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Biomedical subjects

C Bode

Publications and source records attributed to C Bode.

At least 235 records · Page 13Linked to original sources
PubMed1984

Jejunal microflora in patients with chronic alcohol abuse.

The types and numbers of bacteria were examined in aspirates from the jejunums of 27 chronic alcoholics and 13 hospitalized control patients of comparable age distribution without alcohol abuse or diseases of the liver. Samples of jejunal juice were aspirated in the fasting state. The mean number of microorganisms obtained during anaerobic incubation was distinctly higher in the alcoholics (log10, mean +/- SD: alcoholics 4.9 +/- 2.2, controls 3.2 +/- 1.5, p less than 0.025). A similar difference was found for the number of aerobic bacteria (alcoholics 4.7 +/- 1.9, controls 3.3 +/- 2.1, p less than 0.05). Significant counts (greater than 10(5)/ml) of bacteria obtained during anaerobic incubation were more frequent in the alcoholics (48.1%) than in the controls (7.6%, p less than 0.001). Coliform microorganisms were cultured much more frequently from the jejunal fluid of the alcoholics (alcoholics 55.6%, controls 15.4%, p less than 0.025). In addition the incidence of Gram-negative anaerobic bacteria and endospore-forming rods was higher in the aspirates from alcoholics (p less than 0.05). In both groups the number of microorganisms in jejunal fluid correlated closely with the pH found in the gastric juice. No correlation was found between the numbers or types of microorganisms in the jejunum and the type or degree of liver disease in the alcoholics. It is concluded that bacterial overgrowth might contribute to functional and/or morphological abnormalities of the small intestine commonly found in patients with chronic alcohol abuse.

Actinomyces↗
PubMed1983

[Diagnostic value of lipase and isoamylase determination. Monitoring studies in patients with proven and suspected pancreatitis].

Changes of lipase (turbidimetric evaluation), total amylase and isoamylases (inhibition test) were determined in 93 patients with proven or suspect pancreatitis. In 35 patients with established acute pancreatitis 143 sera were investigated in the course of disease. Lipase and pancreatic amylase were increased in these samples significantly more often (thus longer in the course of disease) than total amylase. Eight patients with chronic pancreatitis and exocrine insufficiency showed very low lipase and pancreatic amylase activities whereas total amylase was normal. Observations in the course of two groups of patients with suspect (but not established) pancreatitis showed superior organ specificity of lipase and pancreatic amylase when compared to total amylase. However, no relevant difference of the diagnostic validity of both enzymes could be demonstrated.

Acute Disease↗
PubMed1983

Serum apolipoprotein AI synthesis in rat hepatocytes and its secretion as proform.

Rat hepatocytes in monolayer or suspension culture synthesize serum lipoprotein AI. It is secreted into the serum-free culture medium. Synthesis and secretion processes were studied in the presence of radiolabelled amino acids. The synthesis product of the hepatocytes and the secretion product from the medium were isolated by immunoprecipitation with a mono-specific rabbit antiserum against rat apolipoprotein AI. The intracellular and secreted products were homogeneous and identical in polyacrylamide gel electrophoresis but had reduced electrophoretic mobility as compared to native apolipoprotein AI. They were submitted to automated Edman degradation. They were present in their proform, the N-terminus of which is extended by a hexapeptide. In the presence of rat serum the proform is proteolytically transformed into the mature form of apolipoprotein AI.

Amino Acid Sequence↗
PubMed1983

A serum proteinase converts proapolipoprotein AI secreted by rat hepatocytes to the mature apolipoprotein.

Apolipoprotein AI integrated into the high-density lipoprotein particle in serum was synthesized in the rat hepatocyte in the presence of radiolabelled amino acids and isolated from the cells in primary culture (suspension) as its proform, with the N-terminus extended by a hexapeptide segment. The primary secretion product is this proform which is only further proteolytically processed in the presence of the serum fraction with density higher than 1.21 g/ml. The secretion product and the proteolytically converted product were characterized by Edman degradation of their respective amino-acid sequences after radiolabelling with [3H]valine and [3H]phenylalanine, the positions of which are well established in the preproform and in the N-terminus of mature rat apolipoprotein AI. The products from the lysed cells and their culture medium were purified by immunoprecipitation, sodium dodecyl sulfate gradient gel electrophoresis and subsequent electroelution of the apo AI band. The proform sediments associated with a particle of density 1.16-1.20 g/ml. The serum proteinase which is inhibited by phenylmethanesulfonyl fluoride, but not by sulfhydryl reagents, is presumably a serine proteinase.

