On the Mechanism of Action of Colisan

Bergmann, Felix; Chaimovitz, M.; Leon, Shalom A.; Preiss, B.

doi:10.1111/j.1476-5381.1962.tb01410.x

British Journal of Pharmacology and Chemotherapy

1962

DOI: 10.1111/j.1476-5381.1962.tb01410.x

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On the Mechanism of Action of Colisan

Felix Bergmann¹,

M. Chaimovitz²,

Shalom A. Leon³

et al.

Abstract: Purified Colisan produces instantaneous lysis of paramecia and amoebae, and blebbing of paramecia, rat mast cells and ascites tumour cells. Colisan liberates histamine from mast cells. It also suppresses competitively the bradykinin-provoked contraction of the guinea-pig ileum. Most of these effects are not shared by staphylococcus-haemolysin. The results suggest a rapid change of the permeability of the cell membrane as the mechanism of all the diversified biological actions of Colisan.

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Cited by 3 publications

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Properties and biological activity of a new peptide antibiotic (Colisan)

Leon

Bergmann

1968

Biotech & Bioengineering

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Colisan has the formula Lys3Va14Leu311eTyr and a molecular weight of approximately 1500. The peptide is highly resistant to hydrolysis by proteolytic enzymes (pepsin and trypsin). The t-amino groups of lysine are indispensable for biological activity, since either deamination or acetylation completely inactivates Colisan. A comparative study with basic peptides like polylysine demonstrated their similarity of action, on one hand, and an antagonistic effect to Colisan, on the other. The fast action of the antibiotic and the specific effect on the cell membranes of many different biological systems (Entameba, Paramecium, erythrocytes, smooth muscle, and others) support the hypothesis that the primary damage occurs in the membrane with consequent alteration of permeability. The leakage of intracellular material (histamine) from mast cells after application of Colisan is in accord with this hypothesis. The results strongly suggest that the biological activity of the peptide is based essentially, but not exclusively, on its basic character.

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Properties and biological activity of a new peptide antibiotic (Colisan)

Leon

Bergmann

1968

Biotech & Bioengineering

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Dual Action of Nitroparaffins on the Guinea‐pig Ileum

Bergmann¹,

Chaimovitz²,

Wind³

1962

British Journal of Pharmacology and Chemotherapy

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Nitroparaffins act on the guinea-pig ileum by several mechanisms. They produce contraction partly by ganglionic stimulation and partly by direct liberation of transmitter from the nerve endings. They also inhibit the response to acetylcholine and nicotine, but interfere less with the action of histamine, serotonin or bradykinin. The two opposite effects of the nitro compounds are independent of each other. Within the homologous series of normal nitroparaffins, the excitatory action diminishes and the inhibitory effect increases with the lengthening of the carbon chain.The mechanism of drug effects on smooth muscle organs represents a difficult problem due to the complexity of the reacting system involved and the many sites available for interaction. Thus, excitation or inhibition may take place not only at any part of the nervous system present in the wall of such organs, especially at the ganglion cells, but also at the neuromuscular junction or on the smooth muscle cell itself. In many instances a drug may attack at several sites, but the dosage required for the different actions is not identical. For example, morphine depresses the response to drugs which stimulate nervous structures in the intestinal wall causing release of acetylcholine (Schaumann, 1955(Schaumann, , 1956), but higher doses of the alkaloid also counteract direct stimulation of the smooth muscle fibres (Lewis, 1960). Morphine is thus a representative of agents which produce the same type of effect-excitation or inhibition-at more than a single site. In such cases, it is a laborious task to separate the components of the overall effect.Almost all agents, active on smooth muscle organs, are either bases or acids. In the present study we have selected a third type, embodying a strongly polar but uncharged group at the end of a non-polar chain, viz., the nitroparaffins. It is well known that these compounds range among the aliphatic substances with the highest dipole moments (Groves & Sugden, 1935). It was found that the members of this series may act on the intestine in two or more different ways, the main action shifting within the homologous series from excitation to inhibition. As will be shown in this study, the combination of effects exerted by a given nitroparaffin can be resolved into excitatory and inhibitory components. Experiments with nitrobenzene are also included, since its actions are qualitatively similar to those of the aliphatic nitro compounds.

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Polylysine as histamine releaser

Bergmann¹

1968

Journal of Pharmacy and Pharmacology

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On the Mechanism of Action of Colisan

Cited by 3 publications

References 11 publications

Properties and biological activity of a new peptide antibiotic (Colisan)

Properties and biological activity of a new peptide antibiotic (Colisan)

Dual Action of Nitroparaffins on the Guinea‐pig Ileum

Polylysine as histamine releaser

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