bluuebunny/crossref_metadata_2025_split huggingface dataset:
Anwendung des Larynxtubus in der Notfallmedizin – Komplikationen und Fallstricke
Authors: Schalk Richard , Byhahn Christian , Klüner Claudia , Bernhard Michael 
Published: July 2018

ZusammenfassungMit der zunehmenden Anwendung von Larynxtuben in der prähospitalen Notfallmedizin, sowohl durch Notärzte als auch durch nicht ärztliches Rettungsdienstpersonal, werden zunehmend Komplikationen, auch schwerwiegender Art, beobachtet. Anhand eines Fallbeispiels von einem Patienten, bei dem es durch einen unbemerkt fehlplatzierten Larynxtubus zunächst zu einer Cannot intubate, cannot ventilate-Situation mit der Notwendigkeit für einen chirurgischen Atemweg, in der Folge zu einem abdominellen Kompartment-Syndrom aufgrund gastraler Luftinsufflation durch den Larynxtubus kam, werden die typischen Anwenderfehler und Komplikationen aufgezeigt. Den aktuellen Leitlinien der Fachgesellschaften folgend sollen in der Notfallmedizin ausschließlich Larynxtuben der 2. Generation zum Einsatz kommen, welche die Möglichkeit der gastrischen Drainage bieten. Damit diese effizient erfolgen kann, muss eine Magensonde unmittelbar nach Platzierung eingelegt werden. Kann diese nicht eingebracht werden, ist dies quasi beweisend für eine unmittelbar korrekturbedürftige Fehllage. Die Cuffdruckmessung soll zu einem frühestmöglichen Zeitpunkt vorgenommen und der Cuffdruck auf in der Regel maximal 60 cmH2O adjustiert werden, um druckbedingte Zirkulationsstörungen der Zunge mit entsprechender Schwellung zu vermeiden. Schlussendlich sollte ein strukturiertes Ausbildungscurriculum angewendet werden, dass den zukünftigen Anwender für diese Komplikationen sensibilisiert.
Dilation catheter-guided mini-forceps biopsy improves the diagnostic accuracy of malignant biliary strictures
Authors: Ren Ying-Chun , Huang Chun-Lan , Chen Su-Min , Zhao Qiu-Yan , Wan Xin-Jian , Li Bai-Wen 
Published: July 2018

Abstract
Background Tissue sampling for biliary stricture is important for differential diagnosis and further treatment. The aim of this study was to assess a novel dilation catheter-guided mini-forceps biopsy (DCMB) method in the diagnosis of malignant biliary strictures.
Methods 42 patients with malignant biliary stricture who underwent both brush cytology and DCMB during endoscopic retrograde cholangiopancreatography between October 2014 and November 2015 were retrospectively included. During DCMB, the mini biopsy forceps was introduced into the biliary stricture through the dilation catheter, and then the position and direction of the forceps were adjusted to obtain tissue samples.
Results The positive rate of DCMB was significantly higher than that of brush cytology (81.0 % [34/42] vs. 38.1 % [16/42]; P < 0.001). No severe complications occurred; three patients (7.1 %) experienced mild procedure-related acute pancreatitis.
Conclusions The novel DCMB technique was a practical, safe, efficient, and low-costing method for diagnosing malignant biliary stricture with a high accuracy rate.
Expression of Functional Coagulation Factor XIII in Escherichia coli
Authors: Board P G , Pierce K , Coggan M 
Published: July 2018