Animals↗
PubMed1982

Salivary secretion in chronic pancreatitis with special reference to albumin and lactoferrin.

Saliva from one parotid gland was collected under citric acid stimulation in three groups consisting of 69 control subjects and two groups consisting of 25 patients with chronic and relapsing chronic pancreatitis. Mixed saliva was collected under mechanical stimulation from 10 patients and 6 control subjects. Flow rates and the contents of bicarbonate, amylase and protein were determined. In a subgroup of patients and controls albumin and lactoferrin were measured. Wide inter- and intraindividual variations of secretory values were observed and normal values (which are reported in detail) were highly dependent from conditions of stimulation. Secretory patterns were not significantly different between patients and control subjects. It is concluded that the alterations leading to an elevation of albumin and lactoferrin and a fall in other secretory values are restricted to the exocrine pancreas and do not affect salivary glands in chronic pancreatitis.

Adult↗
PubMed1982

The effect of storage at - 80 degrees C on the activities of cytoplasmic, mitochondrial and microsomal enzymes in rat liver.

The effect of storage at - 80 degrees C for 1-28 days on the activity of 12 enzymes in intact liver tissue, liver extract and isolated hepatic microsomes was investigated. To find optimal conditions for tissue homogenization for this study the effects of three types of homogenization on the activity of 10 enzymes from different cell compartments were compared. The activities of glucokinase and phosphofructokinase decreased markedly during storage of both supernatant and liver tissue. Storage of liver tissue increased the activity of mitochondrial enzymes or isoenzymes. While this effect can be explained by additional disintegration of liver tissue caused by freezing and thawing for enzymes like glutamine dehydrogenase, other mechanisms may be involved in the prolonged increase observed in the activity of citrate synthase and xanthine oxidase during storage. The activity of a number of enzymes from the cytosol, mitochondria and microsomes decreased more markedly in the stored liver samples than in the stored supernatant or in the stored microsomal pellet. Cytochrome P 450 content remained stable throughout the whole storage period in both intact liver tissue and isolated microsomes.

Animals↗
PubMed1982

Activities of cytoplasmic, mitochondrial and brush border enzymes in jejunal mucosa of chronic alcoholics.

The activity of certain enzymes of the energy producing metabolism of the cytoplasmic and mitochondrial compartment and of disaccharidases was determined in jejunal biopsies of 24 chronic alcoholics (CA) and 10 non-alcoholic control subjects (C). The activity of glucokinase, an enzyme of glycolysis, was markedly (44%, p less than 0.05) increased in the biopsies obtained from CA, while the activity of fructose bisphosphatase, an enzyme of gluconeogenesis, was significantly (p less than 0.05) depressed in CA when compared to C. The activity of other glycolytic enzymes was not affected in CA. The activity of L-alanine amino-transferase was lower in CA (p less than 0.05). A reduction was also seen for mean succinate dehydrogenase activity in CA (-30%), however, this difference was not statistically significant. The mean activity of lactase, maltase and sucrase was comparable in both groups.

Alanine Transaminase↗
PubMed1981

Influence of feeding fructose on fructose and glucose absorption in rat jejunum and ileum.

The influence of feeding isocaloric diets containing either 65% of fructose (F 65) on 65% of glucose (G 65) were studied on the uptake of both sugars in segments of rat proximal jejunum and distal ileum. The hexose absorption was compared to that obtained in animals receiving isocaloric amounts of a diet containing 30% of glucose (G 30). Feeding fructose (F 65) for 3 days resulted in a 2.5-fold increase of fructose uptake in the jejunum and a 40% increase in the ileum as compared to group G 30. When fructose (F 65) was administered instead of G 65 the uptake of fructose was enhanced by 75% in the jejunum and 35% in the ileum. Stimulation of glucose absorption in segments of the proximal and distal small intestine by diets F 65 and G 65 was nearly identical as compared to the values of group G 30. The stimulation of the uptake of fructose induced by fructose feeding parallels an adaptive increase in the activity of enzymes involved in fructose metabolism in the mucosa of the small intestine.

Animals↗
PubMed1981

The pattern of D-galactosamine-induced hepatocellular injury modified by simultaneous application of D (--)-fructose.

