Physalaemin: an amphibian tachykinin in human lung small-cell carcinoma.

Abstract

Immunoreactivity to the amphibian peptide physalaemin was characterized from extracts of a human lung small-cell carcinoma by immunological, chemical, and pharmacological means. Tumor-related peptide cross-reacted with three antiserums to physalaemin to yield 1.1 to 1.6 nanomoles per gram of tissue. Physalaemin and tumor peptide had similar retention times on high-performance liquid chromatography after chemical and enzymic modifications that included pH changes, oxone oxidation, use of a hydrophilic ion-pairing reagent, and digestion with trypsin and pyroglutamate aminopeptidase. Both physalaemin and the tumor peptide produced a contractile response of isolated guinea pig ileum at threshold concentrations of approximately 100 to 150 picograms per milliliter. These data suggest that small-cell carcinoma of the lung contains a physalaemin-like peptide that has structural and biological homology to its amphibian counterpart.

• Authors: L H Lazarus, R P DiAugustine, G D Jahnke, O Hernandez
• Journal: Science (New York, N.Y.) (Science) Vol. 219 Issue 4580 Pg. 79-81 (Jan 07 1983) ISSN: 0036-8075 [Print] United States
• PMID: 6294828 (Publication Type: Journal Article)

Chemical References

• Immune Sera
• Kinins
• Peptides
• Tachykinins
• Physalaemin

Topics

• Carcinoma, Small Cell (metabolism)
• Chromatography, High Pressure Liquid
• Cross Reactions
• Humans
• Immune Sera
• Kinins (metabolism)
• Lung Neoplasms (metabolism)
• Oxidation-Reduction
• Peptides (metabolism)
• Physalaemin (metabolism)
• Tachykinins