SummaryCoagulation factor XIII is a zymogen that can be activated by thrombin cleavage to a transglutaminase that catalyses the formation of covalent crosslinks between fibrin chains in the final stages of the blood clotting cascade. Although circulating factor-XIII is composed of A and B subunits the catalytic activity is a property of the A subunits. In this study we have constructed a plasmid (pKKF13A) that contains a cDNA encoding the A subunit positioned downstream of a tac promoter. Escherichia coli containing this plasmid produce A subunit protein when grown in the presence of IPTG. The cloned A subunit has been partially purified and characterized. Comparison with A subunits purified from plasma showed that the cloned A subunits were of the same size, assembled as dimers, and had the same native electrophoretic mobility. The cloned A subunits expressed transglutaminase activity with putrescine, dansylcadaverine and casein as substrates, and were able to crosslink fibrin in clots formed from A subunit deficient plasma. These studies have demonstrated that functional recombinant factor XIII A subunit can be produced in E. coli and suggest that recombinant factor XIII can potentially provide a safe and inexhaustible supply for therapeutic use.
A Plasminogen Activator Inhibitor-2 from a Promyelocytic Leukemia Cell Line, PL-21, Binds to the Carboxy-Terminal Chain of Plasminogen Activators
Authors: Takeuchi Tetsuo , Niiya Kenji , Kubonishi Ichiro , Miyoshi Isao 
Published: July 2018

SummaryA promyelocytic leukemia cell line, PL-21, was found to produce an inhibitor of plasminogen activators (PAI). The PAI reacted to anti-PAl-2 but not anti-PAI-1 anti-serum and had an apparent molecular weight of 43 kDa on unreduced SDS-PAGE. The PAI inhibited not only urokinase-type plasminogen activator (u-PA) but single- and two-chain tissue-type plasminogen activators (t-PAs) on plasminogen-containing fibrin plate. It formed SDS-stable complexes with both t-PA and u-PA but not with prourokinase as demonstrated by both fibrin zymography and immunoblotting using anti-PA and anti-PAI-2 antisera after SDS-PAGE. These complexes were still present even after reduction with dithiothreitol. The PAI appears to bind to the carboxy-terminal chain of both PAs, because the part of the band corresponding to the carboxy-terminal chain of PAs moved to an upper position as a result of complex formation when two-chain form of PAs were incubated with the PAI and analyzed by SDS-PAGE followed by immunoblotting
Expression of the Drug-Dependent Antigen for Quinine-Dependent Antiplatelet Antibodies on GP III a but not that on GPI b, II b or IX on Human Endothelial Cells
Authors: Pfueller Sharron L , Bilston Robyn A , Jane Stephen , Gibson Jannine 
Published: July 2018

SummaryIn quinine- and quinidine-induced thrombocytopenic purpura IgG antibodies are known to react in a drug-dependent manner with different combinations of surface glycoproteins (GP) Ib , IIb, IIIa and IX. Because endothelial cells share a number of properties of platelets, including the presence of GP Ilia and GPIb-like proteins, we have compared these two cell types for their quinine-dependent IgG binding abilities. By immunoblotting of endothelial cells, quinine-dependent IgG binding from four patient sera was observed only to a 93 kDa component corresponding to GP Ilia. Strong IgG binding independent of the drug was found at 170–180 kDa. Thus endothelial cells express the GP Ilia quinine-dependent epitope on platelet GP IIIa , but not those on other platelet glycoproteins.
Agglutination of Rabbit Platelets in Plasma by the Thrombin Inhibitor D-phenylalanyl-L-prolyl-L-arginyl Chloromethyl Ketone
Authors: Packham M A , Bryant N L , Guccione M A 
Published: July 2018

SummaryThe specific thrombin inhibitor D-phenylalanyl-L-prolyl-Larginyl chloromethyl ketone (FPRCH2Cl, PPACK) has been used as an anticoagulant with human blood to permit the preparation
of platclct-rich plasma in which the physiological concentration of Ca2+ is maintained. When we attempted to use FPRCH2Cl(40 εM) as an anticoagulant for rabbit blood, clotting was prevented for at least 6 h at room temperature, but nearly all the platelets agglutinated. Thromboxane B2 was not formed and indomethacin and prostaglandin E1 were not inhibitory. The presence of citrate delayed this agglutination, but only EDTA (not EGTA) prevented it, indicating a dependence on Mg2+. Addition of FPRCH2Cl to suspensions of rabbit platelets in Tyrode-albumin solution had no effect on responses to ADP or collagen, but completely blocked all responses to human or rabbit thrombin. Thus plasma is required for the agglutination. Intravenous injection of FPRCH2Cl (5 mg/3 kg rabbit) reduced the platelet count to less than 50% by 15 to 25 min. Thus FPRCH2Cl cannot be used as an anticoagulant for rabbit blood when platelets are to be examined, and has a profound effect on the platelet count in vivo in rabbits. These effects should be considered when FPRCH2Cl is used as an antithrombotic agent for in vivo experiments with rabbits.
Involvement of Cyclooxygenase- and Lipoxygenase-Mediated Conversion of Arachidonic Acid in Controlling Human Vascular Smooth Muscle Cell Proliferation
Authors: Brinkman Herm-Jan M , Buul-Worteiboer Marijke F van , Mourik Jan A van 
Published: July 2018

