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Biomedical subjects

W H Taylor

Publications and source records attributed to W H Taylor.

At least 37 records · Page 2Linked to original sources
PubMed1988

The effect of dopamine on renal function during aortic cross clamping.

Eighteen male patients undergoing elective surgical reconstruction of the abdominal aorta were divided into two groups. Patients in Group I (nine) were given dopamine intravenously, in a dose of 2 micrograms/kg/min, during the first half of the period of cross-clamping, whilst those in Group II received dopamine during the second half. Each patient acted as his own control and for each, three periods were examined, namely: pre-clamp, clamping with dopamine and clamping without dopamine. Dopamine infusion during aortic clamping caused a significant rise in sodium output (P less than 0.01), potassium output (P less than 0.05), creatinine clearance (P less than 0.05) and urine output (P less than 0.05). We conclude that dopamine infusion during aortic clamping helps to protect the kidney from any deleterious effect of clamping.

Aged↗
PubMed1987

Inhibition of chondroitin and heparan sulfate biosynthesis in Chinese hamster ovary cell mutants defective in galactosyltransferase I.

We have isolated five Chinese hamster ovary cell mutants defective in galactosyltransferase I (UDP-D-galactose:xylose beta-1,4-D-galactosyltransferase) and studied the effect of p-nitrophenyl-beta-D-xyloside supplementation on glycosaminoglycan biosynthesis in the mutant cells. Assays of galactosyltransferase I showed that the mutants contained less than 2% of the enzyme activity present in wild-type cells, and enzyme activity was additive in mixtures of mutant and wild-type cell extracts, suggesting that the mutations most likely defined the structural gene encoding the enzyme. Cell hybridization studies showed that the mutations in all five strains were recessive and that the mutants belonged to the same complementation group. The mutants contained wild-type levels of xylosyltransferase (UDP-D-xylose:core protein (serine) beta-D-xylosyltransferase), lactose synthase (UDP-D-galactose:N-acetyl-glucosaminide beta-1,4-D-galactosyltransferase), and lactosylceramide synthase (UDP-D-galactose:glucosylceramide beta-1,4-D-galactosyltransferase). Their sensitivity to lectin-mediated cytotoxicity was virtually identical to that of the wild-type, indicating that there were no gross alterations in glycoprotein or glycolipid compositions. Anion-exchange high performance liquid chromatography of 35S-glycosaminoglycans from one of the galactosyltransferase I-deficient mutants showed a dramatic reduction in both heparan sulfate and chondroitin sulfate, demonstrating that galactosyltransferase I is responsible for the formation of both glycosaminoglycans in intact cells. Surprisingly, the addition of 1 mM-p-nitrophenyl-beta-D-xyloside, a substrate for galactosyltransferase I, restored glycosaminoglycan synthesis in mutant cells. This finding suggested that another galactosyltransferase, possibly lactose synthase, can transfer galactose to xylose in intact cells.

Animals↗
PubMed1987

Interference in the measurement of red cell glycogen by glycogen from white cells.

An enzymatic method for determining red cell glycogen was developed and its recovery and precision ascertained. Initial red cell glycogen values in 24 healthy volunteers ranged from 11-60 micrograms/g haemoglobin which compares with 20-105 micrograms/g haemoglobin previously reported. More thorough removal of leucocytes suggested however that variations in the determined red cell glycogen were due to glycogen derived from leucocytes. In 34 red cell preparations with varying leucocyte numbers, the glycogen concentration correlated positively with leucocyte count (r = +0.81, p less than 0.001), whereas glycogen concentration showed poor correlation with red cell count (r = -0.30, 0.1 greater than p greater than 0.05). The results question the reported presence of glycogen in normal red cells and suggest that contamination by leucocytes has been responsible for the previously reported normal range.

Erythrocytes↗
PubMed1987

A general method for cloning DNA fragments in multiple copies.

A general method for the cloning of DNA fragments in tandem arrays is presented. Synthetic directional adapters are attached to the fragment ends to establish complete control over fragment orientation during ligation. Use of these directional adapters thereby ensures the production of direct repeats, an arrangement essential for clone stability. The technique involves a protocol that is both less complex and less time-consuming than previous methods. Using this technique, a 10-min ligation has yielded a plasmid containing 20 copies of a 151-bp fragment.

Cloning, Molecular↗
PubMed1987

Determination of iron in cardiac and liver tissues by plasma emission spectroscopy.

A simple plasma emission spectroscopic method for the determination of iron in liver and cardiac tissue is described. Using this technique, iron was extracted quantitatively from liver tissue of mass 14.2 to 65.4 mg wet weight, and heart tissue of mass 5.9 to 27.4 mg wet weight. Iron added to liver as aqueous ferric nitrate was recovered in the range 93 to 108%. Reference ranges for liver and myocardial iron on post mortem tissue gave respectively mean values of 0.841 mg/g dry weight (Range 0.310 to 1.600, n = 37) and 0.340 mg/g dry weight (Range 0.290 to 0.470, n = 8). Data on patients with haemochromatosis and transfusion siderosis are also presented.

