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Biomedical subjects

J Lloveras

Publications and source records attributed to J Lloveras.

At least 109 records · Page 6Linked to original sources

[Effects of hypobaric hypoxia and erucic acid on mitochondrial triglycerides in rat heart].

At normal atmospheric pressure, an erucic acid-supplemented diet produces an increase of heart mitochondrial triglycerides. With the same quantity of erucic acid, hypoxia emphasizes the triglyceride overload in rat heart mitochondria. Thus, hypoxia increases the risk caused by rapeseed-oil. In hypoxia or at normal atmospheric pressure, rapeseed-oil without erucic acid does not modify the level of mitochondrial triglycerides.

Animals↗

[Spontaneous phospholipase A activity of rat pancreatic homogenates].

Rat pancreas presents a spontaneous phospholipase A activity which appears before trypsin activation at optimal pH 6.5. The responsible enzyme is independent of pancreatic prophospholipase A, as can be seen through experiments done in the presence of trypsin inhibitors. On the other hand, this enzyme is distinct from excretory phospholipase which is more active and whose optimal pH is 8.8. Thermostability and insensibility of spontaneously active phospholipase A to DFP differentiate it from lipase, carboxyl-esterhydrolase and lysophospholipase, respectively.

Animals↗

Phospholipases A1 and A2 in subcellular fractions and plasma membranes of Krebs II ascites cells.

A method is described for the localization and characterization of phospholipases A1 and A2 (EC3.1.1.4) in Krebs II ascites cells, particularly in the plasma membranes. Cells were lysed with a Dounce homogenizer in an isotonic sucrose medium. Plasma membranes sediment with mitochondria and lysosomes during subcellular fractionation and are finally isolated on a continuous sucrose gradient. The membranes are localized at two levels in the gradient, at densities of 1.06 and 1.15, in which 5'-nucleotidase (EC 3.1.3.5) activity exhibits a 9- and 21-fold purification, respectively. Total contamination by endoplasmic reticulum, lysosomes, and mitochondria is 17 percent for the low-density membrane fraction and 25 percent for the high-density fraction. The phospholipases A present in Krebs II cells are active at pH 4.0 and pH 7.5. At the 2 pH values, they have A1 and A2 specificities. The intracellular distribution of acidic forms is comparable to that of acid phosphatase (EC 3.1.3.1), while neutral forms are localized like lactate dehydrogenase (EC 1.1.1.27). A small proportion of neutral phospholipase A2 has the same repartition on the sucrose gradient as nicotinamide adenine dinucleotide diaphorase (EF 1.6.4.3), an endoplasmic reticulum marker, and as 5'-nucleotidase, a plasma membrane marker.

Animals↗

Cyclophosphamide (CP) substituting azathioprine after renal transplantation.

Eighteen patients received CP substituting AZ after renal transplantation following evidence of hepatitis. We have compared graft evolution before and after treatment with CP. Twelve patients showed no modification in graft evolution. In four patients the renal function decreased but it did not seem attributable to the change of the drug. Two patients showed intolerance attributable to the change of the drug. In one patient who received CP instead of AZ since the data of the transplant onwards, with no evidence of hepatic lesion, renal function decreased but this did not seem attributable to the use of the drug. The dose of CP in renal transplantation is discussed. We conclude that CP is a good substitute for AZ in renal transplanted patients. Adequate doses seemed to range between 0.7 and 1 mg/kg/day.

Azathioprine↗

[Specificity of action of phospholipases of rat intestinal mucosa].

The total homogenate of rat intestine is devoid of C or D phospholipase activity. At pH 6,5 in the presence of phosphatidylcholines, it exhibits a B phospholipase activity and in the presence of exogen lysophosphatidylcholines an A1 lysophospholipase activity. At pH 8,5 the intestinal mucous membrane of a rat shows an isolated A2 phospholipase activity.

Animals↗

[Comparative diffusion of 14C-ethionine and 14C-methionine in rat tissue].

The pancreas is the tissue which traps the most intensively the trace-dosis injected ethionine -14C; 30 min after the injection, the pancreas fixes the labelled product twice more than the liver and five times more than the stomach. This trapping might explain the pancreatic modifications occuring during the intoxication. In the same experimental conditions, the pancreas fixes the ethionine -14C twice less than methionine. Urinary excretion of ethionine is faster and more important than that of methionine.

Adipose Tissue↗