[Diagnosis and treatment of diving accidents. New German guidelines for diving accidents 2014-2017]. / Diagnostik und Behandlung von Tauchunfällen: Neue "Leitlinie Tauchun2014-2017".

In 2015 the German Society for Diving and Hyperbaric Medicine (GTÜM) and the Swiss Underwater and Hyperbaric Medical Society (SUHMS) published the updated guidelines on diving accidents 2014-2017. These multidisciplinary guidelines were developed within a structured consensus process by members of the German Interdisciplinary Association for Intensive Care and Emergency Medicine (DIVI), the Sports Divers Association (VDST), the Naval Medical Institute (SchiffMedInst), the Social Accident Insurance Institution for the Building Trade (BG BAU), the Association of Hyperbaric Treatment Centers (VDD) and the Society of Occupational and Environmental Medicine (DGAUM). This consensus-based guidelines project (development grade S2k) with a representative group of developers was conducted by the Association of Scientific Medical Societies in Germany. It provides information and instructions according to up to date evidence to all divers and other lay persons for first aid recommendations to physician first responders and emergency physicians as well as paramedics and all physicians at therapeutic hyperbaric chambers for the diagnostics and treatment of diving accidents. To assist in implementing the guideline recommendations, this article summarizes the rationale, purpose and the following key action statements: on-site 100% oxygen first aid treatment, still patient positioning and fluid administration are recommended. Hyperbaric oxygen (HBO) recompression remains unchanged the established treatment in severe cases with no therapeutic alternatives. The basic treatment scheme recommended for diving accidents is hyperbaric oxygenation at 280 kPa. For quality management purposes there is a need in the future for a nationwide register of hyperbaric therapy.

[Hemorrhage in external eye muscles]. / Uber äussere Augenmuskelblutungen.

Of 91 unselected forensic autopsy cases then lateral muscles of both eyes were prepared in stepped sections and examined for microscopical haemorrhages. During autopsy we payed attention to macroscopical haemorrhages. Microscopical haemorrhages were found in 12 cases mainly in suffication processes as in two cases of fulminant pulmonary embolism. In five of the examined cases we also found macroscopical hemorrhage, mainly with strangulation. According to our results till now, haemorrhage in ocular muscles are seen in the process of aspyxia; if this is protracted as in manual strangulation or strangulation by ligature, macroscopical haemorrhage may occur.

Characterization of N- and C-terminal deletion mutants of the rat serotonin HT2 receptor in Xenopus laevis oocytes.

Deletion mutants of the serotonin HT2 receptor have been constructed in which the N- and C-terminal sequences have been gradually removed. The mutant constructs were assayed for their biological activity by electrophysiological measurements in Xenopus oocytes previously injected with the respective in vitro synthesized cRNAs. No significant loss of biological activity was observed when either the extracellular N-terminal sequence, including all potential glycosylation sites, up to the beginning of the first transmembrane domain or the C-terminal sequence up to cystein residue 397, which is conserved in most G-protein coupled receptor known so far, was deleted from the serotonin HT2 receptor constructs.

The core proteins of 35S hnRNP complexes. Characterization of nine different species.

Ribonucleoprotein complexes (hnRNP) containing fragments of heterogeneous nuclear (hn)RNA and sedimenting at 35-40 S were isolated from the nuclei of HeLa S3 cells using the pH 8.0/diffusion technique. These hnRNP complexes are thought to be part of the hnRNA processing apparatus. The major protein components (core proteins) were identified by their constant ratios in native particles and in 35S hnRNP particles reconstituted in vitro. All of the core proteins, with one exception, show an increase in Mr on sodium dodecylsulfate (NaDodSO4)/polyacrylamide gels containing 8 M urea, indicative of secondary structure elements resistant to denaturation by NaDodSO4. The nine core proteins found by us are: A1 [Mr(NaDodSO4) 31 X 10(3)/Mr (urea) 38 X 10(3), apparent isoelectric point, pIapp 9.3], A2 (32.5 X 10(3)/39 X 10(3), 8.4), B1a (35.5 X 10(3)/41 X 10(3), 8.8), B1b (35.5 X 10(3)/44 X 10(3), 8.3), B1c (35.5 X 10(3)/43 X 10(3), 5.7) B2 (37 X 10(3)/42 X 10(3), 9.15), C1 (39 X 10(3)/46 X 10(3), 9.2), C2 (40.5 X 10(3)/45 X 10(3), 5.55) and C3 (38.5 X 10(3)/37 X 10(3), 4.8). Individual proteins were electroeluted from two-dimensional gels and their amino acid composition determined. Difference indices were calculated and show a group of closely related basic proteins (A1, A2, B1a, B1b, B2, C1), two related slightly acidic proteins (B1c, C2) and a distinct acidic member (C3). Two-dimensional analysis of tryptic fragments and one-dimensional separation of peptides after V8 protease treatment support these data. Peptide mapping of the proteins A1 and A2 from bovine and human cells yields identical fragments indicating a high degree of cross-species conservation. An additional protein (D4: 44 X 10(3)/55 X 10(3), greater than 9.5) was found, which preferentially associates with heavier, oligomeric hnRNP structures. Only traces of actin are present in the 35S hnRNP fraction. All core proteins are modified by charge. A large part of the charge isomers arises by phosphorylation, which has been shown by labeling with 32PO4 in vivo and with [gamma-32P]ATP in vitro. In vitro the phosphate transfer is mediated by an endogenous protein kinase associated with the 35S hnRNP complexes. The major core protein A1 exists in two conformeric forms (A1 and A1x) of which only A1x serves as phosphate acceptor in vivo.

Mammalian single-stranded DNA binding protein UP I is derived from the hnRNP core protein A1.

Antibodies induced against mammalian single-stranded DNA binding protein (ssDBP) UP I were shown to be cross-reactive with most of the basic hnRNP core proteins, the main constituents of 40S hnRNP particles. This suggested a structural relationship between both groups of proteins. Using the anti-ssDBP antibodies, a cDNA clone (pRP10) was isolated from a human liver cDNA library in plasmid expression vector pEX1. By DNA sequencing this clone was shown to encode in its 949 bp insert the last 72 carboxy terminal amino acids of the ssDBP UP I. Thereafter, an open reading frame continued for another 124 amino acids followed by a UAA (ochre) stop codon. Direct amino acid sequencing of a V8 protease peptide from hnRNP core protein A1 showed that this peptide contained at its amino terminus the last 11 amino acids of UP I followed by 19 amino acids which are encoded by the open reading frame of cDNA clone pRP10 immediately following the UP I sequence. This proves that ssDBP UP I arises by proteolysis from hnRNP core protein A1. This finding must lead to a re-evaluation of the possible physiological role of UP I and related ssDBPs. The formerly assumed function in DNA replication, although not completely ruled out, should be reconsidered in the light of a possible alternative or complementary function in hnRNA processing where UP I could either be a simple degradation product of core protein A1 (as a consequence of controlling the levels of active A1) or may continue to function as an RNA binding protein which has lost the ability to interact with the other core proteins.(ABSTRACT TRUNCATED AT 250 WORDS)