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Biomedical subjects

J D Faulhaber

Publications and source records attributed to J D Faulhaber.

At least 19 recordsLinked to original sources
PubMed1984

[Dissolution of recurrent stones in the choledochus by a modified irrigation treatment via an indwelling nasobiliary catheter].

Alternating fluid rinsing with a modified glyceromono-octanoate (GMOC) and bile salt-EDTA (BA-EDTA) solution via an endoscopically placed indwelling nasal biliary catheter was performed on 15 patients (13 women, 2 men) with recurrent stones in the choledochal duct after cholecystectomy. Of 12 radiotranslucent and three radioopaque concrements with a mean diameter of 1.72 X 2.05 cm (largest concrement: 3.0 X 3.5, smallest 1.0 X 2.1 cm) 13 were dissolved (87% success rate). In one patient chemolitholysis had to be stopped because of electrolyte abnormalities, before treatment had been completed. After the end of treatment all patients were free of symptoms and during a fairly long follow-up period no stone recurrences were observed.

Aged↗
PubMed1983

An ABO-blood group abnormality leading to the detection of a colon-carcinoma.

A patient who had been admitted to hospital for surgical treatment of inguinal hernias was found to have group phenotype of A1B in the presence of a non-auto-anti-B. No previous records of the patient's blood group were available. The serological workup including absorption and saliva inhibition studies yielded a high probability for an acquired B-antigen which is known to be often associated with carcinoma of the colon. Subsequent coloscopy revealed the presence of a carcinoma of the sigmoid, unaccessable to palpation. To our knowledge this is the first report in the literature that the serological diagnosis of an acquired B-antigen led to the detection of a hitherto undetected carcinoma.

ABO Blood-Group System↗
PubMed1981

Characterization of beta-adrenergic receptors by (3H) isoproterenol in adipocytes of humans and rats.

The specific binding of (3H) isoproterenol to isolated fat cells of human and rat was characterized. Binding of (3H) isoproterenol to isolated fat cells of rat was saturable with 420 pmol of (3H) isoproterenol bound/100 mg of lipid. Half-maximal saturation occurred at 5 microM providing an estimate of the equilibrium dissociation constant, KD, for the interaction of (3H) isoproterenol with its binding sites. Kinetic analysis of (3H) isoproterenol binding provided a value of 2.01 x 10(4) min-1. M-1 for the forward bimolecular rate constant, k1. Dissociation of (3H) isoproterenol was a first order reaction with a rate constant, k2, of 0.62 x 10(-1) min-1. The ratio k2/k1 = 3.07 microM provides an independent measurement of the KD for the interaction of (3H) isoproterenol with its binding sites which is in agreement with the values obtained by steady state analysis (3 to 5 microM). The apparent equilibrium dissociation constant, KD, for the interaction of (3H) isoproterenol with its receptor in human fat cells obtained by steady state analysis was 1 to 0.9 microM. Scatchard- and Hill-analysis suggest the possibility of different negatively cooperative interactions among the binding sites in human and rat. beta-Adrenergic agonists competed for the binding sites. The order of potency was isoproterenol greater than epinephrine greater than norepinephrine. Compounds such as DOPA, dopamine and (m-Hydroxyphenyl)2-methyl-aminoethanol which are structurally related to catecholamines had little or no affinity for (3H) isoproterenol binding sites.

Adipose Tissue↗
PubMed1981

Thyroid hormone effects on beta-adrenergic receptors in isolated fat cells in rats.

The effect of thyroid hormones (thyroxine and triiodothyronine) on catecholamine receptors in isolated rat fat cells was investigated. Binding of (3H)isoproterenol and (3H)norepinephrine were increased by thyroid hormones. (3H)isoproterenol binding was more enhanced than (3H)norepinephrine binding. Triiodothyronine had a more potent effect than thyroxine. (3H)isoproterenol was used to estimate the number or affinity of beta-adrenergic receptors in rat fat cells treated with thyroid hormones. The binding sites for (3H)isoproterenol were the same in untreated and with triiodothyronine treated fat cells. The equilibrium dissociation constants (KD) for the interaction of receptors with (3H)isoproterenol were altered in thyroid hormone treated cells. There was a significant difference between the untreated and triiodothyronine treated fat cells in the affinity of beta-adrenergic receptor binding sites for (3H)isoproterenol. Thyroid hormone could alter negative cooperative site-to-site interaction among the binding sites for (3H)isoproterenol.

Adipose Tissue↗
PubMed1980

Thyroid hormone stimulation of lipolysis and cyclic adenosine 3', 5'-monophosphate accumulation in human adipose tissue.

The role of thyroid hormones on lipolysis in human subcutaneous adipose tissue was investigated. Incubation of subcutaneous fat pads with thyroxine (0.1--10 000 nM) augmented the subsequent isoproterenol stimulation of lipolysis, measured by glycerol release. The basal lipolysis could not by stimulated by thyroxine. The theophylline- and dibutyryl-cyclic AMP stimulated lipolysis also could not be increased by thyroxine at these concentrations. In separate studies, the effect of thyroxine (0.01 pM--1 microM) and triiodothyronine (0.01 pM--1 microM) on cyclic AMP accumulation was examined. No effect of thyroid hormones on cyclic AMP accumulation was seen in non-isoproterenol stimulated tissue. Fat pads stimulated by isoproterenol and then treated with thyroid hormones showed marked increases in accumulation of cyclic AMP as compared to control tissue in the presence of isoproterenol alone.

Adipose Tissue↗
PubMed1980

Calciotropic hormones and lipolysis of human adipose tissue: role of extracellular calcium as conditioning but not regulating factor.

The influences of different calcium concentrations (0, 0.924 and 2.772 mMol/l) on lipolysis of in vitro incubated human adipose tissue slices or adipocytes were studied under the conditions of stimulation with isoproterenol and parathyroid hormone preparations or inhibition by insulin. Extractive bovine PTH (as well as synthetic PTH 1--34) stimulated glycerol release in a biphasic pattern similarly to isoproterenol; PTH was about half as potent as isoproterenol. The optimal conditions for lipolysis were observed using a calcium concentration of 0.924 mMol/l, whereas lipolysis was distinctly impaired at concentrations of 0 or 2.772 mMol/l; this was true for basal as well as isoproterenol- and PTH stimulated lipolysis or the inhibitory effect of insulin. In contrast to partially purified extractive calcitonin, pure synthetic calcitonin did not inhibit lipolysis. Isoproterenol- and PTH-administrations led to cAMP accumulation in the adipose tissue, this process was also diminished at the non-optimal calcium concentrations. The results suggest a conditioning, but not a regulating significance of extracellular calcium for lipolysis, whereas the importance of the lipolytic potency of PTH remains to be elucidated.

Adipose Tissue↗
PubMed1972

New device for preparing thin slices of adipose tissue for metabolic studies in vitro.

A new microtome is described which allows the rapid preparation of equal slices of well-defined thickness of fresh human tissue, especially adipose tissue. Presetting the microtome for a section thickness of 500 micro m, we found a variation of about 5% with human adipose tissue. Slices of human adipose tissue sliced by the microtome showed a higher sensitivity to insulin and a better reproducibility of results than slices prepared freehand.

Adipose Tissue↗