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S Ruggieri

Publications and source records attributed to S Ruggieri.

At least 127 records · Page 7Linked to original sources
PubMed1981

Lipid composition of Balb/c3T3, SV3T3, and Concanavalin A-selected revertant cells grown in media containing lipid-depleted serum.

The effects of growth in media supplemented with lipid-depleted fetal calf serum (LDS-media) on morphology, saturation density, and lipid composition were studied in Balb/c3T3, SV3T3, and Concanavalin A selected SV3T3 revertant cells (SV3T3 Rev cells). Cells grown in media containing complete fetal calf serum (FCS-medium) or reconstituted FCS (RS-medium) were used as controls. Growth in LDS-media reduced saturation densities of both SV3T3 and SV3T3 Rev cells while it affected only slightly the saturation density of normal parental cells. Similar inhibitory effects on growth were also induced by exposure of RS-medium. Growth in LDS-medium did not change the typical morphology of the three cell lines. 3T3, SV3T3, and SV3T3 Rev cells grown in LDS-medium showed an accumulation of triacylglycerols and free fatty acids together with a reduction of free cholesterol. All these changes were also present, however, in cells grown in these changes were also present, however, in cells grown in RS-Medium. Growth in LDS-medium induced an increase of 16:1 and 18:1, a decrease of 20:4, and an accumulation of 20:3 (n-9) in phosphatidylethanolamine, phosphatidylcholine, and phosphatidylinositol + phosphatidylserine of 3T3 cells. By contrast, only a slight accumulation of 20:3 (n-9) accompanied by a moderate increase of monoenoic acids was found in the phospholipids of SV3T3 cells grown in LDS-medium. SV3T3 Rev cells grown in LDS-medium showed changes in phospholipid fatty acids composition similar to those found in SV3T3 cells grown under the same conditions.

Animals↗
PubMed1979

Lipid composition of Yoshida ascites hepatoma and of livers and blood plasma from host and normal rats.

The lipid composition of Yoshida ascites hepatoma cells was analyzed together with that of ascitic plasma and of livers and blood plasma from host and normal rats. In comparison to normal livers, host livers showed no significant differences in the content of the various lipid classes, but contained a higher percentage of palmitic acid and a lower proportion of arachidonic acid in the major phospholipid classes. In addition, tumor growth induced a marked hypertriglyceridemia in host animals; changes in the concentration of other plasma lipid classes were not statistically significant. The ascitic plasma contained small amounts of lipids mainly constituted by cholesteryl esters and phospholipids. Yoshida hepatoma cells contained less phospholipids in comparison to both host and normal liver, while the increased level of triglycerides and the decrease of free fatty acids were not statistically significant. Hepatoma cells showed appreciable amounts of ether-linked lipids associated in part to neutral lipids (as glyceryl ether diesters) and, in part, to ethanolamine and choline phosphoglycerides. The alkyl groups in GEDE as well as in ethanolamine and choline phosphoglycerides were mainly constituted by C16:0 and C18:0 followed by C18:1. The alk-1-enyl groups in ethanolamine and choline phosphoglycerides were C16:0 and C18:0 with only a minor proportion of C18:1. In comparison to both host and normal liver, Yoshida hepatoma cells showed significant changes in the fatty acid composition of neutral lipids and phospholipids. Some of the major changes consisted of an increase of monoenoic acids associated with a decrease of arachidonic and docosahexaenoic acids in phosphatidylethanolamine, phosphatidylcholine, and phosphatidylinositol.

Animals↗
PubMed1979

Lipid composition of Morris hepatoma 5123c, and of livers and blood plasma from host and normal rats.

The lipid composition of Morris hepatoma 5123c was analyzed together with that of liver and blood plasma from both normal and tumor-bearing rats. The results showed that the liver of tumor-bearing rats contained higher amounts of glycerides, choelsteryl esters, free fatty acids and phospholipids than the liver of normal rats. In the blood plasma of tumor-bearing rats, there was an increase of free cholesterol and triglycerides; this latter difference, however, was not statistically significant. Acyl chain changes in the liver of tumor-bearing rats consisted of an increase of palmitic and oleic acids and a decrease of stearic and arachidonic acids in phosphatidylinositol. Morris hepatoma 5123c contained a lower amount of triglycerides than the livers (both host and normal) and showed a significant decrease of total phospholipids when compared to the host liver. The major acyl chain changes found in Morris hepatoma 5123c compared with both normal and host rat livers were: a) a higher percentage of arachidonic acid together with a lower proportion of palmitic acid in cholesteryl esters; b) an increase of stearic and arachidonic acids and a decrease of palmitic acid in triglycerides; and c) a higher level of palmitic and oleic acids associated with a lower percentage of stearic and C22 polyunsaturated acids in phosphatidylcholine.

