A Proteomics Analysis of Rat Liver Membrane Skeletons: The Investigation of Actin- and Cytokeratin-Based Protein Components

2010 ◽  
Vol 9 (1) ◽  
pp. 22-29 ◽  
Author(s):  
Qingsong Wang ◽  
Jintang He ◽  
Lingyao Meng ◽  
Yashu Liu ◽  
Hai Pu ◽  
...  
Keyword(s):  
Rat Liver ◽  
Proteomics Analysis ◽  
Liver Membrane ◽  
Protein Components ◽  
Membrane Skeletons

scholarly journals Partial Purification of LDL Receptor of Rat Liver Membrane

1985 ◽  
Vol 13 (1) ◽  
pp. 123-126
Author(s):  
Makoto KINOSHITA ◽  
Tamio TERAMOTO ◽  
Hirokazu KATO ◽  
Yoshiaki HASHIMOTO ◽  
Hiroshi OKA
Keyword(s):  
Rat Liver ◽  
Ldl Receptor ◽  
Partial Purification ◽  
Liver Membrane

Effect of HDL1 infusion on biliary secretion in perfused rat liver

1992 ◽  
Vol 12 (5) ◽  
pp. 425-432 ◽  
Author(s):  
Roberto Rivabene ◽  
Alfredo Cantafora ◽  
Chong Chao Yan ◽  
Flavia Castellano ◽  
Giovannella Bruscalupi ◽  
...  
Keyword(s):  
Rat Liver ◽  
In Vitro Model ◽  
Significant Rise ◽  
Molar Ratio ◽  
Strong Increase ◽  
Perfused Rat Liver ◽  
Biliary Lipid ◽  
Liver Membrane ◽  
Vitro Model

The effects of HDL1 lipoprotein infusion on biliary lipid secretion were studied in the in vitro model of rat perfused liver. A strong increase in bile flow was observed during and after lipoprotein infusion. This caused a significant rise in cholesterol, phospholipid and bile salt secretions. However, only the percentage of cholesterol increased with respect to the other bile lipids. The changes observed in the cholesterol/phospholipid molar ratio values of liver membrane subfractions (i.e., liver plasma membrane, mitochondria plus lysosomes and microsomes) isolated from the perfused rat liver after HDL1 administration were not significant.

SPECIFIC BINDING OF [3H]OESTRADIOL BY CYTOPLASMIC PROTEIN COMPONENTS OF FEMALE RAT LIVER

1976 ◽  
Vol 69 (1) ◽  
pp. 167-168 ◽  
Author(s):  
WENDY POWELL-JONES ◽  
PETER DAVIES ◽  
KEITH GRIFFITHS
Keyword(s):  
Rat Liver ◽  
Specific Binding ◽  
Female Rat ◽  
Cytoplasmic Protein ◽  
Protein Components

scholarly journals Substrate-specificity of glutamine transporters in membrane vesicles from rat liver and skeletal muscle investigated using amino acid analogues

1991 ◽  
Vol 278 (1) ◽  
pp. 105-111 ◽  
Author(s):  
S Y Low ◽  
P M Taylor ◽  
A Ahmed ◽  
C I Pogson ◽  
M J Rennie
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Rat Liver ◽  
Membrane Vesicles ◽  
Transport Processes ◽  
System A ◽  
Liver Membrane ◽  
Glutamine Transport ◽  
Fold Excess ◽  
Glutamine Uptake

