Intrapleural and intravenous Corynebacterium parvum in patients with resected stage I and II non-small cell carcinoma of the lung

Summary A prospective randomized trial compared the administration of intrapleural plus intravenous Corynebacterium parvum (C. parvum) versus placebo in patients with resected Stage I and Stage II non-small cell bronchogenic carcinoma. Treatment consisted of 7 mg C. parvum injected into the pleural space and 7 mg C. parvum intravenously once between days 6 and 12 postoperatively and 7 mg intravenously every 3rd month during the 1st year. Intrapleural administration of 35 cc of saline served as the placebo and the flush after intrapleural C. parvum.Of the 303 patients entered into this study, 286 were evaluable, with an average follow-up time of 3.5 years. More complications, especially fever, were observed in patients receiving C. parvum. A fever greater than 38 °C was observed in 9% of the patients assigned to placebo and 76% of the patients assigned to C. parvum. There was no significant difference between the treatments with respect to disease-free interval or survival.M. Kaufmann, J. Stjernswärd**, A. Zimmermann (Ludwig Institute for Cancer Research, Bern Branch); K. Stanley**, M. Isley, M. Zelen (Frontier Science & Tech. Research Foundation, Brookline, MA, USA); C. Mouritzen, P. Paulsen, U. Henriques (Dept. of Thoracic and Cardiovascular Surgery and Institute of Pathology, Kommunehospital, Aarhus, Denmark); N. Konietzko, W. Maassen, W. Hartung, W. Wierich (Ruhrland Clinic, Essen-Heidhausen, and Pathology Institute, Ruhr-University, Bochum, FRG); P. Oehl (Innere Klinik und Poliklinik Tumorforschung, Essen, FRG); J. Vogt-Moykopf, H. Toomes, W. Hofmann (Rohrbach Hospital, Clinic for Thoracic Medicine and Pathology Institute, Heidelberg, FRG); F. Krause, R. Rios, R. Spanel (Klinik Löwenstein, Löwenstein, and Pathology Institute, Ulm, FRG); J. Orel, B. Hrabar, D. Ferluga, T. Rott (University Medical Center, Thoracic Surgery and Pathology, Ljubljana, Yugoslavia); H. A. Rostad, J. R. Vale, P. Lexow (Rikshospital, Oslo, Norway); S. Hagen, S. Birkeland (Ulleval Hospital, Oslo, Norway); T. Harbitz, R. Nissen-Meyer (Aker Hospital, Oslo, Norway); E. Aspevik, H. Engedal, A. Mykin (Haukeland Hospital, Bergen, Norway); V. O. Björk, L. Rodriguez, K. Böök, J. Willems (Karolinska Sjukhuset, Thoracic Surgical Clinic and Pathology Department, Stockholm, Sweden); E. Grädel, J. Hasse, P. Dalquen (Kantonsspital, Dept of Surgery, Div. of Cardiac & Thoracic Surgery & Pathology Institute, Basel, Switzerland); L. Eckmann, K. Hänni, K. Zimmermann (Tiefenauspital Surg. Clinic, Univ. of Bern, Switzerland); B. Nachbur, H. U. Würsten, H. Cottier, A. Zimmermann (Inselspital Dept. of Thoracic and Cardiovascular Surg. and Pathology Institute, Bern, Switzerland); W. Maurer, M. Kaufmann (Bürgerspital, Surgical Department, Solothurn, Switzerland); H. Denck, E. Zwintz, St. Wuketich (Krankenhaus der Stadt Wien-Lainz, I. Chir. Dept., and Path. Inst., Vienna, Austria); N. Pridun, H. Hackl (Pulmonologisches Zentrum der Stadt Wien, and Path. Inst., Vienna, Austria); E. Moritz, W. Schlick, H. Holzner (II. Chir. University Clinic and Path. Inst., Vienna, Austria); K. Karrer (Institute for Cancer Research, Vienna, Austria); R. G. Crispen (ITR-Biomedical Research, University of Illinois, Chicago, USA); D. S. Freestone, R. Bomford, M. T. Scott, T. Priestman, L. Toy (The Wellcome Research Laboratories, Beckenham, England)** Present address: Cancer Unit, World Health Organization, Geneva, Switzerland Offprint requests to: K. Stanley, Ludwig Institute for Cancer Research, Inselspital, CH-3010 Bern, SwitzerlandLudwig Lung Cancer Study Group:     

Growth Curve and Distribution of Rous Sarcoma Virus (Bryan) in Japanese Quail

On primary infection with the Bryan strain of Rous sarcoma virus (RSV), the growth curve of the virus in the brain of Japanese quail was similar to that observed in chicks and turkey poults. Infectious virus disappeared from the brain after inoculation. After an eclipse period during which no virus was detectable, infectious virus began to appear at 2 days and reached maximal titers in the brain samples at 7 days after inoculation. When Japanese quail were infected intracerebrally with RSV, relatively high titers of virus were recovered from brain tissue but not from liver, lung, kidney, or blood of moribund birds. Only tumors produced in the wing web of quail infected subcutaneously yielded high titers of virus. Other tissues yielded no virus, even though wing web tumors appeared as early as in chicks similarly infected. RSV could be propagated in the wing web of quail for at least 14 passages without any loss of infectivity. On the other hand, serial passage in quail brain resulted in a progressive loss of infectivity until virus was completely lost.     

Signalling by protein kinase C isoforms in the heart

Understanding transmembrane signalling process is one of the major challenge of the decade. In most tissues, since Fisher and Krebs's discovery in the 1950's, protein phosphorylation has been widely recognized as a key event of this cellular function. Indeed, binding of hormones or neurotransmitters to specific membrane receptors leads to the generation of cytosoluble second messengers which in turn activate a specific protein kinase. Numerous protein kinases have been so far identified and roughly classified into two groups, namely serine/threonine and tyrosine kinases on the basis of the target amino acid although some more recently discovered kinases like MEK (or MAP kinase kinase) phosphorylate both serine and tyrosine residues.Protein kinase C is a serine/threonine kinase that was first described by Takai et al. [1] as a Ca- and phospholipid-dependent protein kinase. Later on, Kuo et al. [2] found that PKC was expressed in most tissues including the heart. The field of investigation became more complicated when it was found that the kinase is not a single molecular entity and that several isoforms exist. At present, 12 PKC isoforms and other PKC-related kinases [3] were identified in mammalian tissues. These are classified into three groups. (1) the Ca-activated -, -,and -PKCs which display a Ca-binding site (C2); (2) the Ca-insensitive -, -, -, -, and -PKCs. The kinases that belong to both of these groups display two cystein-rich domains (C1) which bind phorbol esters (for recent review on PKC structure, see [4]). (3) The third group was named atypical PKCs and include , , and -PKCs that lack both the C2 and one cystein-rich domain. Consequently, these isoforms are Ca-insensitive and cannot be activated by phorbol esters [5]. In the heart. evidence that multiple PKC isoforms exist was first provided by Kosaka et al. [6] who identified by chromatography at least two PKC-related isoenzymes. Numerous studies were thus devoted to the biochemical characterization of these isoenzymes (see [7] for review on cardiac PKCs) as well as to the identification of their substrates.This overview aims at updating the present knowledge on the expression, activation and functions of PKC isoforms in cardiac cells. (Mol Cell Biochem 157: 65–72, 1996)