SummaryWe observed that the growth of human umbilical arterysmooth muscle cells was inhibited by the phospholipase A2 inhibitors p-bromophenacylbromide and mepacrine. Thesefindings suggest that fatty acid metabolism might be integrated in the control mechanism of vascular smooth muscle cell proliferation. To identify eicosanoids possibly involved in this process, we studied both the metabolism of arachidonic acid of these cells in more detail and the effect of certain arachidonic acid metabolites on smooth muscle cells growth. We found no evidence for the conversion of arachidonic acid via the lipoxygenase pathway. In contrast, arachidonic acid was rapidly converted via the cyclooxy-genase pathway. The following metabolites were identified: prostaglandin E2 (PGE2), 6-keto-prostaglandin F1α (6-k-PGF1α), prostaglandin F2α (PGF2α), 12-hydroxyheptadecatrienoic acid (12-HHT) and 11-hydroxyeicosatetetraenoic acid (11-HETE). PGE2 was the major metabolite detected. Arachidonic acid metabolites were only found in the culture medium, not in the cell. After synthesis, 11-HETE was cleared from the culture medium. We have previously reported that PGE2 inhibits the serum-induced [3H]-thymidine incorporation of growth-arrested human umbilical artery smooth muscle cells. Here we show that also 11-HETEexerts this inhibitory property. Thus, our data suggeststhat human umbilical artery smooth muscle cells convert arachidonic acid only via the cyclooxygenase pathway. Certain metabolites produced by this pathway, including PGE2 and 11-HETE, may inhibit vascular smooth muscle cell proliferation.
Increased Whole Blood Viscosity during Coronary Artery Bypass Surgery
Authors: Hunter Robert L , Papadea Christine , Gallagher Christopher J , Finlayson Donald C , Check Irene J 
Published: July 2018

SummaryThis study was designed to test the hypothesis that soluble fibrin complexes resulting from the trauma of surgery could produce elevated blood viscosity, to characterize the soluble fibrin polymers, and to evaluate in vitro the effect of a new hemorheologic agent, poloxamer 188, on viscosity in these abnormal situations. Ten patients undergoing aortocoronary bypass surgery were studied before and at various times after surgery. By 6 h after surgery, the mean hematocrit decreased by 23%, fibrinogen decreased 48%, and erythrocyte sedimentation rate decreased 33%, whole blood viscosity at a low shear rate rose on average of 69% and soluble fibrin rose 118%. Over the 6-day observation period, the concentrations of soluble fibrin paralleled the changes in viscosity, whereas the concentrations of fibrinogen varied nearly inversely with viscosity. The effects of various forms of fibrinogen and fibrin were tested by additions to normal blood. Soluble fibrin polymers, but not fibrin monomers, increased blood viscosity two to three fold. Poloxamer 188 reduced the viscosity of all patient samples to the normal range. These data support the hypothesis that increased whole blood viscosity at low shear rates is caused by hydrophobic adhesion of fibrin polymers to red cells and that poloxamer 188 normalizes viscosity by effectively disrupting the weak hydrophobic bonds.
Effects of an Antifibrin Monoclonal Antibody and Fragments thereof on Some Properties of Fibrin
Authors: Wasser M N J M , Welling M , Lamers G , Pauwels E K J , Nieuwenhuizen W 
Published: July 2018