As shown by light and electron microscopy, and by biochemical investigation, D-galactosamine-induced hepatocellular injury in the rat can be prevented by giving fructose simultaneously. However, when injected 3 h after D-galactosamine, fructose has no protective effect. It is suggested that rapid fructose phosphorylation, with the consequent marked depression of the hepatocellular ATP pool, inhibits the more prolonged D-galactosamine phosphorylation and with it the injurious effects of D-galactosamine metabolism.

Animals↗
PubMed1981

Effect of fructose feeding on the activity of enzymes of glycolysis, gluconeogenesis, and the pentose phosphate shunt in the liver and jejunal mucosa of rats.

The influence of fructose feeding for 1 to 12 days on the activity of enzymes of glycolysis and gluconeogenesis was studied in the jejunal mucosa and the liver of rats. In the jejunal mucosa fructose feeding leads to an increase in the activity of 6-phosphofructokinase (p less than 0.05) and fructose-1.6-bisphosphate aldolase (p less than 0.05), while the activity of hexokinase and glucose-6-phosphate dehydrogenase remains unchanged. Fructose feeding increases the activity of fructose-bisphosphatase in the jejunal mucosa, however, the absolute values of this enzyme remain low (less than 10%) when compared to those in the liver. In the liver fructose feeding is followed by a marked increase of the activity of fructose-bisphosphatase and glucose-6-phosphate dehydrogenase. In contrast, the activity of glucose-6-phosphatase decreases significantly under a fructose enriched diet. The enzyme activity rose to a maximum within 3 days; in the following time of observation no major changes occurred. The results are in accordance with the assumption that fructose feeding leads in the jejunal mucosa mainly to adaptive alterations of the activity of those enzymes which are involved in the breaking-down of fructose, whereas in the liver the activity of those enzymes is increased, which take part in the new synthesis of glucose-6-phosphate or which direct glucose-6-phosphate into the pentose-phosphate.

Animals↗
PubMed1980

Adaptative changes of activity of enzymes involved in fructose metabolism in the liver and jejunal mucosa of rats following fructose feeding.

The adaptative response of a diet containing 60% fructose on the activity of those enzymes which are involved in the metabolism of fructose was measured in the liver and in the jejunal mucosa of rats over a period of 12 days. Control animals received isocaloric amounts of glucose or starch. Under fructose feeding there was a marked increase in the activity of fructose-1-phosphate aldolase (3-fold), ketohexokinase (2--3-fold), and triokinase (3-fold) in the jejunal mucosa. In the liver, however, a significant increase in enzyme activity could only be seen for triokinase (2--3-fold), whereas the activity of the other enzymes measured were only slightly or not at all altered. The activity of the three enzymes mentioned above were elevated to a maximum within 3 days after feeding the fructose diet. In the following time of observation no major further changes occurred. The results show that fructose feeding in comparison to a glucose or starch containing diet leads to a marked adaptative increase in the activity of those enzymes, which are involved in the breakdown of fructose, only in the jejunal mucosa.

Alcohol Oxidoreductases↗
PubMed1980

Damage of rat small intestine induced by ethanol. Effect of ethanol on fecal excretion of intestinal alkaline phosphatase.

Single administration of ethanol or alcoholic beverages (5g ethanol/kg body weight) induces a decrease of the 24h excretion of fecal intestinal alkaline phosphatase (I-AP) activity of 28% (P less than 0.05) in comparison to controls (0.9% saline). Administration of higher amounts of 20% (v/v) ethanol (8g/kg body weight on 3 consecutive days) yields a decrease of fecal I-AP excretion up to 82% (P less than 0.005) in comparison to controls (saturated glucose solution). The interpretation of these results as a toxic effect of ethanol to small intestinal mucosa was supported by measurement of enzymatic activity in the small intestinal mucosa and by morphometric data.

Alkaline Phosphatase↗
PubMed1979

Alcohol metabolism in man: effect of intravenous fructose infusion on blood ethanol elimination rate following stimulation by phenobarbital treatment or chronic alcohol consumption.

