Chemotherapy use in end-of-life digestive cancer patients: a retrospective AGEO observational study.

Background: The use of chemotherapy (CT) near the end-of-life (EOL) is an important issue in oncology since it could degrade quality of life. CT near EOL is still poorly studied, with no dedicated study in gastrointestinal (GI) cancer patients.

Aim: To analyze in GI cancer patients the factors associated with the use of CT within 3- and 1-month before patients' death.

Bradykinin metabolism in perfused rat kidney.

The purpose of this study was to assess the capacity of perfused rat kidney to inactivate bradykinin (BK), and to compare the BK degrading capacity of rat kidney with the BK degrading capacities of rat lung, liver, and skeletal muscle, which was approximated by perfusion of rat hind limbs. Radioactively labeled BK, with the Pro2 and Pro3 residues having been tritiated, in an asanguinous salt solution was perfused through the kidney of the rat, over a concentration range of .0028-33 microM.

Bradykinin metabolism in rat hind limbs.

The purpose of this study was to assess the capacity of perfused rat hind limbs, the majority of which is skeletal muscle, to inactivate bradykinin (BK), and to compare the BK degrading capacity of rat hind limbs with the BK degrading capacities of rat lung and liver. BK, with tritiated Pro2 and Pro3 residues, in an asanguinous salt solution was perfused for a single passage through skeletal muscle and other tissues in the hind legs of the rat over a concentration range of .0029 to 49.

Bradykinin metabolism in the liver and lung of the rat.

Bradykinin (BK) in an asanguinous salt solution was perfused through intact rat liver. The perfusate was delivered through the portal vein and was collected from the inferior vena cava. BK concentrations varied from 0.

The effect of smoke inhalation on bradykinin metabolism by the perfused and ventilated rat lung.

The effect of smoke inhalation on bradykinin metabolism was studied in the rat lung perfused with Ringer's bicarbonate solution. After smoke (from cotton, polyester, or seat cushion material) inhalation, tritium-labeled bradykinin was added to the Ringer's bicarbonate solution, and then the lung perfusion effluent aliquots containing bradykinin and its metabolic fragments were collected after a single transpulmonary passage. For the 20 control rats without smoke inhalation, 91% of the bradykinin dose was metabolized, with Pro-Pro (I), 49%, and Arg-Pro-Pro-Gly-Phe (II), 32%, being the predominant bradykinin cleavage fragments.

Kinin metabolism in the perfused ventilated rat lung. II: Influence of ventilation, perfusion, and perfusate composition variation on bradykinin metabolism in uninjured lung.

Bradykinin metabolism by peptidases of the pulmonary endothelium has been investigated in the previously uninjured, ventilated, and asanguinously perfused rat lung. The influence of short-duration (up to 20 min) abnormal ventilation and perfusion conditions on bradykinin metabolism was assessed. Neither variation of the oxygen concentration (0 to 45%) nor omission of carbon dioxide in the ventilatory gas altered bradykinin metabolism significantly.

Kinin metabolism in the perfused ventilated rat lung. I: Bradykinin metabolism in a system modeling the normal, uninjured lung.

Bradykinin (BK) in an asanguinous salt solution was perfused through intact rat lung. BK concentration varied from 0.0015 to 89 microM.

Human lung membrane-bound neutral metallo-endopeptidase-catalyzed hydrolysis of bradykinin.

Human lung membrane-bound neutral metallo-endopeptidase (NME; EC 3.4.24.

Toxicity of polymerized hemoglobin solutions.

Four solutions of bovine polymerized hemoglobin (BPHS) and rabbit plasma were used to replace one-third of the blood volume in five groups of rabbits. The first three solutions were "impure" because of the presence of stromal phosphatidyl-ethanolamine and phosphatidyl-serine in BPHS-1, environmental endotoxins in BPHS-2, and a large amount of higher molecular weight hemoglobin-glutaraldehyde polymers in BPHS-3. These solutions caused a 33 per cent mortality rate and significant morbidity which was characterized by hemodynamic instability, respiratory and renal insufficiency, elevation of hepatic enzyme levels, thrombocytopenia, leukopenia, disseminated intravascular coagulation (DIC) and activation of the alternate pathway of complement.

A multicatalytic high-molecular-weight neutral endopeptidase from human kidney.

A multicatalytic endopeptidase (ME) with three distinct activities, chymotrypsin-like, cucumisin-like, and trypsin-like, occurred in all rat tissues examined with highest activities in kidney, testes, liver, and spleen; they were assayed with benzyloxycarbonyl-Gly-Gly-Leu-p-nitroanilide (Z-Gly-Gly-Leu-pNA), benzyloxycarbonyl-Leu-Leu-Glu-2-naphthylamide (Z-Leu-Leu-Glu-2NA), and benzyloxycarbonyl-Gly-Gly-Arg-2-naphthylamide (Z-Gly-Gly-Arg-2NA), respectively. All three activities were recovered from a single protein band on a polyacrylamide gel after electrophoresis of purified human kidney ME. The native enzyme had a Mr of 650,000, and it consisted of about 5,135 amino acid residues.

Carotid sinus reflexes in rats given small doses of lead.

