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Biomedical subjects

M Hess

Publications and source records attributed to M Hess.

At least 163 records · Page 9Linked to original sources

Long-term oral administration of amrinone for congestive heart failure: lack of efficacy in a multicenter controlled trial.

A number of uncontrolled studies have indicated that oral administration of amrinone, a phosphodiesterase inhibitor with potent positive inotropic effects in experimental preparations, may be beneficial in patients with chronic congestive heart failure. The present multicenter trial was designed to prospectively evaluate clinical response and change in exercise tolerance during 12 weeks of amrinone therapy in a double-blind, placebo-controlled protocol. Ninety-nine patients with NYHA functional class 3 or 4 congestive heart failure on digitalis and diuretics, of whom 31 were also receiving captopril, were enrolled. After baseline clinical assessment and determination of exercise tolerance, radionuclide left ventricular ejection fraction, and roentgenographic cardiothoracic ratio, patients were randomly assigned to receive amrinone or placebo, beginning at 1.5 mg/kg tid and increasing to a maximum dosage of 200 mg tid. After 12 weeks of therapy or at the last blinded evaluation in patients who did not complete this protocol, there were no significant differences from baseline values between treatment with amrinone or placebo with regard to symptoms, NYHA functional class, left ventricular ejection fraction, cardiothoracic ratio, frequency and severity of ventricular ectopy, or mortality. Exercise tolerance improved significantly from baseline by 37 +/- 10% (mean 163 sec) in patients on amrinone and 35 +/- 11% (mean 149 sec) in patients on placebo, but there was no significant difference between treatments. Adverse reactions were significantly more frequent and more severe on amrinone, occurring in 83% of patients and necessitating withdrawal in 34%.(ABSTRACT TRUNCATED AT 250 WORDS)

Administration, Oral↗

Bone mineral status in childhood accidental fractures.

We studied the bone mineral and calcium (Ca) status of 17 children who suffered an accidental fracture in 1980. These children were matched by age and sex to a nonfractured control group. Blood was drawn for serum Ca, phosphorus, magnesium, 25-hydroxycholecalciferol ( calcidiol ), alkaline phosphatase, and albumin. Bone mineral content (BMC) was evaluated by photon absorptiometry. There were no differences in serum values between the two groups. Twelve (71%) of the 17 children in the fracture group had a lower BMC than their matched controls. The BMC of the fracture group was lower than their controls, 0.423 +/- 0.042 v 0.461 +/- 0.037 g/cm. Four of the 15 in the fracture group ingested less than 60% of the recommended dietary allowance (RDA) for Ca and P (800 mg/day), while all the controls were ingesting at least 60% of the RDA. Four children of the fracture group who were ingesting less Ca and P than those of the control group also had low BMC.

Alkaline Phosphatase↗

Immunohistochemical localization of alcohol dehydrogenase in human kidney, endocrine organs and brain.

Antibodies against human liver alcohol dehydrogenase (ADH) were produced in rabbits. Peroxidase-labeled protein-A with diaminobenzidine as substrate was used to detect anti-ADH binding in human tissue thin sections. In the kidney, ADH was localized in the epithelia of the tubuli; glomeruli and collecting tubules appeared negative. In prostata and epididymis, the epithelia stained strongly. In the testes, the seminiferous epithelium and the Leydig cells stained higher in the cortex than in the medulla. In the pancreas, the Langerhans islets exhibited particularly high ADH concentrations. In the brain, ADH was localized in neurons of the cerebral cortex, hypothalamus, infundibular stalk of the pituitary, and Purkinje cells of the cerebellum. In summary, ADH could be localized primarily in cells known as targets of ethanol toxicity.

Adrenal Glands↗

Immunohistochemical localization of alcohol dehydrogenase in the human gastrointestinal tract.

To elucidate the possible role of alcohol dehydrogenase in the generation of damages caused by alcohol abuse, it is important to know the exact localization of this enzyme. Anti-alcohol dehydrogenase antibodies were used to localize the enzyme in human gastrointestinal tissues. Alcohol dehydrogenase was detectable in the mucosa of all parts of the gastrointestinal tract. There is a notable decrease in the amount of alcohol dehydrogenase with increasing distance from the stomach. In the stomach, the reaction for alcohol dehydrogenase was strongest in the mucus-producing cells, moderate in the parietal cells, and weak in the chief cells. Throughout the gut, alcohol dehydrogenase was present in cells exposed to the lumen in amounts comparable to that of the parietal cells. Crypt cells and goblet cells were negative. The results strongly indicate that alcohol dehydrogenase is an intrinsic component of gastrointestinal epithelial cells.

Alcohol Oxidoreductases↗

Immunohistochemical evidence for cell surface and Golgi localization of galactosyltransferase in human stomach, jejunum, liver and pancreas.

