Isabelle Camby ◽

Nathalie Belot ◽

Florence Lefranc ◽

Niloufar Sadeghi ◽

Yvan de Launoit ◽

...

Keyword(s):

Cell Migration ◽

Actin Cytoskeleton ◽

Small Gtpases ◽

Glioblastoma Cell ◽

Human Glioblastoma ◽

Human Glioblastoma Cell ◽

The Brain

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Dynamic changes in the brain protein interaction network correlates with progression of Aβ42 pathology in Drosophila

Scientific Reports ◽

10.1038/s41598-020-74748-9 ◽

2020 ◽

Vol 10 (1) ◽

Author(s):

Harry M. Scholes ◽

Adam Cryar ◽

Fiona Kerr ◽

David Sutherland ◽

Lee A. Gethings ◽

...

Keyword(s):

Protein Interaction ◽

Protein Interaction Network ◽

Neuronal Damage ◽

Interaction Network ◽

The Arctic ◽

Model Organisms ◽

Brain Protein ◽

Amyloid Toxicity ◽

Network Analyses ◽

The Brain

Abstract Alzheimer’s disease (AD), the most prevalent form of dementia, is a progressive and devastating neurodegenerative condition for which there are no effective treatments. Understanding the molecular pathology of AD during disease progression may identify new ways to reduce neuronal damage. Here, we present a longitudinal study tracking dynamic proteomic alterations in the brains of an inducible Drosophila melanogaster model of AD expressing the Arctic mutant Aβ42 gene. We identified 3093 proteins from flies that were induced to express Aβ42 and age-matched healthy controls using label-free quantitative ion-mobility data independent analysis mass spectrometry. Of these, 228 proteins were significantly altered by Aβ42 accumulation and were enriched for AD-associated processes. Network analyses further revealed that these proteins have distinct hub and bottleneck properties in the brain protein interaction network, suggesting that several may have significant effects on brain function. Our unbiased analysis provides useful insights into the key processes governing the progression of amyloid toxicity and forms a basis for further functional analyses in model organisms and translation to mammalian systems.

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Amount of 14C Assimilated in Different Organs and Tissues of the Rat After a Single Injection of [U-14C]glucose

Canadian Journal of Biochemistry ◽

10.1139/o73-011 ◽

1973 ◽

Vol 51 (1) ◽

pp. 93-100 ◽

Cited By ~ 2

Author(s):

R. Vrba ◽

Anna Winter

Keyword(s):

Skeletal Muscles ◽

Alimentary Tract ◽

Single Injection ◽

Lipid Fraction ◽

Protein Fractions ◽

Brain Protein ◽

Immunological Responses ◽

Glucose Carbon ◽

Lipid Fractions ◽

The Brain

Labelling of proteins and lipids of 20 organs and tissues of the rat was studied 4 h after subcutaneous injection of D(+)-[U-14C]glucose. Gross differences between the rate of labelling of acid-insoluble constituents of various organs were noted; specific radioactivities of protein fractions obtained from the pancreas, plasma, ileojejunal segment of the alimentary tract, thymus, and spleen were equal to or higher than those of the brain protein fraction. This indicates that, apart from the brain, the high rates of assimilation of glucose carbon occur at anatomical sites of release of proteins, of rapid cell proliferation, or of immunological responses. In comparison with the above-mentioned organs, the rate of incorporation of glucose carbon into protein fractions of the heart, skeletal muscles, and formed elements of blood was low. In all organs and tissues investigated significantly more glucose carbon was incorporated into protein fractions than into lipid fractions, with the exception of adipose tissue, where glucose carbon was incorporated mainly into the lipid fraction.

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