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Biomedical subjects

D S Jackson

Publications and source records attributed to D S Jackson.

At least 37 records · Page 2Linked to original sources
PubMed1985

Sigmoid volvulus in late pregnancy.

Sigmoid volvulus in late pregnancy is an uncommon complication. We report a case of a 35 year old Caucasian woman who presented with symptoms and signs of intestinal obstruction when 34 weeks pregnant. Surgical management of the case is described and the literature reviewed.

Adult↗
PubMed1984

Sepsis in soft tissue limbs wounds in soldiers injured during the Falklands Campaign 1982.

The factors related to the development of sepsis in the soft tissue limb injuries sustained by soldiers during the Falklands Campaign have been assessed. Delay in surgery and delay in antibiotic administration are the most important factors, and where delay in surgery is inevitable, delay in antibiotic administration assumes an even greater importance.

Anti-Bacterial Agents↗
PubMed1983

Prospective randomized multicentre trial of proximal gastric vagotomy or truncal vagotomy and antrectomy for chronic duodenal ulcer: results after 5-7 years.

In a prospective, randomized study 145 patients with duodenal ulcer have been followed 5-7 years after proximal gastric vagotomy (PGV) or truncal vagotomy with antrectomy (TVA). Postoperative complications were significantly higher after TVA (P less than 0.0005). There was one death due to anastomotic leakage after TVA. The recurrence rate was significantly higher after PGV (9.9 per cent). Postoperative symptoms were less after PGV (P less than 0.01). Due to the recurrence rate after PGV there was no overall significant difference in the Visick grading, although perfect results (Visick I) were seen significantly more often (P less than 0.01). It is concluded that better results follow PGV.

Body Weight↗
PubMed1983

Interaction of blood platelets with a microfibrillar extract from adult bovine aorta: requirement for von Willebrand factor.

Adult bovine aortic tissue was treated with 6 M guanidinium chloride in the presence of proteinase inhibitors to obtain an extract that was essentially devoid of collagenous components and appeared homogeneous by electron microscopy. When this extract was dispersed by sonication it was found to be a very potent inducer of human platelet aggregation. This interaction required the presence of von Willebrand factor and of its receptor (glycoprotein Ib) on platelet membrane. This was demonstrated by the fact that the aggregation of normal blood platelets resuspended in plasmas deficient in von Willebrand factor was significantly diminished as compared to aggregation in control plasma. Moreover, this aggregation was inhibited by a monoclonal antibody, IgG AN51, to platelet glycoprotein Ib. These studies provide direct biochemical evidence for the existence of a thrombogenic constituent of the vessel wall that is noncollagenous and von Willebrand factor-dependent.

Amino Acids↗
PubMed1983

The Falklands war: Army field surgical experience.

In the recent Falklands campaign four Army Field Surgical Teams were deployed in the two phases of the war. They functioned as Advanced Surgical Centres and operated on 233 casualties. There were 3 deaths. The patterns of wounding and the methods of casualty management are discussed and compared with other recent campaigns.

Adult↗
PubMed1982

Two major non-collagenous glycoproteins in embryonic chick arteries.

Glycoprotein-containing extracts were obtained from thoracic arteries of embryonic chicks by sequential treatment involving 6 M guanidinium chloride, purified bacterial collagenase, and 6 M guanidinium chloride plus 50 mM dithiothreitol. Two major glycopolypeptides, designated G1 and G2, having apparent mol. wts. of 140,000 and 130,000 respectively were detected by SDS/polyacrylamide gel electrophoresis. Equilibrium density gradient ultracentrifugation demonstrated G1 and G2 to be glycoproteins and not proteoglycans or glycosaminoglycans. Amino acid analysis of a glycoprotein-enriched fraction confirmed the non-collagenous nature of G1 and G2. The highly insoluble nature of these glycoproteins suggests that these species are intimately associated with the extracellular matrix. Glycoproteins of similar size were also extracted from wing tendons indicating that G1 and G2 may be common to the elastic tissues of the chick.

Amino Acids↗
PubMed1981

The nature of the microfibrillar glycoproteins of elastic fibres. A biosynthetic study.