Immunohistochemical localization of galactosyltransferase (UDP-galactose: 2-acetamido-2-deoxy beta-D-glucopyranose beta (1-4) transferase) in human tissue specimens of gastric and jejunal mucosa, exocrine pancreas, and liver was carried out at the light microscopic level using affinity purified rabbit anti-human milk galactosyltransferase antibodies. Intracellular localization of galactosyltransferase in epithelial cells appeared as a triangular compact structure close to the apical pole of the nucleus. In hepatocytes, the enzyme was found in discrete spots in the cytoplasm between the nuclei and the bile canaliculi. In addition to the intracellular, juxtanuclear location an intense reaction at the luminal part of the cell surface was found in the lining epithelium of the stomach, in enterocytes of the jejunal villus tips, and in ductular cells of the pancreas. Enterocytes located in the middle portion along the cryptvillus gradient exhibited cytoplasmic staining adjacent to the brush borders. Basolateral membranes appeared negative. Little or no enzyme could be demonstrated in cells belonging to the connective tissue. These results show that secretory cells contain a Golgi apparatus which can be visualized at the light microscopic level by virtue of its content in galactosyltransferase. Presence of galactosyltransferase antigen on the surface of certain cells supports the assumption that ectoglycosyltransferases do exist, at sites, however, apparently not involved in cell contact and adhesion.

Cell Membrane↗

Immunohistochemical localization of human liver alcohol dehydrogenase in liver tissue, cultured fibroblasts, and HeLa cells.

Human liver alcohol dehydrogenase (ADH, EC 1.1.1.1) was purified by double ternary complex affinity chromatography on Sepharose-4-(3-[N-6 aminocaproyl]aminopropyl) pyrazole. The purified enzyme preparation still contains several isoenzymes reflecting the isoenzyme composition of the starting material. Antibodies against this mixture of isoenzymes were elicited in rabbits. The specificity of the antiserum was tested by double immunodiffusion, enzyme-linked immunosorbent assay, immunoprecipitation of ADH enzymatic activity, and adsorption to ADH, which was immobilized to Ultrogel AcA 44 by the use of glutardialdehyde as the coupling agent. Protein-A peroxidase with diaminobenzidine or amino ethyl carbazole as substrate, served to detect binding of anti-human liver ADH antibodies in human liver thin sections, cultured human skin and lung fibroblasts, and HeLa cells. Fluorescein-conjugated antibodies were also used in direct immunofluorescence on liver tissue. In the human liver, ADH was found to be localized in the cytoplasm of hepatocytes. Differences in the staining intensity of hepatocytes may reflect differences in ADH content. Strongly stained hepatocytes were localized mainly around the central veins. Perinuclear staining is often seen, especially in the more lightly stained cells. Human skin and lung fibroblasts, as well as HeLa cells, all exhibited positive staining for ADH. The pattern was identical to that found in hepatocytes, although the staining intensity was much weaker, indicating a lower ADH content.

Alcohol Oxidoreductases↗

[Plasma exchange in pemphigus vulgaris].

An attempt to treat a patient with pemphigus vulgaris by large volume plasma exchange with intravenous application of high doses of immunoglobulin at the end of each exchange procedure is reported. The therapeutic results--temporary clinical improvement parallel to a significant reduction in the level of circulating antiepithelial autoantibodies--are discussed in comparison with published case reports on plasma exchange in pemphigus vulgaris and bullous pemphigoid.

Autoantibodies↗

Successful orthotopic canine heart transplantation after 24 hours of in vitro preservation.

A protocol was developed to provide continuous, hypothermic, low-pressure perfusion for 24 hours' preservation of the isolated canine heart prior to orthotopic transplantation. Donor cardiectomy included coronary vasodilatation with diltiazem, potassium arrest, and rapid cooling of the heart. The graft was perfused at a pressure of 18 to 22 cm H2O and at an average flow of 0.743 cc/min/gm of tissue. The septal temperature was 5 degrees to 7 degrees C and perfusate pH was 7.25 to 7.4. Two groups of mongrel dogs were studied after orthotopic transplantation: Group I (n = 15) received hearts perfused for 24 hours. Group II (n = 9) received hearts removed by the same cardiectomy technique, but transplanted immediately. All grafts were able to support the recipient circulation after cardiopulmonary bypass. These was no significant difference in survival or in graft function when hemodynamic studies were done in five animals of each group, between 5 and 10 days after operation. We conclude that a reliable and reproducible method of 24 hours' in vitro perfusion of the canine heart has been obtained and should be applicable in clinical cardiac transplantation when prolonged periods of preservation are required.

Animals↗

[Specific characteristics of hairy cell leukemia].

Report on a now 58-year-old female patient who presented in 1969 with the following objective findings: anemia, thrombocytopenia, lymphocytosis and hepatosplenomegaly. The first first diagnosis was lymphosarcoma, but up to 1976 nearly ten other diagnoses were established, e.g. reticulum sarcoma, leukemic lymphosarcoma, CML, ALL, CLL and Waldenström's disease. The patient did not respond to combined chemotherapy, but splenectomy brought about significant improvement in anemia and thrombocytopenia. She is now doing well without cytotoxic treatment. Hairy cell leukemia was diagnosed on the basis of electron microscopic findings in peripheral lymphocytes and histologic findings in bone marrow and spleen. The tartrate-resistant acid phosphatase was positive. Immunologic tests in the hairy cells showed surface immunoglobulins of monoclonal origina and the T-cells were shown to be decreased. The tests for phagocytosis and nonspecific esterase were negative. The hairy cells in this patient exhibited no colony stimulating activity in culture studies with bone marrow from 4 normal donors, as compared with the stimulating activity of normal monocytes in the same assay. In the light of this case report the question is discussed whether the hairy cells are mainly cells with lymphocytic (B-lymphocytes) or monocytic characteristics. On this question the findings in our patient support the hypothesis of a B-cell nature for the hairy cells.

Acid Phosphatase↗