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Biomedical subjects

D M Power

Publications and source records attributed to D M Power.

At least 55 records · Page 3Linked to original sources
PubMed1999

Anatomy, demonstrating and basic surgical training.

Calmanisation of surgical training has led to the introduction of the concept of a two-year basic surgical training (BST) rotation. Successful completion of this training is assessed by the new MRCS/AFRCS examination. Within these constraints there is no room for the previously popular anatomy demonstrating posts. The aim of this study, therefore, was to examine the views of FRCS and MRCS surgical trainees about their own demonstrating experience, their current anatomical knowledge and on the future value of anatomy demonstrating.

Anatomy↗
PubMed1998

Cloning, characterisation and expression of the apolipoprotein A-I gene in the sea bream (Sparus aurata).

A full length cDNA clone representing apolipoprotein A-I was isolated from a sea bream (Sparus aurata) liver library. The clone encodes a 261 amino acid protein which shows highest amino acid identity (38%) with salmon apolipoprotein A-I. Northern blot analysis showed strong expression of a 1.4 kb transcript in liver with lower expression in intestine. Expression of apolipoprotein A-I in intestine was markedly reduced by treatment with triiodothyronine (T3).

Amino Acid Sequence↗
PubMed1998

Parathyroid hormone-related protein in lower vertebrates.

1. Parathyroid hormone-related protein (PTHrP) is an important mediator of humoral hypercalcaemia of malignancy in humans. Normal human subjects have very low levels of PTHrP in their circulation. 2. Parathyroid hormone-related protein has recently been demonstrated in high levels in the circulation and tissues of the sea bream and the dogfish, leading to the hypothesis that PTHrP may be a 'classical' hormone in fish. 3. Immunohistochemistry and in situ hybridization were performed to investigate the evolutionary history of PTHrP. Tissues were examined from a number of lower vertebrates, including lungfish, lamprey and several species of bony and cartilaginous fish. Parathyroid hormone-related protein was localized to the skin and to kidney tubules in all animals studied. In the developing lungfish, PTHrP was observed in the notochord, developing brain and skeletal muscle layers. These results suggest that PTHrP is of ancient origin and has a basic and fundamental function in vertebrates.

Animals↗
PubMed1997

Cloning and sequencing of a full-length sea bream (Sparus aurata) beta-actin cDNA.

A full-length cDNA clone encoding beta-actin (beta-actin) was isolated from a sea bream (Sparus aurata) liver cDNA library. Sequencing of this clone reveals an open reading frame encoding a 375 amino acid protein that shares a high degree of conservation to other known actins. The sea bream beta-actin sequence showed 98% identity to carp and human beta-actin and 95% and 94% identity to sea squirt and Dictyostelium cytoplasmic actins, respectively.

Actins↗
PubMed1996

Immunochemical detection of parathyroid hormone-related protein in the saccus vasculosus of a teleost fish.

Using antisera to regions of human parathyroid hormone-related protein (PTHrP) the saccus vasculosus (SV) of the sea bream (Sparus aurata) has been shown to contain immunoreactive PTHrP. By immunohistochemistry (IHC) the epithelial coronet cells in fixed and wax-embedded SV tissue reacted with antisera to the prepro region of human PTHrP (-13 to +2), the N-terminus PTHrP (1-16), and the midmolecule PTHrP (50-69). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of saccus extracts and incubation media contained two major proteins of 14.3 and 15 kDa. By Western blotting these two proteins both reacted with the three antisera used for IHC, suggesting that they are immunochemically similar to human PTHrP (1-84). Ultrastructurally the coronet cells of Sparus saccus vasculosus resembled coronet cells described for other teleosts, with an abundant smooth endoplasmic reticulum (SER) which was more highly organized in the coronets. IHC at EM level showed reaction mainly with the membranes of the SER. These results suggest that S. aurata saccus vasculosus may produce a PTHrP-like molecule similar to human PTHrP.

Animals↗
PubMed1996

Somatotropin release-inhibiting factor and galanin innervation in the hypothalamus and pituitary of seabream (Sparus aurata).

The distribution of galanin (GAL) and somatotropin-release-inhibiting-factor (SRIF) immunoreactivity in the hypothalamus and pituitary of the sea bream (Sparus aurata) was studied by immunocytochemistry. An extensive system of neurons immunoreactive with antisera to the two peptides was identified throughout the brain with staining particularly in the hypothalamus. In the hypothalamus, GAL immunoreactive perikarya were detected principally in the nucleus preopticus and nucleus tuberis. Major nerve tracts were observed to sweep down from the hypothalamic nuclei and reached the pituitary via the preoptico-hypophysial tract. Many of the fibers had varicose swellings indicating they were secretory. SRIF immunoreactivity was distributed similarly to GAL but the network of nerve fibers was less dense; no colocalization of these two peptides was seen. SRIF immunoreactive perikarya were present in the preoptic nucleus, the tuberal nucleus, and the basolateral hypothalamus. These perikarya were large and densely staining and were predominately bipolar, although some multipolar perikarya were observed. In the pituitary GAL and SRIF immunoreactivities were confined principally to the pars distalis where fibers infiltrated between growth hormone, prolactin, and adrenocorticotrophic cells. More of the fibers were immunoreactive for SRIF than for GAL. There was no immunoreaction for GAL or SRIF in any of the pituitary cells. There is thus morphological evidence for a neuroendocrine control of the pars distalis by GAL and SRIF and for a possible functional interaction between these two systems.