SummaryAntifibrin monoclonal antibody Y22, of IgG1-subclass, has its epitope in the D-domain of fibrin. In a thrombin time assay, Y22 and its F(ab)2 fragments interfere with clotting of citrated plasma. Transmission and scanning electronmicroscopic studies show that clotting of citrated blood or plasma in the presence of Y22 results in formation of thin, short fibrin fibres. The (smaller) Fab fragments of Y22 did not have an anti-clotting effect. This suggests that the anticoagulant effect of Y22 is due to steric hindrance of the association of fibrin monomers. A control antibody and its F(ab)2 and Fab fragments have no effect on fibrin formation.In a parabolic rate assay, Y22 Fab fragments interfered strongly with the fibrin-induced enhancement of the t-PA-catalyzed plasminogen activation, whereas intact Y22 and a control antibody did not. In contrast with their effects on the fibrin assembly, the effects of Y22, Y22-F(ab)2 and Y22-Fab on the capacity of fibrin to act as a rate-enhancer in the plasminogen activation by t-PA appears to decrease with the size of the immunoreactive entity. As is discussed, this may be due to the differential accessibility of sites involved in stimulation and polymerization which are located in the fibrin D-domain.
Localization of von Willebrand Factor and Thrombin-Interactive Domains on Human Platelet Glycoprotein Ib
Authors: Katagiri Yashuiro , Hayashi Yaeko , Yamamoto Kazuo , Tanoue Kenjiro , kosaki Goro , Yamazaki Hiroh 
Published: July 2018

SummaryPlatelet membrane glycoprotein Ib (GPIb) functions as receptors for thrombin and von Willebrand factor (vWF) in the presence of ristocetin. To precisely locate the domains on GPIb interacting with vWF and thrombin, we prepared several peptides that have amino acid sequences analogous to that ol the GPIb α-chain and examined their effects on ristocetin-induced (vWFdependent) and thrombin-induced platelet aggregations. A peptide extending from residues Asp235 to Lys262 showed the strongest inhibitory effect on ristocetin-induced platelet agglutination, and a group of overlapping peptides composed of 24-28 amino acid residues representing sequences extending from Phe216 to Asp274 was found to inhibit platelet aggregation induced by thrombin. Other peptides did not inhibit platelet aggregations. Moreover the binding to platelets of the monoclonal anti-GPIb antibody (TM60) which had been shown to inhibit both ristocetin- and thrombin-induced platelet aggregations was strongly inhibited by a peptide extending from Asp249 to Asp274. These data demonstrate that the vWF-hinding domain exists in a small region between residues Asp235 and Lys262; the thrombin-interacting domain, in contrast, is located between residues Phe216 and Ala274, with a possible center of interaction in the sequence from Phe216 to Thr240 on the GPIb α-chain, and thrombin binding requires a relatively strict conformation in this domain.
Antithrombotic Mechanisms of Urokinase lmmobilized Polyurethane
Authors: Kitamoto Y , Tomita M , Kiyama S , Inoue T , Yabushita Y , Sato T , Ryoda H , Sato T 
Published: July 2018

SummaryUrokinase immobilized polymer is highly antithrombotic, which cannot be explained only by fibrinolysis. We immobllized 10 IU/cm2 of urokinase to polyurethane by using maleic anhydride methylvinyl ether copolymer as a carrier. Then we incubated blood in circular tubes made of this material, measured the clotting factors and observed the surface of the tubes after incubation by scanning electronmicroscopy and immunofluorescence microscopy. After 5 min incubation, the relative activities of factors V, VIII, IX, X and XII, fibrinogeil, plasminogen and α2 plasmin inhibitor decreased, but the activity of factor VII increased. No platelet adhesion to the surface of the urokinase immobilized polyurethane was observed and there was no significant adsorption of serum proteins, including fibrinogen, fibronectin and vWF antigen, or the surface. Urokinase-immobilized polyurethane catalyzed the digestion of clotting factors as well as fibrinolysis and also inhibited platelet adhesion on its surface probably by inhibiting protein adsorption and its clinical application including vessel prosthesis should be developed further.
Blood Flow Stasis Induced by cw-Nd: YAG Laser Irradiation: Comparative Morphology of Mesenteric and Choroidal Vessels in Pigmented Rabbits
Authors: Zypen E van der , England C , Fankhauser F , Kwasniewska S 
Published: July 2018

