In vitro and in vivo effect of immunoglobulin G on the integrity of bacterial membranes

Infection ◽  
1985 ◽  
Vol 13 (S2) ◽  
pp. S185-S193 ◽  
Author(s):  
A. Dalhoff
Keyword(s):  
Immunoglobulin G ◽  
Bacterial Membranes

Mechanism of Action of the Antitumour Effect of K18

1989 ◽  
Vol 17 (2) ◽  
pp. 132-140
Author(s):  
T. Fujii ◽  
K. Niimura ◽  
T. Furusho ◽  
N. Sugita ◽  
M. Oikawa ◽  
...  
Keyword(s):  
Nude Mice ◽  
Immunoglobulin G ◽  
Antitumour Activity ◽  
Inhibitory Effect ◽  
Human Lung Cancer ◽  
Covalently Bonded ◽  
Human Lung Cancer Cells ◽  
Rpmi 8226

K18 is an anticancer drug for oral administration comprising about five molecules of melphalan, an alkylating drug, covalently bonded to human immunoglobulin G. This study measured the in vitro antitumour activity of K18, melphalan and immunoglobulin G on human myeloma cells (RPMI-8226) and the in vivo antitumour effects of K18 and melphalan in BALB/c nude mice bearing human lung cancer cells (LC-10). The relative tumour-inhibitory effect, in vitro, was found to be: immunoglobulin G <K18 <melphalan. This activity of K18 was about half the theoretical value indicating that melphalan molecules are not released easily from the conjugate. K18 showed strong antitumour activity in vivo which continued after stopping administration. On the other hand, the effects of melphalan did not continue after administration was stopped. The distribution of [125I]K18 and [14C]melphalan was examined in BALB/c nude mice 14 days after implantation of LC-10 cells. Radioactivity levels in the major organs showed a transient rapid increase followed by a gradual decline. In tumours, [14C]melphalan levels increased transiently and then decreased, whereas [125I]K18 levels persisted following intravenous administration.

In vivo diffusion of immunoglobulin G in muscle: effects of binding, solute exclusion, and lymphatic removal

1997 ◽  
Vol 273 (6) ◽  
pp. H2783-H2793 ◽  
Author(s):  
Michael F. Flessner ◽  
Joanne Lofthouse ◽  
El Rasheid Zakaria
Keyword(s):  
Abdominal Wall ◽  
Immunoglobulin G ◽  
Diffusion Profile ◽  
Lymph Flow ◽  
Time Dependent ◽  
Concentration Profiles ◽  
Isotonic Solution ◽  
Cross Sectional

Previously, we demonstrated that immunoglobulin G (IgG), dissolved in an isotonic solution in the peritoneal cavity, transported rapidly into the abdominal wall when the intraperitoneal (ip) pressure was >2 cmH2O. We hypothesized that this was chiefly caused by convection and that diffusion of IgG was negligible. To investigate the role of diffusion, we dialyzed rats with no pressure gradient across the abdominal wall muscle for 2 or 6 h with an ip isotonic solution containing125I-labeled IgG. At the end of the experiment, the animal was euthanized and frozen and abdominal wall tissue was processed to produce cross-sectional autoradiograms. Quantitative densitometric analysis resulted in IgG concentration profiles with far lower magnitude than profiles from experiments in which convection dominated. In other in vivo experiments, we determined the lymph flow rate to be 0.8 × 10−4ml ⋅ min−1 ⋅ g−1and the fraction of extravascular tissue (θs) available to the IgG to be 0.041 ± 0.001. An in vitro binding assay was used to determine the time-dependent, nonsaturable binding constant: 0.0065 min−1 × duration of exposure. A non-steady-state diffusion model that included effects of θs, time-dependent binding, and lymph flow was fitted to the diffusion profile data, and the IgG diffusivity within the tissue void was estimated to be 2 × 10−7cm2/s, a value much higher than that published by other groups. We also demonstrate from our previous data that convection of IgG through tissue dominates over diffusion at ip pressures >2 cmH2O, but diffusion may not be negligible. Furthermore, nonsaturable binding must be accounted for in the interpretation of tissue protein concentration profiles.

scholarly journals Non-Lytic Antibacterial Peptides That Translocate Through Bacterial Membranes to Act on Intracellular Targets

2019 ◽  
Vol 20 (19) ◽  
pp. 4877 ◽  
Author(s):  
Marlon H. Cardoso ◽  
Beatriz T. Meneguetti ◽  
Bruna O. Costa ◽  
Danieli F. Buccini ◽  
Karen G. N. Oshiro ◽  
...  
Keyword(s):  
Cell Wall ◽  
Protein Synthesis ◽  
Pathogenic Bacteria ◽  
Biological Properties ◽  
Antibacterial Peptides ◽  
Bacterial Cells ◽  
Bacterial Membranes ◽  
Intracellular Targets

