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Biomedical subjects

M Wallis

Publications and source records attributed to M Wallis.

At least 73 records · Page 4Linked to original sources
PubMed1986

Effects of two enkephalin analogues, morphine sulphate, dopamine and naloxone on prolactin secretion from rat anterior pituitary glands in vitro.

Experiments were carried out on the antagonistic effects of opiates on the inhibition by dopamine of prolactin secretion from rat anterior pituitary glands. Dose-response and time-course experiments were carried out using both static incubation of paired hemipituitary glands and perifusion of whole glands. Dopamine (10-1000 nmol/l) was found to have an inhibitory effect on prolactin secretion, but at a lower concentration (0.1 nmol/l) a small stimulation was observed. Against an inhibition established with 100 nmol dopamine/l in static incubation, the three opiates under study, morphine sulphate, Leu5-enkephalin and D-Ala2,Met5-enkephalin (DAME), had a maximum antagonistic effect at 50-1000 nmol/l in a 90-min incubation. Morphine and DAME were rather more effective than Leu5-enkephalin, possibly because of degradation of the latter. Naloxone reversed the effect of morphine. All three opiates showed little effect on dopamine-inhibited prolactin secretion in a perifusion system. The data accord with previous suggestions that prolactin secretion may be stimulated both by very low concentrations of dopamine and by opiates acting to reverse the inhibition exerted by higher dopamine concentrations. It should be noted that both morphine and the enkephalins have similar effects on prolactin secretion, despite their normal specificity for different opiate receptors; their actions on the pituitary may thus be rather non-specific.

Animals↗
PubMed1986

Somatomedin C/insulin-like growth factor I: simplified purification procedure and biological activities of the purified growth factor.

Human somatomedin C has been purified from Cohn fraction IV paste by a simplified procedure using chromatofocusing, hydroxylapatite chromatography and reverse-phase high performance chromatography. The purified material has a specific activity by somatomedin C radioimmunoassay of 9160 units/mg (1 unit is defined as the amount of somatomedin present in 1 ml normal adult male human serum), representing a 650,000-fold purification, and possesses sulphation, mitogenic and insulin-like activities (specific activities of 3388 units/mg, 832 units insulin equivalents/mg and 1122 units/mg respectively). Somatomedin C is shown to be a potent stimulator of DNA synthesis (50% maximum stimulation at 150 fmol/ml) in isolated chondrocytes derived from costal cartilage, a major physiological target tissue.

Amino Acids↗
PubMed1985

Effects of growth hormone-releasing factor and somatostatin on growth hormone secretion and cellular cyclic AMP levels. Cultured ovine and rat anterior pituitary cells show markedly different responses.

Human pancreatic growth hormone-releasing factor (GRF-44-NH2) stimulated growth hormone (GH) secretion and intracellular cyclic AMP levels in cultured pituitary cells from both sheep and rat. Somatostatin (SRIF), over a wide range of doses and time, showed no significant effect on the elevated cyclic AMP levels in sheep cells, but did block the GH release in a dose-dependent manner. In rat cells, however, SRIF inhibited GRF-stimulated cyclic AMP levels by 75% maximum (still 8-fold greater than the basal levels) and GH release to almost half the basal value. We conclude that somatostatin inhibits GRF-elevated cyclic AMP levels in rat pituitary cells but not in sheep cells.

Animals↗
PubMed1985

Pacemaker discomfort induced by the wearing of seat belts.

A survey was made of 100 consecutive pacemaker recipients to examine problems they may have experienced with seat belts whilst travelling by car, either as drivers (29 patients) or front seat passengers (50 patients). Twenty-one per cent of the drivers and 30% of the front seat passengers had experienced symptoms, usually of a mild nature. Re-siting of the generator was only necessary in 1 patient and no example of electrode displacement was observed. Suggestions are made as to how this problem might be overcome.

Adipose Tissue↗
PubMed1984

Effects of growth hormone-releasing factor, somatostatin and dopamine on growth hormone and prolactin secretion from cultured ovine pituitary cells.

A synthetic form of human pancreatic growth hormone releasing factor (GRF-44-NH2) was shown to be a potent stimulator of growth hormone (GH) secretion and cellular cyclic AMP levels in cultured sheep pituitary cells. A small dose-dependent stimulation of prolactin secretion was also observed. Somatostatin (0.5 microM) completely blocked the maximal GRF (1 nM)-stimulated secretion without a significant effect on cyclic AMP levels. Dopamine (0.1 microM) inhibited the GRF-elevated GH secretion by 50% and lowered cyclic AMP levels by 30%. Dopamine (0.1 microM) inhibition of basal prolactin secretion was not affected by GRF (1 nM). The data support the hypothesis that cyclic AMP is involved in the action of GRF but suggest that somatostatin can inhibit GRF-induced secretion of GH independently of cyclic AMP.

Animals↗
PubMed1984

Size heterogeneity of prolactin secreted from and stored in the rat anterior pituitary gland in vitro.

