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Biomedical subjects

C Mineo

Publications and source records attributed to C Mineo.

29 records · Page 2Linked to original sources
PubMed1992

Isolation of rat bone marrow mast lineage cells using Thy 1.1 and rat stem cell factor.

Recent reports have shown that various marrow-derived cell populations respond vigorously to recombinant rat stem cell factor (rrSCF164), one form of the kit-ligand. In the present study, we isolated cell populations from rat bone marrow using the Thy 1.1 antigen (an antigen that in the rat is differentially expressed on primitive hemopoietic progenitor cells) and fluorescently conjugated rrSCF164 (rrSCF164-PE). We show that rrSCF164 only stimulates cells that are enriched in the brightest Thy 1.1 populations (Thy 1.1bright). Numerous cell lines were generated by serial passage in rrSCF164 containing medium, and the prototypic cell lines have been designated SRT002 and SRT003. Each cell line retains the Thy 1.1bright phenotype and does not respond to interleukins (IL) 1-8, IL-10, granulocyte (G) colony-stimulating factor (CSF), granulocyte macrophage (GM) CSF, M-CSF, or crude preparations of mitogen-stimulated T-cell supernatants. The Thy 1.1bright population of rat marrow was subdivided into a subset that binds rrSCF164-PE (Thy 1.1bright, rrSCF164+). The majority of these cells possess certain characteristics in common with marrow-derived mast cells and the Thy 1.1bright, rrSCF164 responsive cell lines, having similar granule morphology, being metachromatic, and reacting positively with alcian blue. Moreover, rats treated with rrSCF164 displayed significant increases in Thy 1.1bright, rrSCF164+ cells in the bone marrow. These studies show that the combination of Thy 1.1 and rrSCF164 makes possible the isolation of a unique subset of rat bone marrow cells that differentially express the Thy 1.1 antigen and the cell surface receptor c-kit, the majority of which are morphologically similar to marrow-derived mast cells.

Animals↗
PubMed1992

Hydrolysis of lipid droplets in acid cholesteryl-esterase-deficient fibroblasts.

The mechanisms of hydrolysis and accumulation of cholesteryl oleate-lipid droplets prepared in vitro were studied in acid cholesteryl-esterase-deficient fibroblasts (GM00863, GM03111). Acid cholesteryl esterase activity was reduced in both GM00863 and GM03111 (8.9% and 17.4% of the normal level, respectively), while neutral cholesteryl esterase activity was highly stimulated in GM03111. The hydrolysis of [14C]-cholesteryl oleate-lipid droplets in GM00863 was almost as efficient as in normal cells, while that in GM03111 was highly stimulated. When viewed by polarized microscopy the lipid droplets which had accumulated in the mutant cells showed anisotropic liquid crystalline structures. As in normal cells, some of these lipid droplets were observed by transmission electron microscopy as membrane-free lipid inclusion bodies in the cytoplasm. These results suggest that lipid droplets internalized into phagolysosomes of these mutant cells transferred to the cytoplasm, and were hydrolyzed there probably by neutral cholesteryl esterase.

Cells, Cultured↗
PubMed1991

Effect of PGI2 on platelet binding to partially denuded endothelial monolayer in vitro.

We have developed a new model for the investigation of platelet interaction with injured vascular endothelium. This involves the quantitative detection of platelet binding to a partially denuded endothelial cell monolayer in vitro. Porcine arterial endothelial monolayer, cultured on collagen gel containing fibrinogen and fibronectin, was partially denuded and the binding of 51Cr-platelets was measured. A synergistic increase in platelet binding was observed in the presence of fibrinogen and fibronectin. A distinct aggregation of platelets along the edge of the denuded area of the endothelial monolayer was seen. Prostacyclin (PGI2) inhibited platelet aggregation, although adhesive platelets were still present at denuded sites.

Animals↗
PubMed1990

Transcellular transport of angiotensin II through a cultured arterial endothelial monolayer.

We have studied the mechanisms of angiotensin II (A-II) transport through a cultured arterial endothelial cell monolayer. The transport of 125I-labeled A-II was inhibited by excess unlabeled A-II (50 microM) and [Sar1, Ile8]-A-II (50 microM), but was not inhibited by bradykinin (50 microM). The transport process was shown to be temperature dependent and was inhibited by 10 mM NaN3 plus 50 mM 2-deoxyglucose. Monensin (50 microM), an inhibitor of endocytotic trafficking, reduced the rate of transport of 125I-A-II. It is also shown that the specific pathway for A-II transport was unidirectional from the apical to the basolateral surface of the endothelial cell monolayer.