The advent of multidrug resistance among pathogenic bacteria has attracted great attention worldwide. As a response to this growing challenge, diverse studies have focused on the development of novel anti-infective therapies, including antimicrobial peptides (AMPs). The biological properties of this class of antimicrobials have been thoroughly investigated, and membranolytic activities are the most reported mechanisms by which AMPs kill bacteria. Nevertheless, an increasing number of works have pointed to a different direction, in which AMPs are seen to be capable of displaying non-lytic modes of action by internalizing bacterial cells. In this context, this review focused on the description of the in vitro and in vivo antibacterial and antibiofilm activities of non-lytic AMPs, including indolicidin, buforin II PR-39, bactenecins, apidaecin, and drosocin, also shedding light on how AMPs interact with and further translocate through bacterial membranes to act on intracellular targets, including DNA, RNA, cell wall and protein synthesis.

scholarly journals Thermo-responsive triple-function nanotransporter for efficient chemo-photothermal therapy of multidrug-resistant bacterial infection

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Guangchao Qing ◽  
Xianxian Zhao ◽  
Ningqiang Gong ◽  
Jing Chen ◽  
Xianlei Li ◽  
...  
Keyword(s):  
Near Infrared ◽  
Multidrug Resistant ◽  
Resistant Bacteria ◽  
Limited Effect ◽  
Bacterial Membranes ◽  
Change Mechanism ◽  
Drug Resistant Bacteria ◽  
New Strategies

Abstract New strategies with high antimicrobial efficacy against multidrug-resistant bacteria are urgently desired. Herein, we describe a smart triple-functional nanostructure, namely TRIDENT (Thermo-Responsive-Inspired Drug-Delivery Nano-Transporter), for reliable bacterial eradication. The robust antibacterial effectiveness is attributed to the integrated fluorescence monitoring and synergistic chemo-photothermal killing. We notice that temperature rises generated by near-infrared irradiation did not only melt the nanotransporter via a phase change mechanism, but also irreversibly damaged bacterial membranes to facilitate imipenem permeation, thus interfering with cell wall biosynthesis and eventually leading to rapid bacterial death. Both in vitro and in vivo evidence demonstrate that even low doses of imipenem-encapsulated TRIDENT could eradicate clinical methicillin-resistant Staphylococcus aureus, whereas imipenem alone had limited effect. Due to rapid recovery of infected sites and good biosafety we envision a universal antimicrobial platform to fight against multidrug-resistant or extremely drug-resistant bacteria.

scholarly journals Anti-CD20 Immunoglobulin G Radiolabeling with a 99mTc-Tricarbonyl Core: In Vitro and In Vivo Evaluations

PLoS ONE ◽  
2015 ◽  
Vol 10 (10) ◽  
pp. e0139835 ◽  
Author(s):  
Hélène Carpenet ◽  
Armelle Cuvillier ◽  
Jacques Monteil ◽  
Isabelle Quelven
Keyword(s):  
Immunoglobulin G ◽  
Anti Cd20

scholarly journals Antiimmunosuppressive action of 3d-metal gluconates in experimental immunodeficiency

2018 ◽  
Vol 99 (2) ◽  
pp. 255-259 ◽  
Author(s):  
O A Knyazeva ◽  
S I Urazaeva ◽  
I G Konkina ◽  
L M Saptarova ◽  
L M Gazdalieva ◽  
...  
Keyword(s):  
Immunoglobulin G ◽  
Functional Activity ◽  
Test System ◽  
Classical Pathway ◽  
Zinc Gluconate ◽  
Sheep Erythrocytes ◽  
Immunodeficient Mice ◽  
Before And After

