scholarly journals Subcellular localization of DNA-binding protein BA by immunofluorescence and immunoelectron microscopy

1979 ◽  
Vol 83 (2) ◽  
pp. 462-463 ◽  
Author(s):  
JJ Catino ◽  
H Busch ◽  
Y Daskal ◽  
LC Yeoman
Keyword(s):  
Immunoelectron Microscopy ◽  
Rat Liver ◽  
Human Lymphocytes ◽  
Chromosomal Protein ◽  
Nonhistone Protein ◽  
Quiescent Cells ◽  
Normal Rat ◽  
Normal Human ◽  
Antigen Localization ◽  
Relationship Of

Nonhistone protein BA has been shown to decrease in amount in the chromatin of growth- stimulated normal rat liver (Yeoman et al. 1975. Cancer Res. 35:1249-1255) and in mitogen-stimulated normal human lymphocytes (Yeoman et al. 1976. Exp. Cell Res. 100:47- 55.). Subsequently, protein BA was purified and was shown to prefer to bind to double- stranded A-T-rich DNAs (Catino et al. 1978. Biochemistry. 17:983-987.). Immunization of rabbits with highly purified protein BA has resulted in the production of a specific antibody. A specific immunoreactivity for chromosomal protein BA has been demonstrated by immunoelectrophoresis and double antibody immunoprecipitation analysis with rabbit anti-BA immunoglobulin and IgG fractions. Light microscope examination of normal rat liver crysections by the indirect immunofluorescence procedure has demonstrated a cytoplasmic as well as a nuclear localization for protein BA with a pronounced perinucleolar fluorescence. Immunoelectron microscopy employing the peroxidase antiperoxidase method of antigen localization has confirmed the immunofluorescence data and has show a heterochromatin localization for protein BA. The relationship of the localization of protein BA to gene control in quiescent cells or to configurations of heterochromatin as well as the marked reduction in the amounts of protein BA which occur in stimulated growth states remains to be defined.

Vitamin A-poor lipocytes: a novel desmin-negative lipocyte subpopulation, which can be activated to myofibroblasts

1995 ◽  
Vol 269 (4) ◽  
pp. G532-G541 ◽  
Author(s):  
G. A. Ramm ◽  
R. S. Britton ◽  
R. O'Neill ◽  
W. S. Blaner ◽  
B. R. Bacon
Keyword(s):  
Vitamin A ◽  
Rat Liver ◽  
Smooth Muscle Actin ◽  
Cell Types ◽  
Receptor Expression ◽  
Alpha Smooth Muscle Actin ◽  
Hepatic Fibrogenesis ◽  
Quiescent Cells ◽  
Isolation And Characterization ◽  
Normal Rat

Lipocytes have been classified as vitamin A-storing, desmin-positive cells. In hepatic fibrogenesis, lipocytes transform into myofibroblasts, which express alpha-smooth muscle actin (alpha-SMA) and produce increased amounts of collagen. We isolated a population of vitamin A-poor lipocytes (VAPL) from normal rat liver and examined the morphological and biochemical differences between VAPL and vitamin A-replete lipocytes (VARL). Desmin and alpha-SMA expression were determined by Western blot in quiescent cells and in cells activated by culture on uncoated plastic. Both cell types were alpha-SMA-negative; however, in contrast to VARL, freshly isolated VAPL did not contain desmin. Desmin expression was induced in VAPL on activation. With time in culture, both VAPL and VARL expressed alpha-SMA and produced collagen, indicative of transformation to myofibroblasts. Ferritin receptor expression was demonstrated in cultured VARL after 1 day and in VAPL after 5 days, indicating that this is an early marker of lipocyte activation. After 7 days, VARL and VAPL were indistinguishable in terms of desmin, ferritin receptor expression, and collagen production. This study demonstrates the first isolation and characterization of two distinct quiescent subpopulations of lipocytes from normal rat liver: desmin-negative VAPL and desmin-positive VARL. Both populations of cells can be activated to myofibroblasts, the phenotype associated with hepatic fibrogenesis.

scholarly journals STUDIES ON THE FUNCTION OF INTRACELLULAR RIBONUCLEASES

1966 ◽  
Vol 29 (3) ◽  
pp. 395-403 ◽  
Author(s):  
Takeshi Utsunomiya ◽  
Jay S. Roth
Keyword(s):  
Natural Products ◽  
Sodium Chloride ◽  
Rat Liver ◽  
Messenger Rna ◽  
Rnase Activity ◽  
Optimum Ph ◽  
Normal Rat ◽  
Pancreatic Rnase ◽  
The Stability ◽  
Normal Constituent

