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Biomedical subjects

B Hadorn

Publications and source records attributed to B Hadorn.

At least 19 recordsLinked to original sources
PubMed2001

Celiac disease in a patient with a congenital deficiency of intestinal enteropeptidase.

We report on a 40-yr-old man with both primary enteropeptidase deficiency and celiac disease. He suffered from severe intestinal malabsorption and growth failure as a child. Enteropeptidase deficiency was found and pancreatic enzyme replacement therapy resulted in a growth spurt. Enteropeptidase levels in his intestinal mucosa and intraluminal fluid remained very low throughout childhood and early adult life. Celiac disease was confirmed by characteristic abnormalities in tests of intestinal function and in mucosal biopsies, which recovered when he instituted a gluten-free diet. He remains clinically intolerant to gluten as an adult. Enteropeptidase levels have remained abnormally low whether or not his intestinal mucosa has been normal in response to gluten restriction. Enteropeptidase levels have previously been shown to be normal in untreated celiac patients. The relationship between the two disorders remains unclear.

Adult↗
PubMed1985

Plasma lipids and lipoproteins of a patient with cholesteryl ester storage disease.

The plasma lipids, lipoproteins and lipolytic enzymes of a patient suffering from cholesterol ester storage disease were investigated and followed over a time period of 3 years. The patient was hypertriglyceridaemic and cholesterolaemic and exhibited very low levels of high density lipoproteins. These lipoproteins consisted almost exclusively of the HDL-subfraction-3. Apolipoprotein-B was elevated and apoAI and AII were grossly reduced. The activity of lipoprotein lipase was normal, but hepatic lipase values were increased. Lecithin: cholesterol acyltransferase was in the upper normal range. The corresponding lipoprotein and enzyme values of one brother were within normal limits but some components measured in the plasma of the father were abnormal. It is speculated that the low plasma HDL levels in this disease may be a consequence of increased hepatic lipase activity in addition to a derangement in the reverse cholesterol flow.

Adolescent↗
PubMed1982

Distribution of human adult lactase phenotypes in the population of Austria.

A total of 528 unrelated, apparently healthy, adult and adolescent Austrians (270 females, 258 males, mean age 22.1 years) were examined for lactose absorption capacity employing a noninvasive field test based on breath hydrogen (H2) determination. Subjects exhibiting a change of breath hydrogen concentration of less than 15 volumes per million (vpm) after a load of 50 g lactose (n = 422) were classified as lactose absorbers, 106 probands (20.1%) showing increases of breath hydrogen concentration between 16 and 111 vpm were diagnosed as lactose malabsorbers. The distribution of the lactase phenotypes was independent of age and sex. Intolerance symptoms after lactose administration were significantly more frequent in lactose malabsorbers. Grouping of probands according to the birth-places of their grandparents revealed significant differences in the distribution of the lactase phenotypes in East and West Austria (East 25%, West 15% lactose malabsorbers). These differences are discussed in the light of the population history of these regions.

Adolescent↗
PubMed1980

The application of a new synthetic substrate to the determination of enteropeptidase in rat small intestine and human intestinal biopsies.

The application of a new synthetic substrate to the direct determination of enteropeptidase is described. The substrate Gly-(L-Asp)4-L-Lys-2-naphthylamide contains the amino acid sequence of the activation peptides of trypsinogen linked via an amide bond to the fluorophore 2-naphthylamine. The sequence of amino acids is responsible for the specificity and substrate recognition of the enteropeptidase-catalyzed activation of trypsinogen. Interference in the assay by trypsin is prevented by the addition of soybean trypsin inhibitor to the substrate solution. The fluorimetric determination of the liberated 2-naphthylamine allows the direct observation of the reaction kinetics. For the hyrolysis of the synthetic substrate by purified enteropeptidase the pH optimum was 8.2 and the Km 0.17 mmol/l. The new substrate was used to determine the distribution of enteropeptidase along the rat small intestine and also to measure enteropeptidase activity in human intestinal biopsies.

2-Naphthylamine↗
PubMed1980

Enhanced adenosine 3':5' - monophosphate response to beta-adrenergic stimulation in cystic fibrosis fibroblasts after removal of conditioned medium.

Skin fibroblasts derived from 6 patients with cystic fibrosis (CF), 1-6 months old, and from 6 age matched donors were investigated for their ability to accumulate cyclic adenosine 3':5'-monophosphate (c-AMP) in response to isoproterenol and prostaglandin E1 (PGE1) using strictly defined culture conditions. In order to obtain, as far as possible, constant protein content and cell number, cultures were synchronized in the early G1 phase of the cell cycle by growing them in serum free medium before adding stimulating drugs. There were no statistically significant differences both in basal c-AMP or after incubation with theophylline alone. When cultures were thoroughly washed prior to stimulation, c-AMP accumulation in response to isoproterenol was consistently higher (p less than 0.001) in CF than in normal fibroblasts, whereas response to PGE, did not differ significantly. This difference in response cannot be attributed to differences in dose- or time-response curves, or to differential escape of cAMP into the culture medium. Returning the conditioned media (CM) to the cultures after the washing procedure, or omitting the washing procedure altogether, normalized the cAMP response of CF cells. These data indicate that CF fibroblasts "delete" or "add to" the conditioned medium a substance when washed out of the cultures leave the cells hypersensitized to beta-adrenergic stimulation.

Cells, Cultured↗
PubMed1979

Turnover studies of human intestinal brush border membrane glycoproteins in organ culture.