Aim. Evaluation of the effect of 3d-metal gluconates on complement-fixing function of immunoglobulin G and functional activity of complement. Methods. The study was conducted in vivo on 2.5-3 month-old white laboratory mice weighing 25-28 g with secondary immunodeficiency, which was induced by a single intraperitoneal injection of cyclophosphamide, as well as in vitro in a test system using sensitized sheep erythrocytes. Immunological studies were performed in intact animals, and before and after the administration of Mn, Co, Cu, and Zn gluconates to mice with induced immunodeficiency. The content of immunoglobulin G and its complexes with subcomponent of the complement first component C1q was determined in serum by ELISA using specific monoclonal antibodies. Results. Two-week oral administration of 3d-metal gluconates (Mn, Co, Cu, Zn) in a dose of 1/10 LD50 to immunodeficient mice was shown to cause a significant increase in the level of immunoglobulin G and its complexes with C1q. The greatest increase in concentration was observed with the introduction of zinc gluconate. Also by means of sensitized sheep erythrocytes in vitro, cobalt and, to a lesser extent, manganese gluconates were shown to increase the functional activity of C1q. Conclusion. 3d-metal gluconates (Mn, Co, Cu, Zn) demonstrate immunocorrecting properties: increase the content of immunoglobulin G and its complexes with C1q, significantly decreasing as a result of cyclophosphamide effect; cobalt and manganese gluconates have a stimulating effect on the functional activity of complement by its classical pathway, which indicates different mechanisms of immunocorrection action of studied metal gluconates and requires further studies.

A new anti-idiotype antibody capable of binding rituximab on the surface of lymphoma cells

Blood ◽  
2004 ◽  
Vol 104 (8) ◽  
pp. 2540-2542 ◽  
Author(s):  
Mark S. Cragg ◽  
Mike B. Bayne ◽  
Alison L. Tutt ◽  
Ruth R. French ◽  
Stephen Beers ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Cell Surface ◽  
Immunoglobulin G ◽  
Human Immunoglobulin ◽  
Lymphoma Cells ◽  
Fine Specificity ◽  
High Affinity ◽  
Anti Cd20

Abstract The chimeric anti-CD20 monoclonal antibody (mAb), rituximab, is an established part of the management of many non-Hodgkin lymphomas. The in vivo action of rituximab remains elusive, and this partially reflects a lack of highly specific reagents to detect rituximab binding at the cell surface. Here we report a new high-affinity mAb (MB2A4) with fine specificity for the idiotype of rituximab. It is able to detect rituximab in vitro, in the presence of high levels of human immunoglobulin G (IgG), in the serum of patients receiving rituximab therapy, and, surprisingly, when rituximab is bound to CD20 on the cell surface. We propose that the anti–idiotype (Id) binds to rituximab molecules bound univalently at the cell surface, facilitated by the relatively high off-rate of rituximab. This reagent provides new insights into the binding of rituximab at the cell surface and demonstrates a mode of binding that could be exploited for the surface detection of other mAbs with clinical and biologic applications.

Assembly of three major subclasses of mouse immunoglobulin G: a theoretical model for covalent assembly in vivo

1976 ◽  
Vol 54 (8) ◽  
pp. 688-698 ◽  
Author(s):  
J. R. Percy ◽  
M. E. Percy ◽  
R. Baumal
Keyword(s):  
Cell Lines ◽  
Immunoglobulin G ◽  
Mean Value ◽  
Individual Values ◽  
In Vitro Assembly ◽  
The Mean ◽  
The Individual ◽  
Mouse Myeloma

A mathematical model, based on second-order reaction kinetics, has been used to describe the covalent assembly of immunoglobulin G (IgG) in vitro from its heavy (H) and light (L) chains (Percy, M. E., Baumal, R., Dorrington, K. J. &Percy, J. (1976) Can. J. Biochem. 54, 675–687). In the present paper, the same model has now been applied to the steady-state assembly of IgG in vivo. This mathematical approach permits a quantitative comparison of the pathways of covalent assembly used by given immunoglobulins in vivo and in vitro. The assumptions in the model are: the species L, H, HL, HH, HHL and LHHL belong to a common pool; incompleted IgG intermediates may freely assemble to form HL, HH, HHL and LHHL; the reaction rate for covalent linkage between any two reacting species is proportional to the products of the number densities of the reactants and to a parameter P which takes the value PHH if the reaction joins two H chains, and PHL if it joins an H and L chain. In vivo values of PHH/PHL were determined for the 18 mouse myeloma tumours and cell lines studied by Baumal et al. (Baumal, R., Potter, M. &Scharff, M. (1971) J. Exp. Med. 134, 1316–1334). From these analyses, we have arrived at the following conclusions: (1) the three major IgG subclasses have distinctive values of PHH/PHL (mean value 53 for IgG1, 12 for IgG2a and 2.8 for IgG2b); (2) for IgGs of the same subclass, the values of PHH/PHL are similar; (3) the mean in vivo values of PHH/PHL are very close to those determined from in vitro assembly experiments. Finally, the individual values of PHH/PHL have been used to simulate pulse-chase experiments in the various tumours and cell lines. Considering the sources and magnitude of experimental error, the theoretical pathways of assembly agree with those determined qualitatively from the pulse-chase experiments.

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