Summarycw-Nd: YAG laser radiation was effective in producing blood flow stasis within arteries (35 – 40 μm in diameter) of pigmented rabbit mesentery (beam spot size: 80 μm; fluence :2 × 104 J cm−2) and choroid (beam spot size : 200 μm; fluence: 6 × 102 J cm−2) However, the mechanism by which this was achieved differed in each case, and depended upon the energy absorbing structures present in the irradiated tissue. In non-pigmented tissue, such as the mesentaty, haemoglobin represents the primary absorption centre, and the temperature attained within the vessel lumen (as inferred from morphological changes) is sufficient to denature plasma proteins, in particular fibrinogen, which consequently occlude the vessel lumen and arrest bleeding. In pigmented tissue, such as the choroid, melanocyte granules represent the primary absorption centre, which is thus shifted from the vessel lumen to the stroma. The temperature rise achieved within the vessel lumen is consequently loweq as evidenced by the absence of plasma protein denaturation. Blood flow stasis nonetheless occurs, but is triggered according to the normal haemostatic mechanism.
Thromboembolism and Bleeding Tendency in Congenital Factor XII DeficienCy - A Study on 74 Subjects from 14 Swiss Families
Authors: Lämmle Bernhard , Wuillemin Walter A , Huber Isabelle , Krauskopf Marina , Zürcher Christian , Pflugshaupt Rolf , Furlan Miha 
Published: July 2018

SummaryIn order to assess the clinical implications of hereditary F XII deficietrcy, all available members of Swiss families with F XII deficiency were investigated. Based on the F XII: C values and the family pedigree, the 74 subjects, aged 8-–82 years, were classified as homozygotes/double heterozygotes for F XII deficiency (n = 18), as obligatory (n = 20) or possibly (n = 25) heterozygotes, respectively, and as norrnals (n = 11). None of the 18 subjects with F XII: C <0.01 U/ml and only one possibly heterozygous woman had an abnormal bleeding tendency, confirming the notion that Hageman trait generally does not result in a hemorrhagic diathesis. Two of the 18 subjects with severe F XII deficiency had suffered from venous thromboembolic disease at age <40 years. One heterozygous woman had a leg ulcer probably due to venous thrombosis. Thus, whereas homozygous F XII deficiency may be associated with an increased risk for venous thromboembolic disease, partial F XII deficiency is not, by itself, a strong risk factor for thrombosis.Where as 17 of the 18 subjects with F xII : C <0.01 U/ml had no detectable F XIL Ag, one cross reacting material-positive F XII deficient subject (F XII:Ag = 0.11 U/ml) was identified. The dysfunctional F XII, present in this subject's plasma and tentatively called F XII Bern, is the fourth abnormal F XII molecule identified so far.
Factor VII Clotting Assay: Influence of Different Thromboplastins and Factor VII-Deficient Plasmas
Authors: Poggio Marina , Tripodi Armando , Mariani Guglielmo , Mannucci Pier Mannuccio ,   on behalf of the CISMEL* Study Group
Published: July 2018