Aged↗
PubMed1987

An investigation of possible risk factors associated with gastric cancer after benign ulcer operations.

The risk of developing gastric cancer has been investigated in a case-control study and in a prospective investigation. In the case-control study, 1495 cases of gastric cancer were identified in five city hospitals and matched with autopsy controls from the same hospitals. The frequency of operations for benign ulcer [partial gastrectomy (PG) and gastroenterostomy] was similar in the two groups. Thus, there was no increased risk for late gastric cancer after an ulcer operation. A total of 140 operated ulcer subjects [80 truncal vagotomy and drainage (TVD), 60 PG and 78 nonoperated cases attending with dyspepsia (C)] were examined by endoscopy, multiple gastric biopsy and analysis of gastric juice for nitrite. Biopsies were graded for gastritis and a gastritis index was derived (normal, 1; superficial gastritis, 2; chronic atrophic gastritis: mild, 3; moderate, 4; severe, 5). More atrophic gastritis was found in operated subjects than in controls: TVD, 2.3 +/- 0.08 (mean +/- SE); PG, 2.6 +/- 0.1 versus C, 1.8 +/- 0.08, p less than 0.01. The severity of atrophic gastritis increased after an operation interval of 20 years in PG subjects (p less than 0.05). Intestinal metaplasia was a common change, but unequivocal epithelial dysplasia was not observed. Two cases of operated stomach cancer were found. High levels of nitrite were positively correlated with pH and a high gastritis index. This evidence does not suggest that ulcer surgery leads to either an increased risk of cancer or a precancerous condition.

Gastrectomy↗
PubMed1986

Sulfate transport-deficient mutants of Chinese hamster ovary cells. Sulfation of glycosaminoglycans dependent on cysteine.

We isolated 59 Chinese hamster ovary cell mutants defective in 35SO4 incorporation into glycosaminoglycans. Thirty-five mutants incorporated [6-3H]glucosamine into glycosaminoglycans normally, suggesting that they were specifically impaired in sulfate incorporation. Cell hybridization studies revealed that the 35 mutants defined a unique complementation group. Pulse-labeling one of the mutants with 35SO4 showed that it possessed a defect in a saturable, 4-acetamido-4-isothiocyanostilbene-2,2'-disulfonic acid-sensitive transport system required for sulfate uptake. Despite the dramatic reduction in 35SO4 incorporation, the mutant synthesized sulfated heparan and chondroitin chains. Incubation of the mutant with [35S]cysteine resulted in the formation of 35SO4, which was subsequently incorporated into the glycosaminoglycans. Similar results were obtained when wild-type cells were incubated in sulfate-free growth medium containing [35S]cysteine, and isotope dilution analysis indicated that about 15 microM of sulfate was derived from cysteine catabolism. We also found that the sulfate transport deficiency rendered the mutant resistant to 5 microM sodium chromate, whereas wild-type cells did not divide under these conditions. However, the mutant also did not proliferate in medium containing 5 microM chromate when grown in the presence of wild-type cells, suggesting that chromate was transported through cell-cell contacts. Since co-cultivating sulfate transport-deficient mutants with mutants defective in xylosyltransferase or galactosyltransferase I partially restored 35SO4 incorporation into glycosaminoglycans, intercellular sulfate transport occurred as well. Therefore, the availability of sulfate for glycosaminoglycan synthesis depends on sulfate uptake, turnover of sulfur-containing amino acids, and sulfate transport between cells.

Animals↗
PubMed1986

Mucus degradation by pepsin: comparison of mucolytic activity of human pepsin 1 and pepsin 3: implications in peptic ulceration.

The ability to digest mucus, mucolytic activity of isolated pepsins and samples of human gastric juice has been assayed by measuring the fall in viscosity when incubated with purified pig gastric mucus glycoprotein. Pure human pepsin 1, the peptic ulcer associated pepsin, digested gastric mucus glycoprotein at a faster rate than did pure human pepsin 3 (the principal human pepsin), or the equivalent pig pepsin (pepsin A). At pH 2.0 pepsin 1 had twice the mucolytic activity of pepsin 3. Above pH 3.8 this difference became more marked and whereas pepsin 1 caused substantial mucolysis up to and including pH 5.1, pepsin 3 had minimal activity. At pH 4.0 pepsin 1 had six times the mucolytic activity of pepsin 3. Gastric juices from patients with duodenal ulcer each exhibited substantial mucolytic activity between pH 2 to 5, similar to that of pepsin 1. In contrast, gastric juice from non-symptomatic volunteers exhibited little mucolytic activity above pH 4. Analysis of the mucus glycoprotein by gel filtration showed that an increase in lower molecular weight, pepsin degraded, glycoprotein was associated with the fall in mucus viscosity for all enzyme preparations. These results showed that pepsin 1 can digest the mucus more effectively than pepsin 3 and at higher pH values. The raised concentrations of pepsin 1 in the juice of peptic ulcer patients may thus promote the ulcerative process by increased erosion of the mucus barrier under conditions likely to pertain in the duodenal bulb as well as the stomach.

