Tracheomediastinal Fistula in a Patient With Lung Adenocarcinoma and Its Treatment With Argon Plasma Coagulation: A Case Report

Tracheomediastinal fistula is a rare complication that occurs during the course of lung cancer. The fistula connects the airways to the mediastinum and is often associated with lymphoma. Clinical data on tracheomediastinal fistulas are limited to case reports. Tracheal stenting, pericardial and omental patch closure, and muscle flap closure can be performed to repair such fistulas. We herein report a case of tracheomediastinal fistula in a 47-year-old man.The main symptoms were shortness of breath and a feeling of fullness in the neck. Thoracic magnetic resonance imaging revealed an approximately 57 × 16 × 20 mm multiloculated cystic lesion with air density located in the upper mediastinum of the right paratracheal region and a fine fistula tract at this level. The main diagnosis was primary lung adenocarcinoma-related mediastinal lymphadenomegaly with a tracheomediastinal fistula.The patient underwent fistula opening on the trachea, which was then coagulated and sealed using argon plasma coagulation.The patient is currently asymptomatic and doing well 8 months after the intervention.     

SD Plasma in TTP and Coagulation Factor Deficiencies for which no Concentrates are Available

Abstract: Clinical studies of SD-Plasma (SDP) have included treatment of patients with both the acute and chronic relapsing (CRTTP) forms of TTP and replacement of coagulation factors in patients with congenital deficiencies. With the infusion of SDP in 6 patients with CRTTP, platelet counts rose, LDH values dropped, hemoglobin levels remained constant, and the patients continued in good health. In an FFP-controlled study in acute TTP, 16 patients were exchanged with SDP and 10 with FFP. There was no difference between the two groups in patient survival; relapse or remission rate; incidence of treatment resistance; or in per patient total volume infused, number of treatments, average volume per treatment, or number of relapses. Finally, 48 coagulation factor-deficient patients received SDP for surgical prophylaxis, active bleeding and routine prophylaxis for Factor XIII deficiency. The expected levels of the deficient factors were achieved, and the treating physicians concluded that there was control of bleeding.     

A Therapeutic Concentrate of Coagulation Factors II, IX and X from Citrated, Factor VIII-Depleted Plasma

Abstract. A simple procedure is described for the large-scale absorption on to DEAE-cellulose of coagulation factors II, IX and X from citrated, factor VIII-depleted plasma. The coagulation factors are eluted frontally from the exchanger in a high yield and in a form suitable for therapeutic use, without further fractionation. The lyophilised concentrate is very stable without the addition of heparin and, when redissolved to isoosmolar solution, contains approximately 30 U/ml factors II, IX and X, 250–300 times purified from the starting plasma. The effectiveness of the concentrate in the treatment of haemophilia B is discussed.     

Granulocyte-Macrophage Colony-Stimulating Factor for Perianal Hidradenitis Suppurativa: Report of a Case

Perianal hidradenitis suppurativa is a chronic inflammatory disease associated with significantly high morbidity, which severely affects the quality of life of those patients suffering from it. We describe a 46-year-old patient with extensive, severe gluteal and perianal PHS of 28 years duration. Repeated wide excisions, fistulotomies, treatments with hyperbaric oxygen, and finally a diverting colostomy were unsuccessful. A new form of treatment with repeated perilesional injections of granulocyte-macrophage colony-stimulating factor, in conjunction with surgical procedures, was performed with excellent results.     

Studies on Thrombopoiesis. I. A Factor in Normal Human Plasma Required for Platelet Production; Chronic Thrombocytopenia Due to its Deficiency

1. A case of chronic thrombocytopenic purpura has been presented inwhich the pathogenesis appears to be due to congenital deficiency of aplatelet-stimulating factor.

2. The factor exists in normal plasma and is stable on storage under normalblood banking conditions and on freezing.

3. The factor appears to act by stimulating megakaryocyte maturation andplatelet production in an orderly and sequential manner.

Submitted on August 15, 1959 Accepted on October 9, 1959     

Immunologic Studies of Antihemophilic Factor (AHF, Factor VIII) II. Properties of Cross-reacting Material

Patients with a genetic variant of hemophilia A have in their plasmas material which has antigenic characteristics similar to those of antihemophilic factor(AHF). The physical properties of the biologically inactive cross-reacting material (CRM) are like those of AHF from normal plasma. The CRM is concentrated in Cohn fraction I and in cryoprecipitates and is not adsorbed fromplasma by calcium phosphate or barium sulfate. It is inactivated by heating to56° for 30 minutes. The CRM is less sensitive to thrombin inactivation thanAHF and is recovered in serum. The similar properties of AHF and CRM support the hypothesis that patients with this genetic variant of hemophilia Asynthesize a material similar to AHF but lacking procoagulant activity.

Submitted on November 10, 1969 Accepted on January 15, 1970     

Studies on Plasma Coagulation and Fibrinolysis during Oral Contraception of Various Types With Special Reference to Cold Activation of Factor VII

Various coagulation and fibrinolysis parameters and proteinase inhibitors were studied in plasma samples from 72 women treated with oral contraceptives. Anovlar® was given to 40 women, Sequens® to 21, and the progestogen Ro-3129 to 11. The most impressive observation was the marked effect of oestrogen treatment on the extrinsic coagulation system. Notably the cold activation of factor VII was influenced by the oestrogens, increasing the incidence in this series from about 9 % to about 65 %. Progestogen treatment had no such effect. This effect of oestrogen treatment was additional to changes in the concentrations of fibrinogen, factors II-VII-X, VIII, IX, and antithrombin III, that were in accordance with earlier reports. The concentration of C'l-inactivator of complement decreased. Also for plasminogen and plasminogen proactivator the concentrations increased as a result of oestrogen treatment. The in vivo importance of the changes is discussed, and it is suggested that cold activation of factor VII may indicate an increased tendency towards intravascular coagulation.     