The RNase activity and properties of ribosome and polysome preparations from normal rat liver and some hepatomas have been examined. Polysome and ribosome preparations from the Novikoff, McCoy MDAB, and Dunning hepatomas had considerably higher specific RNase activity than corresponding preparations from normal rat liver, Novikoff ascites, or Morris 5123 hepatomas. The optimum pH of the RNase was approximately 8.5 for all samples tested, and the samples showed no evidence of latent RNase activity when treated with 3 M sodium chloride, EDTA, urea, or p-chloromercuribenzenesulfonic acid. The RNase activity appeared to be associated principally with breakdown products and/or subunits smaller than 80S. In the presence of Mg++ ions, subunits could reaggregate to form monomer ribosomes indistinguishable from the natural products, but some of the reassociated ribosomes could contain RNase activity which had been bound to the smaller particles. Similar results were obtained with spermine. In the hepatomas, evidence was obtained for the preexistence of considerable amounts of the smaller, RNase-containing subunits in the cell. When a small amount of crystalline bovine pancreatic RNase was added to partly dissociated ribosomes, the RNase was found only in association with the smaller subunits, and little or no enzyme was taken up by ribosomes or polysomes. The results have led to the conclusion that RNase is not a normal constituent of the ribosome or polysome, but that RNase may become associated with these particulates if dissociation and reassociation take place. Some implications of these findings for the stability of messenger RNA and for the mechanism of its breakdown are discussed.

Intracellular re-localisation by photochemical internalisation enhances the cytotoxic effect of gelonin — Quantitative studies in normal rat liver

2010 ◽  
Vol 142 (3) ◽  
pp. 347-353 ◽  
Author(s):  
Josephine Woodhams ◽  
Pei-Jen Lou ◽  
Pål K. Selbo ◽  
Alexander Mosse ◽  
Dahmane Oukrif ◽  
...  
Keyword(s):  
Rat Liver ◽  
Cytotoxic Effect ◽  
Quantitative Studies ◽  
Normal Rat

scholarly journals Retinyl palmitate hydrolase activity in normal rat liver.

1981 ◽  
Vol 256 (9) ◽  
pp. 4498-4503
Author(s):  
J.H. Prystowsky ◽  
J.E. Smith ◽  
D.S. Goodman
Keyword(s):  
Rat Liver ◽  
Retinyl Palmitate ◽  
Hydrolase Activity ◽  
Normal Rat

scholarly journals A monoclonal antibody to a human neutrophil-specific plasma membrane antigen. Effect of the antibody on the C3bi-mediated adherence by neutrophils and expression of the antigen during myelopoiesis.

1988 ◽  
Vol 167 (2) ◽  
pp. 421-439 ◽  
Author(s):  
B Pytowski ◽  
T G Easton ◽  
J E Valinsky ◽  
T Calderon ◽  
T Sun ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Bone Marrow Cells ◽  
Human Lymphocytes ◽  
Leukemic Cell ◽  
Human Neutrophils ◽  
Binding Studies ◽  
Granulocytic Differentiation ◽  
Average Molecular Mass ◽  
Cytochemical Analysis ◽  
Normal Human

We have used mice selectively tolerized to antigens of human lymphocytes by treatment with cyclophosphamide to raise an mAb, BH2-C6, that reacts with a plasma membrane antigen specific for human neutrophils. This specificity is demonstrated by indirect immunofluorescence microscopy, cytochemical analysis of fluorescence-positive and -negative cell populations separated by flow cytometry, and by the selective, complement-mediated killing of mAb BH2-C6-treated neutrophils. Additional evidence for the neutrophil specificity of mAb BH2-C6 is shown by immunoelectron microscopy, which demonstrates a lack of reactivity with human eosinophils. Immunoblotting of SDS-PAGE-separated proteins of polymorphonuclear leukocytes with 125I-labeled BH2-C6 identifies protein with an average molecular mass of 157 kD. Binding studies show that, at saturation, neutrophils bind 214,000 molecules of 125I-BH2-C6 per cell. Addition of mAb BH2-C6 to neutrophils significantly reduces the number of C3bi-opsonized sheep erythrocytes (EIgMC3bi) bound by these cells. This reduction is partly reversed by the presence of soybean trypsin inhibitor (SBTI), indicating that at least one part of this inhibition is due to BH2-C6-stimulated secretion of a serine protease that may affect ligand binding. Cytochemical analysis of normal human bone marrow cells sorted by cytofluorimetry identifies the promyelocyte as the precursor cell that first expresses BH2-Ag on the plasma membrane. Using the leukemic cell line HL-60, we demonstrate that only inducers of granulocytic differentiation, cis-retinoic acid, and dimethyloxazolidine stimulate the expression of BH2-Ag. These results show that the expression of BH2-Ag during myelomonocytic differentiation is a property uniquely possessed by cells committed to the neutrophilic lineage.

Hepatoma, host liver, and normal rat liver phospholipids as affected by diet

Lipids ◽  
1975 ◽  
Vol 10 (12) ◽  
pp. 736-745 ◽  
Author(s):  
Randall Wood
Keyword(s):  
Rat Liver ◽  
Host Liver ◽  
Normal Rat
Sign in / Sign up

Export Citation Format

Share Document