Chromatography, Gel↗
PubMed1986

Limits to parathyroid imaging with thallium-201 confirmed by tissue uptake and phantom studies.

Correct location by 201TI imaging of 48 parathyroids in 35 patients was related to size; 25 out of 26 parathyroids of mass greater than 1.0 g were correctly located, none of ten parathyroids less than 0.3 g was correctly located. In seven patients previously imaged, 108 microCi (4.0 MBq) of 201TI was injected when the thyroid was first exposed surgically. Subsequently weighed and histologically confirmed samples of parathyroid, thyroid, and skeletal muscle were counted against a standard in a well counter. Thallium-201 uptake, as %/g, did not differ between hyperplastic and adenomatous parathyroids. Mean parathyroid uptake was 0.018%/g, thyroid 0.01%/g, muscle 0.0026%/g of administered dose. Lower limits for correct location lay between 0.006-0.0149% of administered dose and between 0.25-0.8 g. Studies using a 201TI phantom containing small aliquots of 201TI at higher concentrations suggested approximately 0.0075% of the usual patient imaging dose as a lower limit for correct location.

Adenoma↗
PubMed1985

Animal cell mutants defective in glycosaminoglycan biosynthesis.

We have obtained Chinese hamster ovary cell mutants defective in the biosynthesis of glycosaminoglycans by screening replicate colonies immobilized on polyester cloth. Depending upon the strain, the mutants accumulated less 35S-labeled glycosaminoglycans per microgram of cell protein by a factor of 6-60 compared to the wild type. Some of the mutants incorporated [6-3H]glucosamine into glycosaminoglycans to the same extent as the wild type, suggesting that sulfate addition was specifically altered. In contrast, five strains failed to generate 3H-labeled glycosaminoglycans normally. In four of these, the initiation of glycosaminoglycan assembly was specifically altered, since the addition of p-nitrophenyl-beta-xyloside restored sulfation to normal. Enzymatic assay of the xylosyltransferase in extracts prepared from these mutants revealed that one of the strains, S745, contained less enzyme activity by a factor of 15 than the wild type. This mutant provides genetic evidence that the xylosyltransferase assayed in vitro is responsible for the initiation of chondroitin sulfate and heparan sulfate biosynthesis in vivo.

Animals↗
PubMed1985

Localization of enlarged parathyroid glands by thallium-201 and technetium-99m subtraction imaging. Gland mass and parathormone levels in primary hyperparathyroidism.

Twenty-two patients, all with surgically proven primary hyperparathyroidism, were studied by TI-201 thallous chloride and Tc-99m pertechnetate subtraction imaging. Fifteen parathyroid adenomata and one hyperplastic gland between 0.33 and 14.8 g were correctly localized in 16 patients. Two adenomata and seven hyperplastic or histologically normal parathyroids between 0.1 g and 1.4 g in seven patients were not localized. One patient had a correctly localized 13.0-g adenoma with a nonlocalized 0.3 g hyperplastic parathyroid gland and there were two false positive localizations. Sensitivity was 64% (glands), and 73% (patients). There was only fair correlation with parathormone (PTH) levels, but these were elevated in all but four of the patients with correctly localized parathyroids. The authors conclude that the imaging procedure is useful but its sensitivity is limited by difficulty in localizing correctly small glands, particularly those of less than 0.5 g, which comprised 29% of those excised.

Adenoma↗
PubMed1985

Measurement of copper, zinc and magnesium in serum and urine by DC plasma emission spectrometry.

The application of a DC plasma emission spectrometer to the measurement of copper, zinc and magnesium in serum and urine is reported. Each assay requires only a simple dilution in 1% nitric acid. Comparisons with standard atomic absorption techniques showed good analytical agreement, especially for copper and magnesium. Analysis of quality control preparations for copper and zinc gave results ranging from -1.5% to +3.6% of the stated values for five copper and four zinc experiments, with an unexplained result of +7.6% for one zinc experiment. Reference ranges were compiled for serum zinc and urinary copper which agreed closely with those established by atomic absorption and neutron activation analysis. Assays by DC plasma emission are thus precise and reproducible, and simple enough to authenticate the method for use in a clinical laboratory.

Copper↗
PubMed1985

Low serum magnesium concentration in Paget's disease of bone (osteitis deformans).

Approximately 25% of patients presenting with Paget's disease of bone have a low serum magnesium concentration (below 0.74 mmol/L). Metabolic balance studies of 12 normomagnesaemic and seven hypomagnesaemic subjects show that the latter have a significantly more positive balance and a significantly higher net absorption of magnesium than have the former. The urinary output of the two groups did not differ significantly. The serum magnesium and alkaline phosphatase (log) concentrations were significantly negatively correlated, as were the serum magnesium and the daily urinary hydroxyproline (log) output. Low serum magnesium concentrations are thus associated with highly active Paget's disease; they do not arise from increased urinary loss nor from a lowered net absorption of magnesium, but probably from increased uptake by bone. The balance data show that to avoid a negative magnesium balance, the magnesium intake in Paget's disease should be at least 8.0 mmol/day.

Absorption↗