We investigated the effects of glutamine and histidine analogues on glutamine transport processes in membrane vesicles prepared from rat liver (sinusoidal membrane) and skeletal muscle (sarcolemma). L-[14C]Glutamine is transported in these membranes predominantly by Systems N/Nm (liver and muscle respectively), and to a lesser extent by Systems A and L (e.g. about 60, 20 and 20% of total flux respectively via Systems N, A and L at 0.05 mM-glutamine in liver membrane vesicles). The glutamine anti-metabolites 6-diazo-5-oxo-L-norleucine and acivicin were relatively poor inhibitors of glutamine uptake into liver membrane vesicles (less than 25% inhibition at 20-fold excess) and appeared primarily to inhibit System A activity (i.e. N-methylaminoisobutyric acid-inhibitable glutamine uptake). In similar experiments azaserine (also a glutamine anti-metabolite) inhibited approx. 50% of glutamine uptake, apparently by inhibition of System A and also of System L (i.e. 2-amino-2-carboxybicyclo[2,2,1]heptane-inhibitable glutamine uptake). Glutamate gamma-hydroxamate, aspartate beta-hydroxamate, histidine and N'-methylhistidine were all strong inhibitors of glutamine uptake into liver membrane vesicles (greater than 65% inhibition at 20-fold excess), but neither homoglutamine nor N'-methylhistidine produced inhibition. L-Glutamate-gamma-hydroxamate was shown to be a competitive inhibitor of glutamine transport via System N (Ki approximately 0.6 mM). Glutamine uptake in sarcolemmal vesicles showed a similar general pattern of inhibition as in liver membrane vesicles. The results highlight limits on the substrate tolerance of System N; we suggest that the presence of both an L-alpha-amino acid group and a nitrogen group with a delocalized lone-pair of electrons (amide or pyrrole type), separated by a specific intramolecular distance (C2-C4 chain equivalent), is important for substrate recognition by this transporter.

scholarly journals Proteomics Analysis of Exosomes From Patients With Active Tuberculosis Reveals Infection Profiles and Potential Biomarkers

2022 ◽  
Vol 12 ◽  
Author(s):  
Min Zhang ◽  
Yiping Xie ◽  
Shasha Li ◽  
Xiaojian Ye ◽  
Yibiao Jiang ◽  
...  
Keyword(s):  
Western Blotting ◽  
Mononuclear Cells ◽  
Label Free ◽  
Proteomics Analysis ◽  
Peripheral Blood Mononuclear ◽  
Mhc I ◽  
Normal Individuals ◽  
Protein Components ◽  
Serum Exosomes ◽  
Potential Biomarkers

Although mycobacterial proteins in exosomes from peripheral serum of patients with tuberculosis (TB) have been identified, other exact compositions of exosomes remain unknown. In the present study, a comprehensive proteomics analysis of serum exosomes derived from patients with active TB (ATB) was performed. Exosomes from patients with ATB were characterized using nanoparticle tracking analysis (NTA), transmission electron microscopy (TEM), and western blotting analysis. Then identified protein components were quantified by label-free proteomics and were determined via bioinformatics analysis. A total of 123 differential proteins were identified in ATB serum exosomes and analyzed with Gene Ontology (GO) analysis. Among these proteins heat shock protein70 (HSP70), CD81, major histocompatibility complex-I (MHC-I ) and tumor susceptibility gene101 (TSG101) were present in exosomes of ATB and normal individuals confirmed via western blotting. In addition, among identified exosomal proteins lipopolysaccharide binding protein (LBP) increased significantly, but CD36 and MHC-I decreased significantly in ATB exosomes. Meanwhile, MHC-I was down-expressed in serum and peripheral blood mononuclear cells (PBMCs) of ATB, but interestingly CD36 was down-regulated in serum and up-expressed in PBMCs of ATB patients validated with ELISA and flow cytometry. CD36 was up-regulated by M. tuberculosis H37Ra infection in macrophages and suppressed in exosomes from H37Ra infected macrophages detected by western blotting. This study provided a comprehensive description of the exosome proteome in the serum of patients with ATB and revealed certain potential biomarkers associated with TB infection.

Oxytocin and vasopressin analogues capable of competition with vasopressin binding to rat liver membranes

1983 ◽  
Vol 48 (6) ◽  
pp. 1788-1795
Author(s):  
Tomislav Barth ◽  
Bernard Cantau ◽  
Daniel Butlen ◽  
Gilles Guillon ◽  
Serge Jard ◽  
...  
Keyword(s):  
Rat Liver ◽  
Membrane System ◽  
Membrane Receptor ◽  
Peptide Chain ◽  
Liver Membrane ◽  
Liver Membranes ◽  
Vasopressin Analogues ◽  
Good Agreement

A number of vasopressin and oxytocin analogues modified in positions 1, 2, 4, 6 and 9 of the peptide chain were tested regarding their affinity to the rat liver membrane receptor. The affinities were estimated from the ability of the analogues to compete with the binding of tritiated vasopressin to rat liver membranes. In the series of vasopressin agonists, the degree of competition was in good agreement with the corresponding pressor activities. In the case of inhibitors of vasopressin pressor action, binding to the membrane system was also observed.

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