Evidence for a Splenic Release Factor of Platelets in Chronic Blood Loss Plasma of Rabbits

S ummary . Rabbits subjected to chronic blood loss with iron supplementation raised their platelet count and megathrombocyte number 1.7x and 2.1 x above baseline, respectively. In similarly treated splenectomized animals, no significant response was obtained. When chronic blood loss plasma was injected into recipient animals there was a rise in platelet count and megathrombocyte number of 1.8 x and 3.4 x respectively compared to animals injected with control plasma. In similarly treated splenectomized animals no such rise was obtained; neither was there a rise in platelet count or megathrombocyte number in intact recipient animals when chronic blood loss plasma was obtained from splenectomized animals. It is concluded that the thrombocytosis of chronic blood loss requires the presence of an intact spleen. The data suggest the presence of a release factor which requires the spleen for its elaboration as well as expression.     

The Coagulation of the Blood. Investigations on a New Clotting Factor. BY PAUL A. OWREN. Oslo, J. Christian Gundersen, 1947

An error was made in Dr. F. H. L. Taylor’s review of Dr. Owren’s book, "TheCoagulation of the Blood," in the February issue of Blood (3: 229, 1948). Theformulae as printed were incomplete and should have read:

See PDF for Equation

See PDF for Equation

See PDF for Equation

     

Large-Scale Production and Properties of a Solvent-Detergent-Treated Factor IX Concentrate from Human Plasma

A human solvent-detergent (SD)-treated factor IX concentrate has been produced from cryoprecipitate-poor plasma using DEAE-Sepharose CL-6B and heparin-Sepharose CL-6B chromatography. The DEAE eluate was incubated with an SD mixture [0.3% tri(n-butyl) phosphate-1% Tween 80, 6-h at 24 degrees C] which was found to inactivate, in less than 1 h, more than 3.8 log10 of vesicular stomatitis virus and more than 4.8 log10 of Sindbis virus; the SD was removed by a subsequent heparin adsorption step. The specific activity of the concentrate was 10.9 +/- 1.3 IU factor IX: c/mg protein (n = 15). The factor IX coagulant to antigen ratio was 0.7 +/- 0.1. The concentrate was essentially free of factors II, VII and X, and protein C. The usual major contaminants of prothrombin complex concentrate (PCC) were absent: the concentrate contained about 94% alpha-1 proteins, and only 4 major proteins were resolved by SDS-PAGE (respective apparent molecular weight: 130, 86, 76 and 69 kilodaltons), and by crossed immunoelectrophoresis against an anti-PCC serum. The nonactivated partial thromboplastin time was equivalent to that of PCC; the product was devoid of factor IXa, of other activated procoagulant factors and of coagulant-active phospholipids (removed with SD in the heparin breakthrough fraction). Animal studies using the Wessler test and acute-toxicity test in rabbits revealed no adverse side effects. SD treatment could thus be used to inactivate viruses in factor IX concentrate and improve the safety of replacement therapy in hemophilia B.     

Immunologic Studies of Antihemophilic Factor (AHF, Factor VIII). III. Comparative Binding Properties of Human and Rabbit Anti-AHF

The binding properties of human andrabbit antibodies to antihemophilicfactor (AHF, factor VIII) have beencompared in experiments that soughtthe basis for their different specificities and secondary properties. Agarosegel filtration demonstrated the formation of stable complexes of AHF withrabbit anti-AHF but not with humananti-AHF. Measurement of boundradiolabeled rabbit anti-AHF providesa very sensitive assay for the AHFantigen that is present in normal andhemophilic plasmas but that is markedly reduced in plasmas from patientswith von Willebrand’s disease.

Submitted on July 1, 1971 Revised on August 20, 1971 Accepted on October 11, 1971     

Isolation and Properties of Polypeptide Chain Initiation Factor FII from Escherichia coli: Evidence for a Dual Function

Initiation factor FII (F(3), factor B) has been purified from Escherichia coli Q13 to apparent homogeneity. It is a heat-stable basic protein, consisting of a single polypeptide chain of molecular weight 21,000. FII is required, in addition to the other factors FI and FIII, for the formation of a 70S complex containing fMet-tRNA, poly(U,G) (used as a model messenger RNA), and the ribosome. FII also is capable of dissociating 70S ribosomes to 30S and 50S subunits. Evidence is presented that both activities are mediated by the same protein.     

Immunologic Studies of Antihemophilic Factor (AHF, Factor VIII). V. Immunologic Properties of AHF Subunits Produced by Salt Dissociation

Human antihemophilic factor (AHF, factorVIII), a large plasma protein with a molecular weight of approximately two million, isdissociated by changes in ionic strength.The immunologic properties of subunitsobtained by sucrose density ultracentrifugation in 1 M NaCl and by agarose gelfiltration in 0.24 M CaCl₂ have been determined using human and rabbit anti-AHF.Asymmetric dissociation of AHF has beenidentified with formation of two subunitsin these separations: a nonfunctional highmolecular-weight (HMW) subunit similarin size to plasma AHF which is identifiedby immunoprecipitation and radioimmunoassay for AHF antigen, and an active lowmolecular-weight (LMW) subunit which isnot detected by these antigen assays. TheLMW subunit retains AHF antigens, however, for it is inactivated by both humanand rabbit anti-AHF. Antibody neutralization studies verify the presence of AHFantigens on the HMW subunit. These immunologic studies provide constraintswhich must be incorporated into models ofAHF structure.

Submitted on February 11, 1973 Revised on April 13, 1973 Accepted on May 3, 1973