Animals↗
PubMed1995

Cloning and characterisation of a fish aldolase B gene.

A full length cDNA clone representing an aldolase mRNA was isolated from a sea bream (Sparus aurata) liver cDNA library. Sequencing of this clone revealed it to encode a 364 amino acid protein with 74% amino acid identity to human aldolase B and slightly lower similarity to human aldolase A and C. In view of the sequence data and of Northern blot analysis showing strong expression of a 1.6 kb transcript in liver it was concluded that the cloned gene represents aldolase B. This clone represents the first aldolase gene to be sequenced from any fish species thus providing new data on the evolution of the vertebrate aldolase gene family.

Amino Acid Sequence↗
PubMed1993

Parathyroid hormone-related protein is a factor in normal fish pituitary.

Using antibodies to the amino-terminal region of human parathyroid hormone-related protein (PTHrP) we have demonstrated PTHrP immunoreactivity in pituitaries and plasma of the sea bream (Sparus aurata). Pituitary cells at two distinct locations contained immunodetectable PTHrP; an anterior group in the rostral pars distalis which also contained immunoreactive thyroid stimulating hormone (TSH), and a posterior group lying at the border of the pars intermedia and proximal pars distalis between cells which stained with antibody to human corticotrophin-like intermediate lobe peptide. By Western blot analysis pituitary extracts contained two immunoreactive isoforms of PTHrP, one of 29 kDa and the other of 26 kDa. Media of pituitaries incubated for up to 14 days in Krebs-Ringer bicarbonate also had several isoforms of immunodetectable PTHrP, two of them corresponding to the 29- and 26-kDa molecular forms but there were in addition both larger and smaller molecules. The concentration of PTHrP in sea bream plasma was comparable with levels observed in human subjects with humoral hypercalcaemia of malignancy. There was no reaction between pituitary cells or pituitary extracts and antibody to human parathyroid hormone. Thus sea bream pituitary contains immunoreactive PTHrP, which appears to be released into medium during in vitro incubation and which may be a significant source of plasma immunoreactive PTHrP in vivo.

Animals↗
PubMed1992

Immunocytochemistry of somatotrophs, gonadotrophs, prolactin and adrenocorticotropin cells in larval sea bream (Sparus auratus) pituitaries.

The chronological appearance of endocrine cells in the pituitary of sea-bream (Sparus auratus) larvae was studied using antisera against salmon prolactin, trout growth hormone, salmon gonadotropin and N-terminal human adrenocorticotropin. The larval pituitary (1-12 days after hatching) was oval in shape and was composed of a dense mass of cells with few neurohypophysial fibres. By 60 days after hatching it began to resemble the adult and was divisible into a distinct rostral pars distalis containing prolactin and adrenocorticotropin cells; a proximal pars distalis containing somatotrophs and gonadotrophs and a pars intermedia. Cells immunoreactive with antisera against growth hormone were observed immediately after hatching (2 days post-fertilization). Weakly staining prolactin cells were observed 2 days later in the region corresponding to the rostral pars distalis. Cells immunoreactive with antigonadotropin and anti-adrenocorticotropin sera were observed in the pituitary 6 and 8 days after hatching, respectively. All the cell-types studied were immunoreactive from the time they were first identified until the final samples 90 days after hatching.

Adrenocorticotropic Hormone↗
PubMed1992

Immunocytochemical identification of growth hormone, prolactin, and gonadotropin cells in the pituitary of male plaice (Pleuronectes platessa) during gonadal maturation.

Somatotrophs, gonadotrophs, and prolactin (PRL) cells have been demonstrated in male plaice (Pleuronectes platessa) pituitary by immunocytochemistry. All cell types exhibited patterns of activity correlated with gonadal maturity. Immature and maturing male plaice (gonads very small or filling with sperm, stages I and III) had numerous densely staining somatotrophs and PRL cells but only a few weakly stained gonadotrophs. Mature plaice (fish in which sperm could be extruded under light pressure, stage VI) contained two populations of gonadotrophs. The PRL cells of these fish were densely stained and the somatotrophs more lightly stained. Spent plaice (thin, flabby gonads, stage VII) had little or no staining in PRL cells. Somatotrophs and gonadotrophs from these fish stained weakly with the antisera used in the study and, in some fish, vacuoles were observed in areas of the pituitary normally occupied by gonadotrophs.

Aging↗
PubMed1990

Separation of rainbow trout (Salmo gairdneri) growth hormone by gel electrophoresis.

