ABSTRACT
Introduction Metropolitan Police data, and those from the emergency department at a London major trauma centre show a resurgence in gun crime. The aim of this study was to collect data on all gunshot injuries over a seven-year period at South-East London's trauma hub. Materials and methods This was a retrospective observational study of all gunshot injuries between 1 January 2010 and 31 December 2016 at a London major trauma centre. Information regarding patient demographics, morbidity and mortality was collected. Data from the English indices of multiple deprivation were reviewed in relation to shooting locations and socioeconomic status in South-East London. Results A total of 182 patients from 939,331 emergency admissions presented with firearm injuries. Males comprised 178 (97.8%) victims and 124 (68.1%) were documented as being Black or Afro-Caribbean. The median age was 22 years. Some 124 (71.7%) victims were shot within a 4 km radius of the hospital. The mean indices of multiple deprivation decile ranking in shooting locations compared with non-shooting locations was 2.6 (± 0.1384) and 3.8 (± 0.1149), respectively. A total of 122 (67.0%) patients underwent specialist operative intervention and 111 (61.0%) suffered only superficial or musculoskeletal injuries. Six patients required emergency thoracotomies; three (50.0%) survived to discharge. The median length of stay was 4 days (interquartile range 2-9 days) and 35 (24.0%) were admitted to intensive care. Ten (5.5%) patients died. Discussion and conclusion Firearms injuries are increasing and place a significant burden on hospital resources. Care provided to gunshot victims has improved as a result of recent trauma management initiatives at South-East London's major trauma centre.
Subject(s)
Urban Health/trends , Wounds, Gunshot/epidemiology , Adolescent , Adult , Child , Female , Humans , Length of Stay/statistics & numerical data , Logistic Models , London/epidemiology , Male , Middle Aged , Retrospective Studies , Socioeconomic Factors , Trauma Centers , Urban Health/statistics & numerical data , Wounds, Gunshot/diagnosis , Wounds, Gunshot/etiology , Wounds, Gunshot/therapy , Young AdultABSTRACT
Gingival overgrowth is a well documented and common side-effect of cyclosporin therapy. Gingival swelling in this condition hinders efficient oral hygiene and is of aesthetic concern to patients. This case report outlines rapid and dramatic reduction in overgrowth when tacrolimus replaced cyclosporin as the immunosuppressive agent in a renal transplant patient with established overgrowth.
Subject(s)
Cyclosporine/adverse effects , Gingival Overgrowth/chemically induced , Gingival Overgrowth/therapy , Immunosuppressive Agents/adverse effects , Immunosuppressive Agents/therapeutic use , Kidney Transplantation , Tacrolimus/therapeutic use , Adult , Humans , MaleSubject(s)
Muscles/metabolism , Myosins/biosynthesis , Peptide Chain Initiation, Translational , Peptide Initiation Factors/metabolism , Protein Biosynthesis , RNA, Messenger/metabolism , Animals , Chick Embryo , Chromatography, Affinity , Globins/biosynthesis , Molecular Weight , Peptide Initiation Factors/isolation & purificationSubject(s)
Protein Biosynthesis , RNA/isolation & purification , Actins/biosynthesis , Animals , Chick Embryo , Methods , Molecular Weight , Muscles/metabolism , Nucleic Acid Hybridization , Poly A/isolation & purification , RNA, Messenger/isolation & purification , Ribonucleoproteins/isolation & purificationABSTRACT
In the light of earlier work [1] which demonstrated the presence of a large number of myosin heavy chain (MHC) transcripts in chick myoblasts prior to cell fusion and the burst of MHC synthesis it was of great interest to determine the subcellular localization of the still inactive transcripts. It has been determined in differentiating muscle cells in culture. Two populations of cells were examined -- monucleated myoblasts just prior to cell fusion and myotubes where at least 80% of the cells were fused. Utilizing a myosin complementary DNA (cDNA) probe [2] it is observed that just prior to cell fusion, when the "burst" of myosin synthesis has not yet occurred, the vast majority of cytoplasmic myosin mRNA transcripts are found in a stored messenger RNA protein complex with a minimal amount found in the heavy polysome fraction. In differentiated myotube cultures, when myosin synthesis is progressing at a high rate, the reverse is found, i.e, the amount of stored myosin messenger RNA (mRNA) is minimal while the largest amount of myosin mRNA transcripts are localized in the polysome fraction. The number of total cytoplasmic myosin transcripts is found to decrease after cell fusion at a time when myosin synthesis is maximal suggesting that the efficiency of translation of myosin mRNA increases during terminal differentiation.
Subject(s)
Cell Differentiation , Muscles/cytology , Myosins/metabolism , RNA, Messenger/metabolism , Animals , Chick Embryo , Cytoplasm/metabolism , Microtubules/metabolism , Muscles/ultrastructure , Ribosomes/metabolismABSTRACT
Blood pressures were recorded in 319 ambulatory subjects, largely men, age 50 to 99 years. The mean systolic pressures were maximal in the seventh and eighth decades (136.0 and 132.1 mm Hg with the subjects supine and erect, respectively), whereas the mean diastolic pressures fell progressively after age 69. The distribution of postural changes in mean blood pressure was similar in each decade; a decrease of 20 mm Hg on more was noted in 3.4% of the subjects aged 80 to 99 years and in 4.1% of those aged 50 to 79 years. The frequency of postural hypotension was 4.6% in subjects treated with diuretics and 3.4% in those not so treated. Blood pressures and the frequency of postural hypotension did not progressively increase in age in this elderly population.