The size heterogeneity of rat pituitary prolactin was investigated using anterior pituitary glands from female rats incubated in vitro and gel filtration on Sephadex G-100. Monomeric prolactin was preferentially secreted compared with dimeric and 'trimeric' material. When glands were incubated with dopamine, prolactin secretion was inhibited and the relative proportion of dimer in the gland (but not the medium) was decreased. Morphine sulphate reversed the effect of dopamine on prolactin secretion and on the proportion of prolactin in the gland that was in the dimeric form. The results suggest that monomeric prolactin is more readily secreted than dimer, and that dopamine decreases the production or stability of the dimer.

Animals↗
PubMed1984

Studies of TRH-induced prolactin secretion and its inhibition by dopamine, using ovine pituitary cells.

Prolactin secretion from ovine pituitary cell cultures was stimulated by thyrotropin-releasing hormone (TRH) (10(-10)-10(-7) M) with a half-maximal effect at approximately 2.5 X 10(-9) M. A maximally effective concentration of TRH produced a peak secretory response, 5-10-fold stimulation over basal release, within 15 min. Dopamine (10(-10)-10(-7) M) but not somatostatin caused a dose-related inhibition of TRH (10(-8) M) stimulated prolactin release. Both dopamine (10(-7) M) and somatostatin (10(-7) M) inhibited basal secretion from the cells. TRH did not significantly increase pituitary cell cyclic AMP levels under any of the conditions tested. Stimulation of prolactin secretion by TRH was not prevented when Ca2+ was omitted from the incubation medium. Dopamine inhibited secretion induced by TRH under low Ca2+ conditions. Our results are consistent with a hypothesis that TRH may stimulate prolactin secretion via release of intracellular Ca2+ rather than increased cellular Ca2+ uptake, and imply that dopamine inhibition involves a lowering of intracellular Ca2+ levels.

Animals↗
PubMed1984

Transport of the surgical neonate.

We have shown that the critically ill neonate may be safely transferred over long distances provided some essential criteria are fulfilled. There are obvious advantages in centralising neonatal surgery in a limited number of regional centres where surgical expertise and adequate support services are concentrated and there seems to be no justification, except in situations of dire emergency, for neonatal surgery to be performed in district general hospitals in the United Kingdom. The fact that neonates requiring surgery can be safely transferred adds strength to the plea for the paediatric surgeon to have an absolute monopoly of surgery in this age group.

Body Temperature↗
PubMed1983

Binding specificity of monoclonal antibodies towards fragments of human growth hormone produced by plasmin digestion.

To help define the immunological epitopes on human growth hormone (hGH), interaction of fragments of the hormone with 7 monoclonal antibodies (McAbs) was studied. Plasmin-digested hGH, containing two peptides (hGH1-134 and hGH141-191) joined by a disulphide bond, bound to each McAb with affinity similar to that of intact hGH. The purified C-terminal fragment, hGH141-191, showed low affinity for each McAb. The N-terminal fragment, hGH1-134, bound with quite high affinity to 2 McAbs (EB1 and EB3) but not to the other 5. We conclude that residues 1-134 of hGH contain the epitope to which McAbs EB1 and EB3 bind.

Amino Acids↗
PubMed1983

Cell-density dependence of the rate of prolactin secretion from perifused rat anterior pituitary cells.

Anterior pituitary glands from female rats were dispersed enzymically in the absence of dopamine. Dispersed cells (10(6)-10(7)) were layered onto columns containing Bio-Gel P-2 and were then perifused for 3 h with Dulbecco's Modified Eagle's Medium. The prolactin content of the perifusate and cell homogenates was determined by radioimmunoassay. Prolactin secretion during the third hour of perifusion increased as the loading of cells increased. However, the increase was not linear, and when secretion rate per 10(6) cells was calculated it was found that increased loading decreased the rate, which fell to a plateau of 1.3 +/- 0.1 (S.E.M.) ng/min per 10(6) cells at a loading of about 8 x 10(6) cells from 3.8 +/- 0.1 ng/min per 10(6) cells for a loading of 10(6) cells. This cell-density dependence of the rate of prolactin secretion in the perifusion system may be due to intercellular contact since the isolation of the tissue removes the influence of hypothalamic factors, while localized build up of prolactin (potentially causing direct autoregulation on the lactotroph) seems unlikely because of the continuous flow of medium.

Animals↗
PubMed1982

Actions of dopamine on prolactin secretion and cyclic AMP metabolism in ovine pituitary cells.