1. Cell cultures propagated from foetal bovine ligamentum nuchae synthesized and secreted two glycoproteins, designated MFP I and MFP II, that are closely related to elastic-fibre microfibrils. Glycoproteins MFP I (apparent mol.wt. 150 000) and MFP II (apparent mol.wt. 300 000) were metabolically labelled, separated from other culture-medium components by immunoprecipitation with a specific anti-(microfibrillar protein) serum, and analysed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and sodium dodecyl sulphate/gel-filtration chromatography. 2. Ligament cells also synthesized and secreted fibronectin, but salt-fractionation and immunoprecipitation studies with a specific anti-(cold-insoluble globulin) serum established that neither glycoprotein MFP I nor glycoprotein MFP II was related to fibronectin. 3. The secretion of glycoprotein MFP I, but not that of glycoprotein MFP II, was enhanced by the addition of ascorbate to the culture medium. 4. Ascorbate-supplemented ligament cells incorporated [3H]proline into glycoprotein MFP I, and 36% of the nondiffusible proline residues were hydroxylated, exclusively as 4-hydroxy[3H]proline. Less than 1% of the total proline residues in [3H]proline-labelled glycoprotein MFP II were hydroxylated. 5. Ascorbate-supplemented cells incorporated [14C]lysine into glycoprotein MFP I and 30% of the non-diffusible lysine residues were hydroxylated. 6. Newly secreted glycoprotein MFP I was digested by highly purified bacterial collagenase to yield polypeptide fragments of apparent mol.wts. 50 000 and 30 000. Glycoprotein MFP II was not digested by bacterial collagenase. 7. The results suggest that elastic-fibre microfibrils are composed of a novel collagenous glycoprotein MFP I in association, as yet undefined, with a non-collagenous glycoprotein MFP II.

Animals↗
PubMed1981

Identification of the primary translation product of elastic mRNA.

Poly (A) RNA was prepared from matrix free cells derived from the major thoracic arteries of 17-day old chick embryos. This was translated in a messenger-dependent reticulocyte cell-free system in the presence of [35S]-methionine, [3H]-proline or [3H]-valine. The translation products were analyzed by SDS polyacrylamide gel electrophoresis and fluorography and elastin-related products were immunoprecipitated by the addition of anti-elastin sheep antiserum in the presence of proteinase inhibitors and the precipitate analyzed by the same technique. The elastin-related products were found to consist of a doublet of two closely related polypeptides (mol. wts. 70,000 and 73,000) comigrating with a tropoelastin standard. Unhydroxylated pro alpha 1 and pro alpha 2 collagen polypeptides were also found, but no elastin related product corresponding to proelastin. It is concluded that the primary translation product of elastin mRNA consists of two polypeptides between 70,000 and 73,000 mol wt. which are closely related in size and immunoreactivity to tropoelastin.

Animals↗
PubMed1979

Translation of embryonic-chick tendon procollagen messenger ribonucleic acid in two cell-free protein-synthesizing systems.

Embryonic-chick tendon poly(A)-containing RNA was translated in the wheat-germ and mRNA-dependent rabbit reticulocyte-lysate systems. The ability of each system to synthesize polypeptides similar to pro-alpha chains of collagen was tested on the bases of electrophoretic mobility and susceptibility to highly purified bacterial collagenase. Very small amounts of polypeptides in the size range of pro-alpha chains were synthesized in the wheat-germ system, whereas efficient synthesis of two polypeptides similar to pro-alpha1 and pro-alpha2 chains was achieved in the reticulocyte lysate. The collagenous nature of the major high-molecular-weight products synthesized was demonstrated by their susceptibility to collagenase and ability to act as a substrate for purified collagen proline hydroxylase. Determinations of the relative amounts of these translation products suggest that the 2:1 ratio of pro-alpha1 and pro-alpha2 chains found in type I procollagen is reflected in proportional amounts of translatable mRNA for pro-alpha1 and pro-alpha2 chains. Comparisons of the electrophoretic mobilities of hydroxylated and unhydroxylated reticulocyte-lysate translation products were made with appropriate standards of hydroxylated and unhydroxylated procollagen polypeptides. The results suggest that, in common with a number of secreted proteins, procollagen is synthesized as pre-pro molecules consistent with the ;Signal Hypothesis'.

Animals↗
PubMed1979

The subcellular fractionation of embryonic chick tendon and cartilage cells: a re-examination.

A re-examination of the subcellular fractions obtained from matrix-free chick tendon and cartilage cells has been made since the discovery that three out of four of the micrographs of chick tendon microsomal fractions published in an earlier paper from this laboratory were not authentic. The present studies demonstrate that by using the procedures previously reported it is possible to isolate microsomal and submicrosomal fractions from tendon and cartilage cells which exhibit typical morphology when examined by electron microscopy. These observations are consistent with our original biochemical characterization of subcellular fractions, which we know to be valid. Other publications from this laboratory in which these fractionation procedures have been applied to studies of collagen biosynthesis are in no way compromised, and indeed, most of our data have been confirmed by several other laboratories.

Animals↗
PubMed1979

Possible modification of scar tissue by biochemical methods.

This paper reviews some of the biochemical modifications involved in fibrous tissue formation and discusses possible ways of controlling fibrosis in clinical conditions. The lathyritic agents, beta-aminoproprionitrile (BAPN) and penicillamine, appear in certain situations to be able to control fibrosis by blocking the biosynthesis of collagen. There are no compounds that are yet known which are capable of reversing pre-existing fibrosis and future research may perhaps be more profitably directed towards the stimulation of collagen catabolism rather than the inhibition of its synthesis.

Aminopropionitrile↗