The effect of low level lead poisoning on the carotid sinus reflex in rats was studied. The reflex was evoked by carotid artery clamping, in control and lead-poisoned animals. Wistar rats were given lead acetate trihydrate (50 mg/kg) via stomach tube once weekly for 5 weeks; control animals were given equimolar amounts of sodium acetate.

A high-molecular-mass neutral endopeptidase-24.5 from human lung.

A high-Mr neutral endopeptidase-24.5 (NE) that cleaved bradykinin at the Phe5-Ser6 bond was purified to apparent homogeneity from human lung by (NH4)2SO4 fractionation, ion-exchange chromatography and gel filtration. The final enzyme preparation produced a single enzymically active protein band after electrophoresis on a 5% polyacrylamide gel.

Response of the cardiovascular system to catecholamines in rats given small doses of lead.

Experiments were done in order to assess the influence of low level lead poisoning in rats upon the responses of the rat cardiovascular system to perturbation by norepinephrine, epinephrine, and isoproterenol administration. Wistar rats were given lead acetate (50.0 mg/kg) via stomach tube once weekly for 5 weeks.

Human lung post-proline endopeptidase: purification and action on vasoactive peptides.

Post-proline endopeptidase (PPE, EC 3.4.21.

Serum angiotensin-converting enzyme levels in patients with silicosis.

In a group of control subjects, the mean serum angiotensin-converting enzyme (ACE) level was 38.1 +/- 10.6 nmol/min X ml (n = 30), and in a group of silicosis patients the mean serum ACE level was 45.

Cleavage of the Arg1-Pro2 bond of bradykinin by a human lung peptidase: isolation, characterization, and inhibition by several beta-lactam antibiotics.

An aminopeptidase P (EC 3.4.11.

Kinetic investigation of the hydrolysis of aminoacyl p-nitroanilides by dipeptidyl peptidase IV from human and pig kidney.

Dipeptidyl peptidase IV (dipeptidyl-peptide hydrolase, EC 3.4.14.

Kinin cleavage by human erythrocytes.

An aminopeptidase-P has been purified 230-fold from human erythrocytes. The purified enzyme cleaved arginine from des-(Arg9)-bradykinin (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe) had a molecular weight in nondenaturing buffers of 155,000 +/- 6,900 daltons, was not inactivated by chelating agents, had a pH optimum of 7.2, and was stimulated by manganous ions.

A kininase and a kinin-converting enzyme: two distinct alpha aminoacyl peptide hydrolases from bovine lung.

Two closely related but different aminopeptidases from bovine lung have been isolated and characterized. The first aminopeptidase, which removes the N-terminal arginine residue from L-arginyl-L-prolyl-L-proline, bradykinin, and des-[Arg9]-bradykinin, has kininase activity; it has a pH optimum of 8.0, is stimulated by Mn2+, and its molecular weight in dilute buffers is slightly greater than 240,000 daltons.

Human-liver alanine aminopeptidase. A kinin-converting enzyme sensitive to beta-lactam antibiotics.

Human liver alanine aminopeptidase (EC 3.4.11.

Action of human pancreas alanine aminopeptidase on biologically active peptides: kinin converting activity.

A group of 15 biologically active peptides were studied with respect to their susceptibility to chain shortening by human pancreas alanine aminopeptidase. Those susceptible were somatostatin, melanocyte stimulating hormone, fibrinopeptide A, eosinophilotactictetrapeptide, lysyl-bradykinin, and methionyl-lysyl-bradykinin. The latter two were selected for further study.

Inhibition of Bacillus subtilis aminopeptidase D by beta-lactam antibiotics.

Penicillins and cephalosporins inhibit the hydrolysis of D-alanyl-beta-naphthylamide by aminopeptidase D (EC 3.4.11.

Multiple molecular forms of human alanine aminopeptidase: immunochemical properties.

Human pancreas, kidney, and liver alanine aminopeptidases have similar if not identical antigenic determinants even though these three isoenzymes have distinctly different electrophoretic mobilities. Single precipitin lines without spur formation were obtained for all three enzymes with antisera obtained from rabbits immunized with these three purified enzymes. Treatment of these enzymes with neuraminidase eliminated the differences in their electrophoretic migration on polyacrylamide gels and on agarose immunoelectrophoresis gels.

Multiple molecular forms of human pancreas alanine aminopeptidase.

Human pancreas is the source of an alanine aminopeptidase (HPAA) that is unique to pancreas and is readily distinguishable from the liver, kidney, and duodenal alanine aminopeptidases. Each of these three aminopeptidases appears in small quantities in blood and therefore may consitute tissue/organ specific marker enzymes. In this study alanine aminopeptidase from pancreas has been purified.

Human kidney alanine aminopeptidase: physical and kinetic properties of a sialic acid containing glycoprotein.

Human kidney alanine aminopeptidase has been purified to apparent homogeneity as judged by electrophoresis and sedimentation in the analytical ultracentrifuge. Amino acid analyses indicate that the enzyme is high in tryptophan content and low in cysteine content. The enzyme contains sialic acid, hexoses, and glucosamine, which make up 21% of its dry weight.