Prolactin secretion from cultured sheep pituitary cells was inhibited by low concentrations of dopamine (0.1 nM-0.1 microM) with a half-maximal effect at 3 nM. At a maximally effective dose (0.1 microM) dopamine significantly inhibited prolactin secretion within 5 min. with an 80% inhibition of basal secretion over 2 h. Basal prolactin secretion was stimulated by the addition of methylisobutylxanthine (MIX) (0.3-1.0 mM) and 8-bromo-cyclic AMP (2 mM), but cholera toxin (3 micrograms/ml) and prostaglandin E2 (0.1-1.0 microM), which also raised cellular cyclic AMP levels, had no effect on prolactin release. The inhibition of prolactin release by dopamine (0.1 microM) was not affected by any of these compounds. Dopamine inhibited MIX-induced cyclic AMP accumulation over a similar concentration range to the inhibition of secretion, but had no effect on the changes in cyclic AMP concentration produced by cholera toxin and prostaglandin E2. Overall the results with sheep pituitary cells suggest that lowered cyclic AMP levels do not mediate the inhibitory effects of dopamine on basal prolactin secretion, but that changes in cellular cyclic AMP levels may alter the secretion of this hormone, and dopamine may affect pituitary cell cyclic AMP concentrations in some circumstances.

1-Methyl-3-isobutylxanthine↗
PubMed1982

A procedure for the purification of somatotrophs isolated from rat anterior pituitary glands using Percoll density gradients.

We have used fractionation on density gradients of Percoll to separate the cell types in the rat anterior pituitary gland and to produce a purified preparation of somatotrophs. The method differs from those described previously which used, for example, albumin or Ficoll gradients, in being more rapid and avoiding low temperatures, and therefore gives cells with improved viability. Anterior pituitary glands from male rats were dispersed with trypsin to produce 1.5 x 10 (6) -2.0 x 10 (6) cells/gland. These were fractionated on hyperbolic density gradients of Percoll. Two bands of cells containing somatotrophs were detected, one of which (band A; density 1.075-1.082 g/cm3) contained approximately 90% somatotrophs, whereas the other (band B; density 1.055-1.068 g/cm3) contained about 70% somatotrophs mixed with other cells, especially lactotrophs. Cells in band A appeared more responsive to secretagogues than those in band B; growth hormone secretion was stimulated markedly by cyclic AMP derivatives and prostaglandin E2, and inhibited by somatostatin. Such purified somatotrophs are well suited to biochemical studies on the mechanism of the control of growth hormone secretion.

Adrenocorticotropic Hormone↗
PubMed1982

Effects of domperidone on the secretion of prolactin from rat anterior pituitary glands.

The effects of omperidone on prolactin secretion from the anterior pituitary glands of female rats were studied. A perifusion system and radioimmunoassay were used to study secretion; static incubations, and incorporation of [3H]leucine were used to measure biosynthesis. During perifusion, intact anterior lobes showed a constant rate of prolactin secretion for up to 5h (after a 90-min preincubation to stabilize the tissue). Incorporation studies revealed an increase in protein synthesis in perifused hemipituitary glands. When glands were treated with 10nM-domperidone , prolactin secretion began to decline after the first hour, reaching a maximum of 40-50% inhibition after a further 90 min. Growth hormone secretion showed no such decline. Inhibition of prolactin secretion continued for up to 2h after withdrawal of the drug. Treatment with 100nM-dopamine resuled in a more rapid inhibition of secretion, but the effect was reversed on withdrawal of the catecholamine. The prolactin content of perifused hemipituitary glands was measured after treatment with domperidone; the contents of control and treated glands did not differ, but were depleted compared with hemipituitary glands which had not been perifused.

Animals↗
PubMed1981

An investigation of sites that bind human somatotropin (growth hormone) in the liver of the pregnant rabbit.

The binding of 125I-labelled human somatotropin (growth hormone) to a crude membrane preparation from the liver of pregnant rabbit, and to receptors solubilized from this fraction by Triton X-100, was dependent on time, temperature and receptor concentration. At 4 degrees C a steady state was reached after 20 h, and maximum specific binding (as a percentage of total tracer added) was approx. 50% for both membrane-bound and solubilized receptors. Solubilization did not significantly affect the binding properties of the receptor at low concentrations of Triton X-100 (less than 0.05%, v/v, in the assay tube). However, at higher concentrations (approx. 0.1%, v/v), the detergent lowered the ability of some hormones, for example ovine prolactin, to displace 125I-labelled human somatotropin, but did not affect other hormones such as bovine somatotropin. Some somatogenic hormones, such as bovine somatotropin, and some lactogenic hormones, such as ovine prolactin, displaced 125I-labelled human somatotropin from membrane-bound and solubilized receptor preparations. Furthermore, 85% of 125I-labelled bovine somatotropin was displaced from membrane-bound receptors by ovine prolactin, and 125I-labelled ovine prolactin was almost completely displaced by bovine somatotropin. Scatchard analysis of the binding data for human somatotropin suggested a single class of binding sites in the membrane-bound receptor preparation, with an affinity (Ka) of 1.9 X 10(9) M-1 and a capacity of 1726 fmol/mg of protein; these values were slightly increased by solubilization (Ka = 3.2 X 10(9) M-1, capacity = 2103 fmol/mg of protein). Scatchard analysis of binding to membrane-bound receptors also indicated a single class of high-affinity binding sites for bovine somatotropin (Ka = 4.8 X 10(9) M-1, capacity = 769 fmol/mg) and for ovine prolactin (Ka = 6.1 X 10(9) M-1, capacity = 187 fmol/mg).

Animals↗