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Biomedical subjects

J Bergmann

Publications and source records attributed to J Bergmann.

At least 73 records · Page 4Linked to original sources
PubMed1975

[Studies on the mechanism of action of peptide attacking smooth muscle. II. Differentiation of biologic activity of tachykinins in affinity and intrinsic efficacy].

Under the condition of receptor blockade produced by continuous presence of an agonist in the organ bath, it was attempted to determine the dissociation constants for C-terminal partial sequences of the substance P at an isolated guinea pig ileum, by analogy with the method involving irreversible antagonists, and to compare them with the biological activity at the guinea pig ileum and the rat colon (ED50 values). Differentiation of the biological activity at the guinea pig ileum into affinity and "intrinsic efficacy" allows one to explain quantitative differences in determining the biological value on both isolated organs, and to reveal the contribution of the individual amino acids to affinity and "intrinsic efficacy".

Amino Acids↗
PubMed1975

[Studies on the mechanism of action of peptides attacking smooth muscles. III. The effect of N-azylation on the activity of C-terminal partial sequences of eledoisin, physalaemin and substance P on the guinea pig ileum].

C-terminal pentapeptides of eledoisin, physalaemin, and the substance P, when N-substituted with acetyl, halogenacetyl and other acyl residues, are increased in their action more than 100fold, reaching the activity of acylated hexa- and heptapeptides. The effect found with a number of compounds is interpreted as the influence of predominantly hydrophobic substituents upon the peptide sequence essential for the action. Polar groups in the acylic residue seem to cause additional increase in action.

Animals↗
PubMedDate not supplied

Effect of ALP analogs on inositol trisphosphate formation in H184 mammary epithelial cells before and after transfection with v-erb B oncogene.

The influence of cytostatically active alkyllysophospholipid analogs with different chemical structure on IP3 (inositol-1,4,5-trisphosphate) formation and intracellular Ca++ concentration was studied in human mammary epithelial cells before and after transfection with v-erb B oncogene DNA. Transformed cells showed an increased IP3 formation compared with normal cells. In the presence of ALP (alkyllysophospholipid) analogs IP3 formation is inhibited more strongly in transformed cells than in normal cells, dependent on the structure of ALP analogs. Furthermore, these compounds increased [Ca++]i (intracellular Ca++ concentration) in transformed cells much more strongly than in normal cells. From these results, obtained in pursuit of an oncogene-related cancer treatment, it follows that ALP analogs may inhibit processes in signal transduction in cells more strongly after transfection with a defined oncogene than before.

Alpharetrovirus↗