Adenosine Triphosphate↗
PubMed1990

Atherosclerosis and molecular pathology: mechanisms of cholesteryl ester accumulation in foam cells and extracellular space of atherosclerotic lesions.

This article reviews aspects of the molecular pathology of cholesteryl ester accumulation in atherosclerotic lesions. 1. Transcytosis of lipoproteins through cultured endothelial monolayer. 2. Transformation to foam cell from macrophage. 3. Cholesteryl ester deposition in the extracellular space of atherosclerotic lesions. We also discuss the development and use of novel monoclonal antibodies recognizing atherosclerotic lesions and peroxidized lipoproteins prepared from atherosclerotic lesions.

Animals↗
PubMed1990

Accumulation of oleate-rich cholesteryl esters by acetyl-LDL in macrophages in the presence of an acyl-CoA: cholesterol acyltransferase inhibitor (Sandoz 58-035).

The mechanism through which cholesteryl esters rich in oleic acid accumulate in the cytoplasm was studied. The fatty acid composition of the cholesteryl esters in acetyl-LDL was high in linoleic acid, while that of cholesteryl ester inclusion bodies accumulated in the cytoplasm was high in oleic acid. This compositional change of fatty acids in cholesteryl esters occurred even in the presence of an acyl-CoA: cholesterol acyltransferase (ACAT) inhibitor, Sandoz 58-035. These results suggest that oleate-rich cholesteryl esters accumulated in the cytoplasm, even though the reesterification in microsome was inhibited by an ACAT inhibitor.

Amides↗
PubMed1988

Intracellular transport of cholesteryl esters from lysosomes to cytoplasm in macrophages.

The mechanism through which nonmembranous lipid inclusion bodies consisting of cholesteryl esters accumulate in the cytoplasm was studied. Most lipid inclusion bodies in macrophages after 24 h incubation with anisotropic cholesteryl oleate liquid crystals were surrounded by a limiting membrane. The limiting membrane, however, could not be observed after further incubation for 48 h in the presence of esterastin, which is known to be an inhibitor of lipase and esterase. Under these conditions, the levels of hydrolysis and re-esterification of cholesteryl esters were less than 15% and 5% of the control ones, respectively. These results suggest that the inclusion bodies were transferred from lysosomes to the cytoplasm, with partial hydrolysis of cholesteryl esters, in addition to through the pathway via microsomes.

Animals↗
PubMed1987

Effect of PGI2 on transcellular transport of fluorescein dextran through an arterial endothelial monolayer.

The effects of prostacyclin (PGI2) and stable derivatives of PGI2, such as isocarbacyclin (PGI2 deriv. (A] and isocarbacyclin methyl ester (PGI2 deriv. (B)), on junctional transport of fluorescein dextran (FD) through cultured porcine arterial endothelial cells were investigated. These PGI2S inhibited the transcellular transport dose-dependently. After the elimination of PGI2, its inhibitory effect persisted for at least 1 hr. A good correlation was found between increase of cAMP and the potency of inhibition. Increase of cAMP after PGI2 treatment seemed to be involved in the inhibition of FD transport.

1-Methyl-3-isobutylxanthine↗
PubMed1986

Isolation and analysis of a mammalian temperature-sensitive mutant defective in G2 functions.

A temperature-sensitive (ts) mutant, designated tsFT210, was isolated from a mouse mammary carcinoma cell line, FM3A. The tsFT210 cells grew normally at 33 degrees C (permissive temperature), but more than 80% of the cells were arrested at the G2 phase at 39 degrees C (non-permissive temperature) as revealed by flow-microfluorimetric analysis. DNA replication and synthesis of other macromolecules by this mutant seemed to be normal at 39 degrees C for at least 10 h. However, in this mutant, hyperphosphorylation of H1 histone from the G2 to M phase, which occurs in the normal cell cycle, could not be detected at the non-permissive temperature. This suggests that a gene product which is temperature-sensitive in tsFT210 cells is necessary for hyperphosphorylation of H1 histone and that this gene product may be related to chromosome condensation.

Animals↗