Turnover in organ culture of human small intestinal membrane glycoproteins was measured by the pulse-chase technique, using 14C-glucosamine, 14C-fucose or 14C-leucine as tracers. Apparently, low degradation rates were found for the major high-molecular-weight proteins which co-migrated on SDS-polyacrylamide gels with maltase-glucoamylase, lactase-phlorizin-hydrolase and sucrase-isomaltase enzymic activities. In contrast, an unidentified glycoprotein appearing on gels next to alkaline phosphatase exhibited a higher degradation rate with an apparent half-life of about 30 h, this being similar to the half-life of total glycoprotein as measured in mucosal homogenates. The results obtained with the pulse-chase technique were confirmed by double isotope experiments using 14C-leucine and 3H-leucine as tracers. These findings indicate that in organ culture there is a low basic turnover of human intestinal membrane glycoproteins which co-migrate on gels with known glycosidase enzymic activities.

Cell Membrane↗
PubMed1978

A micromethod for separation and identification of digestive enzymes in brush border membrane fragments of single human intestinal biopsies.

A micromethod for the isolation of brush border membrane fragments from single peroral duodenal biopsies, and their subsequent analysis by polyacrylamide gel electrophoresis is described. The quantity of biopsy material used varied between 5 and 15 mg wet weight, leaving enough mucosa for histological examination. By cutting the gels longitudinally into two halves it was possible to identify several maltases, sucrase, isomaltase and lactase and to correlate these enzymatic activities with distinct co-migrating protein peaks. For alkaline phosphatase and enterokinase this correlation was not possible. This method is suitable for the study on single biopsies of the molecular alterations occurring in the various congenital enzyme deficiencies of the human small intestine.

Cell Membrane↗
PubMed1978

Relative underweight in cystic fibrosis and its prognostic value.

On the basis of observations in 117 children with cystic fibrosis, seen from January 1956 to June 1976, it is demonstrated that the relative underweight (weight loss corrected for height) is most pronounced in children with predominantly pulmonary sypmtoms. The degree of underweight closely correlates inversely with survival. Because of its prognostic value, it is recommended that this clinical parameter be included in the checkups which are periodically carried out on children suffering from cystic fibrosis.

Body Weight↗
PubMed1978

Value of 1-hour blood-xylose test in diagnosis of childhood coeliac disease.

In a series of 46 children with untreated coeliac disease and in 102 controls with normal mucosa the 1-hour blood-xylose test was, in view of its simplicity, of much value in the diagnosis of childhood coeliac disease. Only one blood-xylose result was falsely normal in the 46 coeliac patients. It is concluded that a normal blood-xylose value does not exclude coeliac disease and should not prevent peroral biopsy in the presence of strong clinical suspicion. On the other hand, patients who have repeatedly abnormal blood-xylose values merit an intestinal biopsy even in the absence of suggestive clinical symptoms.

Adolescent↗
PubMed1978

One-hour blood-xylose in cystic fibrosis.

One-hour blood-xylose concentrations after an oral xylose load were measured in children with cystic fibrosis (CF) and healthy controls. The mean of the 1-hour blood-xylose values was significantly increased in the group with CF. The finding confirms an earlier observation by Rolles et al. (1973). Its significance is not at present understood but it suggests that small intestinal function should be further investigated in CF.

Adolescent↗
PubMed1978

Re-evaluation of the techique of organ culture for studying gluten toxicity in coeliac disease.

In vitro cytotoxicity of four different gluten fractions was tested in organ culture for up to 48 hours using flat intestinal biopsies from children with coeliac disease. The fractions were (1) a peptic-tryptic digest of gliadin containing a moderate amount of alpha-gliadin, (2) a peptic-tryptic digest of gluten (Frazer fraction III) froma strain of wheat with a high content of alpha-gliadin, (3) alpha-gliadin, and (4) alpha-GT-18,000, a tryptic fragment of alpha-gliadin. The latter three fractions were toxic to coeliac patients in vivo. In vitro, however, none of these fractions proved to be cytotoxic. When added to the culture medium they were not capable of inhibiting the regeneration of the surface epithelium as visualised by histology and electron microscopy. The only difference between cultures with and without gluten fractions was that the former produced slightly more mucus when maintained in vitro as observed in the dissecting microscope. Furthermore, for Frazer fraction III the absence of apparent toxicity was confirmed by the behaviour of brush border enzyme activities during culture. Our results are not in accordance with those reported in the literature. We believe that the criteria used at the present time for the assessment of gluten toxicity in vitro should be extended to include the process of enterocyte desquamation.

Celiac Disease↗
PubMed1978

Protein-losing enteropathy due to segmental erosive and ulcerative intestinal disease cured by limited resection of the bowel.

Two children suffering from extensive intestinal protein loss due to subacute and chronic segmental small bowel disease are presented. In the first case a tentative diagnosis of chronic erosive and ulcerative non-granulomatous jejunitis as described in adults was made. The second child suffered from subacute erosive and ulcerative segmental transmural ileitis following mechanical ileus. In both instances resection of the involved segments of small intestine promptly cured the enteric protein loss. It is suggested that excessive protein loss due to subacute or chronic segmental erosive and ulcerative intestinal disease may be cured definitively by surgical resection. An explorative laparotomy should be performed if broad internistic investigations do not provide an explanation for the severe and prolonged enteric protein loss.

Adolescent↗