Animals↗
PubMed1979

Lipid composition of SV40-induced transplantable hamster tumor.

The analysis of the lipid composition of the SV40-induced transplantable hamster tumor has shown that: (a) the total phospholipid content in the tumor is lower than that usually found in normal tissues and similar to that reported for other neoplasms; (b) except for a lower percentage of diphosphatidylglycerol, the phospholipid composition is comparable with that reported for normal tissues; (c) the fatty acid profiles of the various glycerophospholipid classes are characterized by high proportions of oleic acid; and (d) phosphatidylethanolamine contains proportions of alkenyl side chains which are consistent with the amounts of plasmalogenic phospholipids found in other neoplasms.

Animals↗
PubMed1979

Lipids of whole cells and plasma membrane fractions from Balb/c3T3, SV3T3, and concanavalin A-selected revertant cells.

The lipid composition of Balb/c3T3, SV3T3, and the concanavalin A-selected SV3T3 revertant cells has been analyzed at the whole cell and plasma membrane levels. In comparison to untransformed 3T3 whole cells, SV3T3 cells showed an unchanged content of triacylglycerols, free fatty acids, and glycerylether diesters but a lower concentration of total phospholipids, while no significant difference was found in the phospholipid composition. Whole SV3T3 revertant cells exhibited a lipid composition similar to that in untransformed 3T3 cells with the exception of a higher proportion of sphingomyelin. Analysis of isolated plasma membranes did not reveal any significant differences in the cholesterol to phospholipid molar ratio between 3T3 and SV3T3 or SV3T3 revertant cells. The major changes in the acyl chain pattern SV3T3 compared with whole 3T3 cells consisted of an increase of oleic and palmitoleic acids coupled with a decrease of C20 and C22 polyunsaturated acids in phosphatidylethanolamine and phosphatidylcholine; an increase of oleic acid was also evident in SV3T3 phosphatidylinositol plus phosphatidylserine. An increase of palmitoleic and oleic acids together with a decrease of arachidonic acid was also found in phosphatidylethanolamine of SV3T3 plasma membranes; the only change in SV3T3 plasma membrane phosphatidylcholine was an increase of oleic acid. An increase of monoenoic acids together with a decrease of arachidonic acid was also found in phosphatidylethanolamine, phosphatidylcholine, and phosphatidylinositol plus phosphatidylserine of SV3T3 revertant cells at the level of both whole cells and plasma membranes.

Animals↗
PubMed1978

Inactivation of uridine nucleosidase in yeast. Purification and properties of an inactivating protein.

It has been previously demonstrated in our laboratory that uridine nucleosidase (EC 3.2.2.3) is subjected in yeast to inactivation. An inactivating fraction has been isolated and purified to homogeneity with a procedure which includes gel filtration, adsorption chromatography, and electrofocusing techniques. The molecular weight of the enzyme, estimated either by sodium dodecyl sulfate disc gel electrophoresis or by gel filtration is approximately 44,000. No quaternary structure was evidenced. The inactivating activity possesses proteolytic activity against casein and hemoglobin with pH optima of 2.5 and 3.2, respectively. The optimal pH for uridine nucleosidase inactivation is around 4.7. The inactivating activity as well as the proteolytic activity of the preparation can be inhibited by IA but not by IB2 and IC, yeast macromolecular inhibitors for proteinase A (EC 3.4.23.8), B (EC 3.4.22.9), and C (EC 3.4.12.8), respectively. The apparent isoelectric point is pH 4.03. The carbohydrate content is 8.5%. A comparison of the properties of the inactivating protein with those of known yeast proteinases leads to the conclusion that it is identical with the enzyme previously designated as proteinase A, which for the first time has been obtained homogeneous and characterized. It has been shown that proteinase A could play a physiological role in the uridine nucleosidase inactivation process when it is associated, as a complex, with proteinase B.

Endopeptidases↗