Pituitaries from immature (n = 12) and mature female (n = 15) rainbow trout were cultured separately in vitro and subjected to polyacrylamide gel electrophoresis. Four protein bands were identified from the immature rainbow trout and three from the adults. The material from the immature trout was used to raise antisera. Three of the bands, including those with the highest (0.74) and lowest (0.27) Rf values, produced antibodies. Immunocytochemical studies revealed that all of the antisera bound strongly to the growth hormone cells and weakly, if at all, to prolactin cells in pituitary sections from rainbow trout.

Animals↗
PubMed1990

Branched chain amino/keto acid supplementation following severe burn injury: a preliminary report.

14 severely burned patients were randomly assigned to receive one of three nasogastric feeds commencing after the resuscitation period and continuing for 15 days. Group A received a feed with a high leucine content (31% of protein as branched chain amino-acids, BCAA). Group B received a similar feed to Group A but 65% of the leucine was replaced by alpha-ketoisocaproate (KIC). Group C received a whole protein feed (16% of the protein content as BCAA), and acted as a control group. Targeted energy intake was twice the calculated Basal Metabolic Rate (BMR). Group A had significantly reduced urinary 3-methylhistidine (3-MEH) and serum urea, compared with the control group. Serum total protein, albumin and transferrin and apparent nitrogen balance were not significantly different. Group B's results did not vary significantly from controls. Leucine enrichment reduces muscle protein breakdown benefiting burn patients fed enterally when compared to a standard feed, whereas KIC enrichment does not.

Journal Article↗
PubMed1990

A comparative study of glycosylated haemoglobin level in the Arabian camel (Camelus dromedarius) during different seasons.

1. The extent of haemoglobin glycosylation from 60 camels has been determined (4.39%) in blood samples drawn during winter. 2. Phosphate (9.45 mg/dl), DPG (2.9 mumol/ml) and glucose (138 mg/dl) levels were also recorded. 3. In addition the P50 at pH 7.4 was measured (22.8 Torrs). 4. The data obtained compared with human blood levels and with levels reported for camels during summer sampling. 5. Despite the fact that camels have higher blood glucose levels than humans, the extent of glycosylation is much less in camel blood than in human blood.

Animals↗
PubMed1989

A study of the biochemical characteristics of NADP+ isocitrate dehydrogenase from the liver and kidney of the Arabian camel (Camelus dromedarius).

1. NADP+ isocitrate dehydrogenase was partially purified from camel liver and kidney by an FPLC. 2. The specific activity of the purified preparation from liver was 63.5 mumol/min/mg protein and from the kidney was similar, 58.7 mumol/min/mg protein. 3. The enzyme from the two sources were similar in their pH optimum (7.6), electrophoretic mobility and stability to thermal inactivation at 60 degrees C. 4. Heat inactivation was accelerated by oxidized glutathione and cystine and decreased by dithiothreitol, reduced glutathione and cysteine. 5. The molecular weight of the enzyme from both organs was estimated as 60,000 +/- 5000. 6. Divalent metal ions increased the activities of both enzymes, with maximum catalytic activity in the presence of Mn2+ ions.

Animals↗
PubMed1988

Ubiquitin deposits in anterior horn cells in motor neurone disease.

A polyclonal antiserum to ubiquitin, a low molecular weight protein involved in the ATP-dependent removal of abnormal cytoplasmic proteins, has been used to stain spinal cord from 10 cases of motor neurone disease and from 12 control spinal cords. All 10 cases of motor neurone disease exhibited antiubiquitin-immunoreactive deposits in a proportion of the surviving anterior horn cells but these deposits were not seen in any of the 12 controls. These ubiquitin deposits do not correspond to previously described neuronal inclusions in motor neurone disease. The ubiquitin deposits represent, therefore, a new neuronal inclusion which possibly reflects previously unrecognised degradative events occurring in the vulnerable neurones.

Humans↗
PubMed1988

A novel gastrin-processing pathway in mammalian antrum.

An antiserum, L221, has been developed that is specific for the C-terminal region of the N-terminal tridecapeptide (i.e., 1-13) fragment of the acid-stimulating hormone, G17. In contrast to N-terminal G17 antisera previously used to estimate 1-13 G17, L221 does not cross-react with other N-terminal gastrin fragments or with C-terminal extensions of G17. Using L221 in conjunction with conventional gastrin antisera, and reversed-phase HPLC, it has been possible to identify in addition to 1-13 G17 a further, formerly unrecognised gastrin fragment, 1-11 G17, in stomach extracts. The production of 1-13 G17, 1-11 G17 and other gastrin forms such as the biologically active hexapeptide G6 which is known to occur naturally cannot be explained by tryptic cleavage of progastrin. Instead, their biosynthesis could be explained by the actions of an enzyme with an endopeptidase 24.11-like specificity. In porcine antrum, unsulphated and sulphated G17 are present in similar amounts, but unsulphated 1-13 G17 was about twice as abundant as sulphate 1-13 G17. This is consistent with previous in vitro findings that endopeptidase 24.11 has a higher affinity for the Ala-11-Tyr-12 and Gly-13-Trp-14 bonds in unsulphated G17, than in sulphated G17. The results suggest a novel albeit minor, processing pathway for gastrin biosynthesis in pig antrum involving an enzyme resembling endopeptidase 24.11.

Amino Acid Sequence↗