The effect of phenobarbital (PB) pretreatment and of chronic alcoholism on blood ethanol elimination rate (BEER) was investigated in man. In order to gain additional information concerning the mechanism of possible changes BEER was determined before and during intravenous infusion of fructose, a compound known to increase the NADH-oxidizing capacity of the liver and thereby stimulating alcohol oxidation rate. Following PB-treatment (300 mg/day for 5-6 days, n = 8) a marked increase in unstimulated (U-) BEER was obtained. But the fructose stimulated (FS-) BEER was not significantly changed by PB-treatment. In chronic alcoholics (n = 15) U-BEER values above the upper limit (chi + 2 S D) obtained in healthy controls, were observed only when the time of sobriety was less than one week (n = 6). Values of FS-BEER in chronic alcoholics with increased basal alcohol oxidation rates were in the same range as those of healthy controls. In 5 out of the 6 alcoholics in whom the values were elevated on admission, BEER decreased significantly after withdrawal of alcohol for 2-4 weeks. Since FS-BEER was nearly identical in all conditions tested, the distinct changes in U-BEER are probably independent of changes in the activity of enzymes involved in alcohol oxidation. It is assumed that alcohol metabolism in man is mainly controlled by the rate of NADH reoxidation in the liver.

Adult↗
PubMed1979

Primary hyperparathyroidism in a dog.

A 6-year-old male Standard Poodle had hypercalcemia, hypophosphatemia, and a urinary concentrating defect. A parathyroid adenoma involving the left caudal parathyroid gland was surgically removed. Transient hypocalcemia followed, which resolved without treatment. A renal biopsy did not demonstrate renal parenchymal mineral deposition. Urinary concentrating ability returned after surgery.

Adenoma↗
PubMed1978

[The question of use of glucose or fructose for parenteral feeding. Results of a comparative study].

Glucose and fluctose (400 g/24 h) were compared as sources of carbohydrate in parenteral nutrition in patients following major abdominal operations or following multiple injuries. Group A (n = 8) received glucose during the first 2 days and fructose for another 2 days thereafter. In group B (n = 8) the sequence of carbohydrate infusion was reversed (2 days' fructose follwed by 2 days' glucose). The additional infusion to amino acids and a fat emulsion remained constant (total calories: 2,700 kcal/24 h). The following results were obtained: 1. Mean blood glucose concentrations were elevated in both infusion periods. During infusion of glucose the values were about 10% higher than those obtained during fructose infusion. Insulin administration was not necessary any of the patients studied. 2. Urinary excretion of both monosaccharides was negligible. 3. Blood lactate concentrations were higher during the infusion of fructose when compared to the glucose infusion period. The concentration of ketone bodies in the blood was not significantly influenced by either regimen. No major changes in base-acid equilibrium were observed. 4. The serum concentration of uric acid and several other metabolites did not differ significantly during the two infusion periods. 5. Mean urinary urea excretion exhibited a 30% increase during fructose infusion when compared to the glucose infusion period (p less than 0.012). From the results of t;is study and earlier findings it is concluded that fructose in a dose up to 400 g/day has no proven advantages over glucose in postoperative parenteral nutrition.

Adolescent↗
PubMed1978

Effect of alcohol on microsomal cortisol 4en-5 alpha-reductase in the liver of rats fed on a standard or low protein diet.

Alcohol feeding (40% of total calories over a period of 9 days) increases microsomal cortisol-5 alpha-reductase activity in rat liver distinctly. It is assumed that this is an adaptive response to an increased release of cortisol caused by alcohol administration. Cortisol-5 alpha-reductase activity is decreased to one third of control values in rats fed an isocaloric, low protein diet. The response to alcohol feeding is susta ined in these animals. Phenobarbital treatment (80 mg/kg x day) stimulates 5 alpha-reduction of cortisol per g of microsomes almost twofold. The activity calculated per total liver increases 4-fold. Alcohol administration has no additional effect on cortisol-5alpha-reductase in phenobarbital-treated rats.

Animals↗
PubMed1978

A comparison between naturally occurring macroamylasaemia and macroamylasaemia induced by hydroxyethyl-starch.

Macroamylasaemia was produced in vitro by incubation of hydroxyethylstarch with serum, and in vivo by intravenous infusion of hydroxyethylstarch. Gel filtration on Sephadex G-100 revealed distinct differences in molecular size distribution between such hydroxyethylstarch-induced macroamylase and the usual form of naturally occurring macroamylase which was observed in a few patients from our hospital. Further studies demonstrated that the gel filtration elution pattern of amylase activity in serum containing hydroxyethylstarch-induced macroamylase is significantly altered with time in vitro and in vivo, probably because of an enzymatic degradation of the hydroxyethylstarch components of the macromolecular complexes. In a healthy volunteer the serum amylase activity was elevated to a maximum of 797 u/l and the renal clearance rate of amylase was diminished to a minimum of 0.3 ml/min after infusion of 500 ml of a 6% solution of hydroxyethylstarch, as compared to 300 u/l, and 0.95 ml/min, respectively, during the pre-infusion period.

Adult↗