SummaryBeing a putative predictor of ischemic heart disease, the measurement of factor VII (FVTI) coagulant activity will be presumably requested to clinical laboratories with increasing frequency. To assess the influence on FVII assays of different thromboplastins and FVII-deficient plasmas we compared performances of all possible combinations of 5 thromboplastins and 6 deficient plasmas. The reproducibility of the clotting times of the dose-response curves for human and rabbit thromboplastins were acceptable (CV lower than 7%), whereas bovine thromboplastin had a higher CV. Reproducibility was very similar for all deficient plasmas when they were used in combination with a given thromboplastin. Responsiveness of the dose-response curve did not depend on the deficient plasma but rather on the thromboplastin: one rabbit thromboplastin was the least responsive, the bovine thromboplastin the most responsive, the human and the remaining two rabbit thromboplastins had intermediate responsiveness. Assay sensitivity to cold-activated FVII varied according to the thromboplastin: the bovine thromboplastin was the most sensitive, the human thromboplastin the least sensitive, of the three rabbit thromboplastins two were relatively sensitive, one was almost insensitive. In conclusion, our results indicate that thromboplastin rather than deficient plasma is the crucial factor in the standardization of FVII assay.
Purified Factor XII Has a Higher Specific Activity than the Parent Molecule in Plasma
Authors: Wuillemin Walter A , Furlan Miha , Huber Isabella , Lämmle Bernhard 
Published: July 2018

SummaryThe specific clot promoting activity of factor XII (F XII) in plasma samples from 50 healthy adults was between 30 and 48 U/ mg, whereas the specific activity of purified F XII ranged from 55 to 66 U/mg. This difference was neither due to partial proteolytic activation during purification of F XII nor to the influence of plasma protease inhibitors. Purified F XII showed normal size and charge, as demonstrated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing, respectively. The increase of the specific F XII activity during the purification process mainly occurred after anion exchange chromatography on DEAE-Sephadex and after the final gel filtration step. Upon dextran sulfate activation, proteolytic cleavage of F XII and generation of kallikrein-like amidolytic activity was faster in F XII deficient plasma containing purified F XII than in F XII deficient plasma containing a corresponding amount of pooled normal plasma (NHP). The binding to kaolin was similar for both, purified F XII and plasma F XII.In conclusion, purification alters the properties of F XII in an unknown way, resulting in an increased specific clot promoting activity.
Blood Group A and B Determinants Are Expressed on Platelet Glycoproteins IIa, IIIa, and Ib
Authors: Santoso S , Kiefel V , Mueller-Eckhardt C 
Published: July 2018

SummaryWe report the localization of A, B blood group determinants on intrinsic glycoproteins using anti-A, B IgG antibodies. By radioimmunoprecipitation, anti-A and anti-B precipitated three bands with apparent molecular masses in sodium dodecylsulphate- polyacrylamide gel electrophoresis (SDS-PAGE) of 159, ~ 120 and 85 kDa under non-reduced conditions and 145, ~ 126 and 97 kDa under reduced conditions. In two-dimensional gel electrophoresis (isoelectric focussing/SDS-PAGE) these three bands could be resolved into six spots and fulfilled previously defined citeria for platelet membrane glycoprotein complexes Ia/IIa, Ic’IIIa, Ib/IX and IIb/IIIa. The results were supported by data obtained by an assay employing antibody-specific immobilizatisn of platelet antigens (MAIPA). By this technique, blood group A, B determinants were shown to be immobilized by monoclonal antibodies specific for GPIa, Ic’, IX, IIb/IIIa and strongly by mab specific for GPIIa, but not by mab specific for HLA class I molecules.The more precise localization on platelet glycoproteins was achieved by immunoblotting technique by which blood group A determinants could be assigned to GPs IIa, IIIa and Ib.
The Effect of Human Platelets on Lipolytic Activity in Plasma
Authors: Vik-Mo Harald 
Published: July 2018

SummaryA method for assay of lipolytic activity in platelet-poor plasma (PPP), platelet-rich plasma (PRP) and washed human platelets is presented. The lipolytic activity in PRP was about twice the activity in PPP. A significant correlation between lipolysis in platelets and platelet number was established. Molar sodium chloride strongly inhibited lipolytic activity in platelets and a washing procedure did not significantly change the lipolysis. The results indicate that a lipoprotein lipase is bound to human platelets and may play a role in metabolism of triglyceride in platelets.