scholarly journals Re-adaption on Earth after Spaceflights Affects the Mouse Liver Proteome

2017 ◽  
Vol 18 (8) ◽  
pp. 1763 ◽  
Author(s):  
Viktoria Anselm ◽  
Svetlana Novikova ◽  
Victor Zgoda
Keyword(s):  
Mouse Liver ◽  
Liver Proteome

Analysis of the Mouse Liver Proteome Using Advanced Mass Spectrometry

2007 ◽  
Vol 6 (8) ◽  
pp. 2963-2972 ◽  
Author(s):  
Rong Shi ◽  
Chanchal Kumar ◽  
Alexandre Zougman ◽  
Yanling Zhang ◽  
Alexandre Podtelejnikov ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Mouse Liver ◽  
Liver Proteome

scholarly journals Subacute calorie restriction and rapamycin discordantly alter mouse liver proteome homeostasis and reverse aging effects

Aging Cell ◽  
2015 ◽  
Vol 14 (4) ◽  
pp. 547-557 ◽  
Author(s):  
Pabalu P. Karunadharma ◽  
Nathan Basisty ◽  
Dao‐Fu Dai ◽  
Ying A. Chiao ◽  
Ellen K. Quarles ◽  
...  
Keyword(s):  
Calorie Restriction ◽  
Mouse Liver ◽  
Aging Effects ◽  
Liver Proteome

Global cPILOT analysis of the APP/PS-1 mouse liver proteome

2015 ◽  
Vol 9 (9-10) ◽  
pp. 872-884 ◽  
Author(s):  
Adam R. Evans ◽  
Liqing Gu ◽  
Rodolfo Guerrero ◽  
Renã A. S. Robinson
Keyword(s):  
Mouse Liver ◽  
Liver Proteome

scholarly journals An update on the mouse liver proteome

2009 ◽  
Vol 7 (1) ◽  
pp. 35 ◽  
Author(s):  
Giuseppe Gazzana ◽  
Jürgen Borlak
Keyword(s):  
Mouse Liver ◽  
Liver Proteome

scholarly journals Nutritional reprogramming of mouse liver proteome is dampened by metformin, resveratrol, and rapamycin

2021 ◽  
Author(s):  
David G. Le Couteur ◽  
Samantha M. Solon-Biet ◽  
Benjamin L. Parker ◽  
Tamara Pulpitel ◽  
Amanda E. Brandon ◽  
...  
Keyword(s):  
Mouse Liver ◽  
Liver Proteome

Ultrastructural localization of specific nucleoprotein fractions

1978 ◽  
Vol 36 (2) ◽  
pp. 204-205
Author(s):  
G. L. Brown
Keyword(s):  
Gel Electrophoresis ◽  
Mouse Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ultrastructural Localization ◽  
Polyacrylamide Gel ◽  
Acid Extraction ◽  
Acid Solutions ◽  
Low Salt ◽  
Liver Nuclei ◽  
Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

Site of Lysosome Production During Hepatic Injury

1969 ◽  
Vol 27 ◽  
pp. 348-349
Author(s):  
Nalin J. Unakar
Keyword(s):  
Electron Microscopy ◽  
Golgi Apparatus ◽  
Mouse Liver ◽  
Hepatic Injury ◽  
Close Approximation ◽  
Experimental Conditions ◽  
Toxic Injury

The increased number of lysosomes as well as the close approximation of lysosomes to the Golgi apparatus in tissue under variety of experimental conditions is commonly observed. These observations suggest Golgi involvement in lysosomal production. The role of the Golgi apparatus in the production of lysosomes in mouse liver was studied by electron microscopy of liver following toxic injury by CCI4.

Nuclear coiled bodies and the nucleolus

1994 ◽  
Vol 52 ◽  
pp. 20-21
Author(s):  
K. Brasch ◽  
J. Williams ◽  
D. Gallo ◽  
T. Lee ◽  
R. L. Ochs
Keyword(s):  
Mouse Liver ◽  
Nuclear Body ◽  
Nuclear Bodies ◽  
Model Systems ◽  
Coiled Body ◽  
Rrna Processing ◽  
Malignant Cells ◽  
Sm Proteins ◽  
Coiled Bodies ◽  
Unique Protein

Though first described in 1903 by Ramon-y-Cajal as silver-staining “accessory bodies” to nucleoli, nuclear bodies were subsequently rediscovered by electron microscopy about 30 years ago. Nuclear bodies are ubiquitous, but seem most abundant in hyperactive and malignant cells. The best studied type of nuclear body is the coiled body (CB), so termed due to characteristic morphology and content of a unique protein, p80-coilin (Fig.1). While no specific functions have as yet been assigned to CBs, they contain spliceosome snRNAs and proteins, and also the nucleolar protein fibrillarin. In addition, there is mounting evidence that CBs arise from or are generated near the nucleolus and then migrate into the nucleoplasm. This suggests that as yet undefined links may exist, between nucleolar pre-rRNA processing events and the spliceosome-associated Sm proteins in CBs.We are examining CB and nucleolar changes in three diverse model systems: (1) estrogen stimulated chick liver, (2) normal and neoplastic cells, and (3) polyploid mouse liver.

RAGE is required for oval cell activation and inflammation-associated mouse liver carcinogenesis

2012 ◽  
Vol 50 (01) ◽  
Author(s):  
T Pusterla ◽  
J Németh ◽  
I Stein ◽  
L Wiechert ◽  
D Knigin ◽  
...  
Keyword(s):  
Mouse Liver ◽  
Cell Activation ◽  
Oval Cell ◽  
Liver Carcinogenesis
Sign in / Sign up

Export Citation Format

Share Document