Subject(s)
Blood Pressure/drug effects , Diuretics/pharmacology , Hypotension, Orthostatic/epidemiology , Age Factors , Aged , Female , Humans , Institutionalization , Male , Middle Aged , OntarioSubject(s)
Nucleoproteins/metabolism , Protein Biosynthesis/drug effects , RNA, Messenger/antagonists & inhibitors , RNA/isolation & purification , Ribonucleoproteins/metabolism , Animals , Cell-Free System , Chick Embryo , Globins/genetics , Methods , Myosins/genetics , Poly U/metabolism , RNA/metabolism , RNA/pharmacology , RNA, Messenger/metabolismSubject(s)
Eukaryotic Initiation Factor-3/metabolism , Globins/biosynthesis , Myosins/biosynthesis , Peptide Chain Initiation, Translational/physiology , RNA, Messenger/metabolism , Triticum/metabolism , Animals , Cell-Free System/metabolism , Chick Embryo , Eukaryotic Initiation Factor-3/isolation & purification , RabbitsABSTRACT
Myosin messenger ribonucleoprotein-translational control ribonucleic acid (mRNP-tcNA) from myosin mRNPs found in embryonic chick muscle has been further purified by Dowex chromatography and, from a number of controls, it is suggested that this small RNA is not an artifact produced through the degradation of RNA during its isolation. This highly purified myosin mRNP-tcRNA is shown to have a molecular weight of 10 000 on formamide-acrylamide gels, and reacts stoichometrically (on a 1:1 mole ratio) with myosin mRNA. The stoichiometric interaction between myosin mRNA and myosin mRNP-tcRNP is demonstrated by ists ability to increase the nuclease resistance of the messenger, as well as inhibit its translation in a cell-free amino acid incorporating system.
Subject(s)
Myosins , RNA, Messenger/metabolism , RNA/metabolism , Animals , Cell-Free System , Chick Embryo , Molecular Weight , Myosins/biosynthesis , Nucleic Acid Hybridization , Peptide Chain Initiation, Translational , Poly A , Protein Biosynthesis , RNA/isolation & purification , Reticulocytes/metabolism , Ribonucleases , RibonucleoproteinsABSTRACT
Muscle translational-control RNA (tcRNA) has been separated into two classes, polysomal and messenger ribonuclear protein (mRNA - protein), which have different sizes as determined by acrylamide gel electrophoresis. While normally translation of mRNA - protein mRNA is inhibited by tcRNA derived from the same mRNA - proteins, this inhibition does not occur if the messenger is previously de-adenylated. This suggests that the poly(A) segment of mRNA is required for the tcRNA activity. Utilizing different mRNA - protein fractions from muscle, myosin mRNA - protein and small mRNA - proteins ( less than 30 S), we have been able to demonstrate that a degree of specificity exists in the interaction of tcRNA and mRNA derived from the same mRNA - proteins. This is illustrated by the facts that (a) each tcRNA only inhibits the translation of its respective mRNA and (b) the highest percentage of structural change occurs when each tcRNA is hybridized to its respective mRNA as measured by its resistance to T1 and T2 RNase.
Subject(s)
Muscles/metabolism , Myosins/biosynthesis , Protein Biosynthesis , RNA, Messenger/metabolism , Animals , Chick Embryo , Molecular Weight , Nucleic Acid Hybridization , Poly A/metabolism , Polyribosomes/metabolism , RNA, Ribosomal/metabolism , Uridine/metabolismABSTRACT
Two classes of translation control RNA (tcRNA) have been isolated from embryonic chick muscle. One of these classes, the tcRNA isolated from messenger ribonucleoprotein particles (mRNP-tcRNA), is effective in inhibiting the translation of mRNP-mRNA while having little if any effect on polysomal mRNA. The other class, polysome-tcRNA, has no effect on mRNP-mRNA while it stimulates the translation of polysomal mRNA. The mRNP tcRNA contains approximately 50 percent uridylate residues and forms small but stable hybrids with poly (A), while polysome-tcRNA contains fewer uridylate residues and is much less effective in forming a hybrid with poly (A). A proposed model concerning the role of these two classes of tcRNA in the regulation of protein synthesis is presented.
Subject(s)
Blood Proteins/biosynthesis , Protein Biosynthesis , RNA, Messenger/metabolism , RNA/metabolism , Reticulocytes/metabolism , Animals , Centrifugation, Density Gradient , Nucleic Acid Hybridization , Nucleoproteins/metabolism , Polyribosomes/metabolism , Rabbits , Ribonucleases , Ribonucleotides/analysisABSTRACT
Two messenger specific factors, phosphocellulose fractions 3 and 4, have been isolated from the initiation factor 3 fraction of red muscle initiation factors by chromatography on phosphocellulose. When added to a reticulocyte cell-free system containing both myoglobin and myosin mRNAs, phosphocellulose fraction 3 is found to specifically stimulate the synthesis of myoglobin while phosphocellulose fraction 4 is found to specifically stimulate the synthesis of myosin. In addition, a new RNA, isolated from the initiation factor 3 fraction, is shown to specifically inhibit the translation of heterologous mRNAs.